Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications
Identifieur interne : 000275 ( Pmc/Corpus ); précédent : 000274; suivant : 000276Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications
Auteurs : E. I. Finkina ; D. N. Melnikova ; I. V. Bogdanov ; T. V. OvchinnikovaSource :
- Acta Naturae [ 2075-8251 ] ; 2016.
Abstract
Among a variety of molecular factors of the plant innate immune system, small proteins that transfer lipids and exhibit a broad spectrum of biological activities are of particular interest. These are lipid transfer proteins (LTPs). LTPs are interesting to researchers for three main features. The first feature is the ability of plant LTPs to bind and transfer lipids, whereby these proteins got their name and were combined into one class. The second feature is that LTPs are defense proteins that are components of plant innate immunity. The third feature is that LTPs constitute one of the most clinically important classes of plant allergens. In this review, we summarize the available data on the plant LTP structure, biological properties, diversity of functions, mechanisms of action, and practical applications, emphasizing their role in plant physiology and their significance in human life.
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PubMed: 27437139
PubMed Central: 4947988
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<author><name sortKey="Finkina, E I" sort="Finkina, E I" uniqKey="Finkina E" first="E. I." last="Finkina">E. I. Finkina</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<author><name sortKey="Melnikova, D N" sort="Melnikova, D N" uniqKey="Melnikova D" first="D. N." last="Melnikova">D. N. Melnikova</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<author><name sortKey="Bogdanov, I V" sort="Bogdanov, I V" uniqKey="Bogdanov I" first="I. V." last="Bogdanov">I. V. Bogdanov</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<author><name sortKey="Ovchinnikova, T V" sort="Ovchinnikova, T V" uniqKey="Ovchinnikova T" first="T. V." last="Ovchinnikova">T. V. Ovchinnikova</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications</title>
<author><name sortKey="Finkina, E I" sort="Finkina, E I" uniqKey="Finkina E" first="E. I." last="Finkina">E. I. Finkina</name>
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<author><name sortKey="Melnikova, D N" sort="Melnikova, D N" uniqKey="Melnikova D" first="D. N." last="Melnikova">D. N. Melnikova</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<author><name sortKey="Bogdanov, I V" sort="Bogdanov, I V" uniqKey="Bogdanov I" first="I. V." last="Bogdanov">I. V. Bogdanov</name>
<affiliation><nlm:aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</nlm:aff>
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<author><name sortKey="Ovchinnikova, T V" sort="Ovchinnikova, T V" uniqKey="Ovchinnikova T" first="T. V." last="Ovchinnikova">T. V. Ovchinnikova</name>
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<series><title level="j">Acta Naturae</title>
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<front><div type="abstract" xml:lang="en"><p>Among a variety of molecular factors of the plant innate immune system, small
proteins that transfer lipids and exhibit a broad spectrum of biological
activities are of particular interest. These are lipid transfer proteins
(LTPs). LTPs are interesting to researchers for three main features. The first
feature is the ability of plant LTPs to bind and transfer lipids, whereby these
proteins got their name and were combined into one class. The second feature is
that LTPs are defense proteins that are components of plant innate immunity.
The third feature is that LTPs constitute one of the most clinically important
classes of plant allergens. In this review, we summarize the available data on
the plant LTP structure, biological properties, diversity of functions,
mechanisms of action, and practical applications, emphasizing their role in
plant physiology and their significance in human life.
</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Acta Naturae</journal-id>
<journal-id journal-id-type="iso-abbrev">Acta Naturae</journal-id>
<journal-id journal-id-type="publisher-id">ActaNaturae</journal-id>
<journal-title-group><journal-title>Acta Naturae</journal-title>
</journal-title-group>
<issn pub-type="ppub">2075-8251</issn>
<publisher><publisher-name>A.I. Gordeyev</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27437139</article-id>
<article-id pub-id-type="pmc">4947988</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
<subj-group><subject>Molecular Biology</subject>
</subj-group>
</subj-group>
</article-categories>
<title-group><article-title>Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Finkina</surname>
<given-names>E. I.</given-names>
</name>
<xref ref-type="aff" rid="AF1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Melnikova</surname>
<given-names>D. N.</given-names>
</name>
<xref ref-type="aff" rid="AF1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Bogdanov</surname>
<given-names>I. V.</given-names>
</name>
<xref ref-type="aff" rid="AF1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ovchinnikova</surname>
<given-names>T. V.</given-names>
</name>
<xref ref-type="aff" rid="AF1"></xref>
<email>ovch@ibch.ru</email>
</contrib>
</contrib-group>
<aff id="AF1">Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Miklukho-Maklaya Str. 16/10, 117997 , Moscow, Russia</aff>
<pub-date pub-type="ppub"><season>Apr-Jun</season>
<year>2016</year>
</pub-date>
<volume>8</volume>
<issue>2</issue>
<fpage>47</fpage>
<lpage>61</lpage>
<history><date date-type="received"><day>05</day>
<month>8</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement>Copyright ® 2016 Park-media Ltd.</copyright-statement>
<copyright-year>2016</copyright-year>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.0/"><license-p>This is an open-access article distributed under the terms of the
Creative Commons Attribution License, which permits unrestricted use,
distribution, and reproduction in any medium, provided the original work is
properly cited.
</license-p>
</license>
</permissions>
<abstract><p>Among a variety of molecular factors of the plant innate immune system, small
proteins that transfer lipids and exhibit a broad spectrum of biological
activities are of particular interest. These are lipid transfer proteins
(LTPs). LTPs are interesting to researchers for three main features. The first
feature is the ability of plant LTPs to bind and transfer lipids, whereby these
proteins got their name and were combined into one class. The second feature is
that LTPs are defense proteins that are components of plant innate immunity.
The third feature is that LTPs constitute one of the most clinically important
classes of plant allergens. In this review, we summarize the available data on
the plant LTP structure, biological properties, diversity of functions,
mechanisms of action, and practical applications, emphasizing their role in
plant physiology and their significance in human life.
</p>
</abstract>
<kwd-group kwd-group-type="author"><kwd>allergens</kwd>
<kwd>antimicrobial activity</kwd>
<kwd>cross reactivity</kwd>
<kwd>plant lipid transfer proteins</kwd>
<kwd>lipid binding and transfer</kwd>
<kwd>plant defense</kwd>
</kwd-group>
</article-meta>
</front>
<body><sec><title>INTRODUCTION</title>
<p>Lipids and their derivatives are involved in a variety of processes, including
membrane biogenesis, cell differentiation, intercellular and intracellular
signaling, and formation of water-repellent and thermal insulation covers
protecting plants from adverse environmental factors; they also function as a
storage and source of energy. The proteins involved in the intra- and
extracellular transport of lipids play an important role in the lipid
metabolism of pro- and eukaryotic cells. In plants, several classes of proteins
capable of binding and transferring lipids and their derivatives have been
identified: acyl-CoA-binding proteins; glycolipid-transfer proteins; sterol
carrier proteins; homologues of the major pollen allergen of birch
(<italic>Betula verrucosa</italic>
), which is listed in the IUIS allergen
database under the name Bet v 1; fatty acid binding proteins; puroindolines;
and lipid transfer proteins.
</p>
<p>Comparison of the amino acid sequences of the proteins of the listed classes
demonstrated no significant structural homology among them. These proteins have
an intra- or extracellular localization, relatively low molecular weight
(7–30 kDa), a high isoelectric point (pI ~ 9–11), and a compact
structure stabilized by disulfide bonds. A common feature of the spatial
structure of lipid transfer proteins is a hydrophobic cavity accommodating a
ligand-binding site. These proteins reversibly bind lipids and deliver them to
their destination. Proteins of some classes have highly specific ligands, while
other proteins bind and transfer a wide range of lipids.
</p>
<p>LTPs belong to the most functionally important classes of plant proteins that
bind and transfer lipids. These proteins were discovered in 1970 and were
originally named phospholipid exchange proteins [<xref rid="R1" ref-type="bibr">1</xref>
], but later they were renamed phospholipid transfer proteins
[<xref rid="R2" ref-type="bibr">2</xref>
]. Further studies showed that not only
phospholipids, but other hydrophobic molecules as well may be ligands of such
proteins, and, therefore, LTPs were given their present name –
non-specific lipid transfer proteins [<xref rid="R3" ref-type="bibr">3</xref>
].
</p>
</sec>
<sec><title>STRUCTURAL CHARACTERIZATION OF PLANT LTPS</title>
<fig id="F1" orientation="portrait" position="float"><label>Fig. 1</label>
<caption><p>Comparison of the amino acid sequences of LTP1s (A) and LTP2s (B). Conserved cysteine residues are shown
in red; amino acid residues typical of most subclass representatives are shown in blue. Disulfide bond arrangement is
denoted by brackets. The localization of 4α-helices in the rice LTP1 (PDB ID: 1RZL) [<xref rid="R5" ref-type="bibr">5</xref>
] and LTP2 (PDB ID: 1L6H) structures
[<xref rid="R10" ref-type="bibr">10</xref>
] is shown on the top of the panels. The asterisks denote the amino acid residues involved in the conformational epitopes
of Pru p 3 (GenBank:AAV40850) [<xref rid="R98" ref-type="bibr">98</xref>
].
</p>
</caption>
<graphic xlink:href="AN20758251-29-047-g001"></graphic>
</fig>
<p>On the basis of structural organization features, plant LTPs are divided into
two subclasses: LTP1s with a molecular weight of 9–10 kDa and LTP2s with
a molecular weight of about 7 kDa
(<italic><xref ref-type="table" rid="T1">Table</xref>
</italic>
). Amino acid
sequence homology among representatives of the two subclasses is less than 30%
(<italic><xref ref-type="fig" rid="F1">Fig. 1</xref>
</italic>
).
All LTPs are basic proteins (pI ~9–10). The
vast majority of LTPs contain eight conserved cysteine residues
(..C<sup>I</sup>
...C<sup>II</sup>
...C<sup>III</sup>
C<sup>IV</sup>
...
C<sup>V</sup>
XC<sup>VI</sup>
...C<sup>VII</sup>
...C<sup>VIII</sup>
..) forming
four disulfide bonds that stabilize their structure and, thereby, underlie the
resistance of LTPs to high temperatures and proteolytic enzymes. Some proteins
from this class retain their native conformation and biological activity even
after incubation at a temperature of about 100°C
[<xref rid="R4" ref-type="bibr">4</xref>
].
The LTP spatial structure is mainly composed of
α-helical regions. Hydrophobic amino acid residues in LTPs are buried
inside a molecule and are not in contact with each other, forming an internal
protein cavity comprising a potential binding site for hydrophobic and
amphiphilic molecules, such as lipids.
</p>
<table-wrap id="T1" orientation="portrait" position="float"><label>Table</label>
<caption><p>Comparative characterization of two plant LTP subclasses
</p>
</caption>
<table frame="hsides" rules="groups"><thead><tr><th rowspan="1" colspan="1">Characteristic</th>
<th rowspan="1" colspan="1">LTP1</th>
<th rowspan="1" colspan="1">LTP2</th>
</tr>
</thead>
<tbody><tr><td align="center" rowspan="1" colspan="1">MW, kDa</td>
<td align="center" rowspan="1" colspan="1">9–10</td>
<td align="center" rowspan="1" colspan="1">6-7</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Number of amino acids (a.a.)</td>
<td align="center" rowspan="1" colspan="1">90–95</td>
<td align="center" rowspan="1" colspan="1">65-70</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Conserveda. a.</td>
<td align="center" rowspan="1" colspan="1">C, G, P, R, Y(F)</td>
<td align="center" rowspan="1" colspan="1">C, Q, P, Y(F)</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">–C<sup>V</sup>
XC<sup>VI</sup>
– motif</td>
<td align="center" rowspan="1" colspan="1">X – a hydrophilic amino acid residue<break></break>
(usually N) exposed on the protein<break></break>
surface</td>
<td align="center" rowspan="1" colspan="1">X – a hydrophobic amino acid residue<break></break>
(usually F) buried inside the protein<break></break>
molecule</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Disulfide bond arrangement</td>
<td align="center" rowspan="1" colspan="1">C<sup>I</sup>
–C<sup>VI</sup>
, C<sup>II</sup>
–C<sup>III</sup>
, C<sup>IV</sup>
–C<sup>VII</sup>
,<break></break>
C<sup>V</sup>
–C<sup>VIII</sup>
</td>
<td align="center" rowspan="1" colspan="1">C<sup>I</sup>
–C<sup>V</sup>
, CII–C<sup>III</sup>
, C<sup>IV</sup>
–C<sup>VII</sup>
,<break></break>
C<sup>VI</sup>
–C<sup>VIII</sup>
</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Spatial structure</td>
<td align="center" rowspan="1" colspan="1">α-helices, a 3<sub>10</sub>
-helix fragment, and an<break></break>
unstructured C-terminal loop</td>
<td align="center" rowspan="1" colspan="1">3 α-helices and a region containing a<break></break>
single helix-turn-helix</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Hydrophobic cavity</td>
<td align="center" rowspan="1" colspan="1">A tunnel with large and small entrances<break></break>
that is formed by H1, H2, and H3 helices<break></break>
arranged parallel to each other</td>
<td align="center" rowspan="1" colspan="1">A triangular hollow box; H1 and H2<break></break>
helices are arranged parallel to each<break></break>
other; the H3 helix forms an angle of 90°<break></break>
with H2</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Sterol-binding ability</td>
<td align="center" rowspan="1" colspan="1">No</td>
<td align="center" rowspan="1" colspan="1">Yes</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Amino acid residues interacting<break></break>
with a ligand</td>
<td align="center" rowspan="1" colspan="1">Arg44 and Tyr79<break></break>
(numeration for rice LTP1)</td>
<td align="center" rowspan="1" colspan="1">Phe36, Tyr45, and Tyr48 (numeration for<break></break>
rice LTP2)</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Signal peptide, a.a.</td>
<td align="center" rowspan="1" colspan="1">21–27</td>
<td align="center" rowspan="1" colspan="1">27–35</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Localization</td>
<td align="center" rowspan="1" colspan="1">Cutin-coated organs (leaves, stems,<break></break>
flowers)</td>
<td align="center" rowspan="1" colspan="1">Suberin-coated organs (subterraneous<break></break>
organs)</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Potential function</td>
<td align="center" rowspan="1" colspan="1">Cutin biosynthesis</td>
<td align="center" rowspan="1" colspan="1">Suberin biosynthesis</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Activation of immune response</td>
<td align="center" rowspan="1" colspan="1">Elicitors in a complex with jasmonic acid</td>
<td align="center" rowspan="1" colspan="1">Elicitors in a complex with sterol</td>
</tr>
<tr><td align="center" rowspan="1" colspan="1">Allergens listed in IUIS</td>
<td align="center" rowspan="1" colspan="1">LTP1s of 42 plants<break></break>
(excluding iso-allergens and variants)</td>
<td align="center" rowspan="1" colspan="1">Tomato Sola l 6, celery Api g 6, peanut<break></break>
Ara h 16</td>
</tr>
</tbody>
</table>
</table-wrap>
<p>LTP1s consist of 90–95 amino acid residues and have disulfide bonds
formed in the following order: C<sup>I</sup>
–C<sup>VI</sup>
,
C<sup>II</sup>
–C<sup>III</sup>
, C<sup>IV</sup>
–C<sup>VII</sup>
,
and C<sup>V</sup>
–C<sup>VIII</sup>
(<italic><xref ref-type="fig" rid="F1">Fig. 1A</xref>
</italic>
,
<italic><xref ref-type="fig" rid="F2">Fig. 2A</xref>
</italic>
). The
fragment –C<sup>V</sup>
XC<sup>VI</sup>
– in the LTP1 structure
contains a hydrophilic amino acid (usually asparagine) whose side chain is
exposed on the surface of a molecule. The spatial structure of these proteins
consists of four α-helices, a 310-helix fragment, and an extended
unstructured C-terminal region
(<italic><xref ref-type="fig" rid="F2">Fig. 2A</xref>
</italic>
)
[<xref rid="R5" ref-type="bibr">5</xref>
, <xref rid="R6" ref-type="bibr">6</xref>
]. In
the structure of some LTP1s, e.g., proteins isolated from maize <italic>(Zea
mays</italic>
) and tobacco (<italic>Nicotiana tabacum</italic>
), the H1 and H4
helices are interrupted by proline residues into two fragments (H1a/H1b and
H4a/H4b, respectively). The LTP1 hydrophobic cavity is shaped as an elongated
tunnel formed by H1, H2, and H3 helices arranged parallel to each other. The
hydrophobic nature of the tunnel surface is determined by the side chains of
amino acid residues, including Ile, Val, Leu, and Ala; however, hydrophilic
amino acid residues (Arg, Lys, Ser) are also involved in the cavity formation
[<xref rid="R7" ref-type="bibr">7</xref>
]. The tunnel in LTP1s has two
entrances that differ in size. In most LTP1s, a basic residue – Arg44
– (position numbering relative to LTP1 of rice (<italic>Oryza
sativa</italic>
)) is located near the larger entrance and is involved in the
interaction with polar lipid heads [<xref rid="R8" ref-type="bibr">8</xref>
].
In rice LTP1, this interaction involves another basic residue, Lys35. In
addition to cysteine residues, most LTP1s contain conserved glycine and proline
residues that enable interhelical turns; two tyrosine residues, one of which is
located in the N-terminal region, outside of the α-helix, and a second
located in the C-terminal region, near the larger entrance to the hydrophobic
tunnel and involved in the interaction with hydrophobic ligands
[<xref rid="R7" ref-type="bibr">7</xref>
, <xref rid="R9" ref-type="bibr">9</xref>
].
</p>
<fig id="F2" orientation="portrait" position="float"><label>Fig. 2</label>
<caption><p>The spatial structures of (A) LTP1 (PDB ID: 1RZL) and (B) LTB2 (PDB ID: 1L6H) from rice in a ribbon representation.
Identification numbers of α-helices (H1–H4) are specified. Hydrophobic amino acid residues are shown in purple;
residues interacting with lipid ligands are shown in red
[<xref rid="R5" ref-type="bibr">5</xref>
, <xref rid="R10" ref-type="bibr">10</xref>
];
disulfide bonds are marked in yellow; the central residue
in the –C<sup>VX</sup>
C<sup>VI</sup>
– fragment, directed either outward or inward the protein molecule, is shown in green.
</p>
</caption>
<graphic xlink:href="AN20758251-29-047-g002"></graphic>
</fig>
<p>LTP2s consisting of 65–70 amino acid residues have been less studied than
LTP1s. The –C<sup>VX</sup>
C<sup>VI</sup>
– fragment of LTP2s usually
contains phenylalanine as the central residue, which points inward the
molecule. LTP2s have a different organization of disulfide bonds:
C<sup>I</sup>
–C<sup>V</sup>
, C<sup>II</sup>
–C<sup>III</sup>
,
C<sup>IV</sup>
–C<sup>VII</sup>
, C<sup>VI</sup>
–C<sup>VIII</sup>
(<italic><xref ref-type="fig" rid="F1">Fig. 1B</xref>
</italic>
,
<italic><xref ref-type="fig" rid="F2">Fig. 2B</xref>
</italic>
spatial structure of proteins of this subclass includes three α-helices
and a region containing single helical coils
(<italic><xref ref-type="fig" rid="F2">Fig. 2B</xref>
</italic>
). In the
LTP2 structure, the H1 and H2 helices are arranged parallel to each other and
the H3 helix forms an angle of 90° with respect to H2. The shape of the
LTP2 hydrophobic cavity resembles a triangular hollow box, with side chains of
the Ala, Ile, Leu, Phe, and Val residues situated within. The volume of the
triangular LTP2 box is smaller than that of the LTP1 hydrophobic cavity, but
pronounced flexibility of the former allows proteins of this subclass to bind
large ligands with a rigid structure, such as sterols
[<xref rid="R10" ref-type="bibr">10</xref>
-<xref rid="R12" ref-type="bibr">12</xref>
].
Side chains of Phe39, Tyr45, and Tyr48 (numbering relative to rice LTP2) are rotated inside
the cavity and in contact with a lipid ligand [<xref rid="R13" ref-type="bibr">13</xref>
].
In addition to cysteine residues, the LTP2 structure comprises conserved Gln, Tyr, and Pro residues.
</p>
<p>The hydrophobic cavity volume in both LTP subclasses
can vary considerably. For example, the hydrophobic
cavity volume of rice LTP1 is 249 A3, but the
cavity volume increases to 1,354 A3 when the protein
binds palmitic acid. This flexibility of LTP molecules
may be the cause of their low specificity to a lipid ligand.
</p>
</sec>
<sec><title>LIPID BINDING AND TRANSFER</title>
<p>The presence of a hydrophobic cavity in the structure of LTP molecules enables
these proteins to bind and transfer a variety of ligands. The LTP-ligand
complex formation <italic>in vitro </italic>
depends on the hydrophobic cavity
size, the amino acid residues constituting the cavity, the spatial structure of
the ligand, as well as experimental conditions (pH, buffer composition,
temperature). LTPs isolated from various plant sources have been shown to be
capable of binding lipids. However, it should be noted that there are
exceptions to this rule. For example, a protein from onion (<italic>Allium
cepa</italic>
) seeds, termed Ace-AMP1, has a pronounced homology with plant
LTPs but does not interact with lipids, perhaps because of the absence of a
one-whole cavity in the protein molecule [<xref rid="R14" ref-type="bibr">14</xref>
].
</p>
<p>Various LTPs bind a wide range of ligands, including fatty acids (FAs) with a
C<sub>10</sub>
–C<sub>18</sub>
chain length, acyl derivatives of coenzyme
A (CoA), phospho- and galactolipids, prostaglandin B2, sterols, molecules of
organic solvents, and some drugs [<xref rid="R15" ref-type="bibr">15</xref>
,
<xref rid="R16" ref-type="bibr">16</xref>
]. Although LTPs lack marked
specificity to ligands, these proteins form the most stable complexes with FAs
containing from 16 to 18 carbon atoms. LTPs do not form stable complexes with
molecules with a chain length longer than C<sub>20</sub>
due to the spatial
constraints imposed by the hydrophobic cavity size [<xref rid="R17" ref-type="bibr">17</xref>
].
Furthermore, the complex stability has been shown to be
affected by the number of double bonds in FA molecules and their configuration.
LTPs form the most stable complexes with various unsaturated FAs with one or
two double bonds in the <italic>cis</italic>
configuration
[<xref rid="R18" ref-type="bibr">18</xref>
], two of which, the linoleic and oleic
acids, are precursors of cutin and suberin monomers.
</p>
<p>Unlike LTP2s, LTP1s do not bind sterols. The ligand orientation in the LTP1
hydrophobic cavity was found to be different, depending on the spatial
arrangement of ligand and LTP1 molecules. For example, in complexes of maize
LTP1 with 1-palmitoyl lysophosphatidylcholine [<xref rid="R9" ref-type="bibr">9</xref>
]
and wheat (<italic>Triticuma estivum</italic>
) LTP1 with
dimyristoyl phosphatidylglycerol [<xref rid="R18" ref-type="bibr">18</xref>
],
ligands in the protein cavity occur in the “forward” orientation;
i.e., polar lipid heads are located near the larger entrance to the hydrophobic
cavity. At the same time, the ligand in the complex of barley (<italic>Hordeum
vulgare</italic>
) LTP1 with palmitoyl CoA occurs in “reverse”
orientation, its aliphatic chains are strongly bent, and the polar head points
towards the smaller entrance to the cavity [<xref rid="R19" ref-type="bibr">19</xref>
].
</p>
<p>Plant LTP1s can bind one or two lysophospholipid molecules
[<xref rid="R20" ref-type="bibr">20</xref>
]. LTPs of this subclass are supposed to
interact with ligands according to a cooperative binding model. If two ligand
molecules occur in the hydrophobic cavity, their orientation and binding
affinity for the protein are not identical. For example, two lyso-myristoyl
phosphatidylcholine molecules bound to wheat LTP1 have a
“head-to-tail” orientation in the hydrophobic cavity
[<xref rid="R19" ref-type="bibr">19</xref>
, <xref rid="R21" ref-type="bibr">21</xref>
].
It is suggested that the second binding site of LTP is
activated only when the first site is already occupied by a ligand.
</p>
<p>The calcium-calmodulin system was shown to be involved in the regulation of
lipid binding to plant LTPs. Plant LTPs bind calmodulin regardless of the
presence of calcium ions. In maize Zm-LTP and onion Ace-AMP1, a potential site
for binding of calmodulin is situated in the middle portion of the LTP
polypeptide chain (residues 46–60) and has a structure similar to that of
the basic amphiphilic α-helix (BAA) domain of calmodulin-binding proteins
[<xref rid="R22" ref-type="bibr">22</xref>
]. A distinctive feature of the
BAA-like domain in plant LTPs is the absence of Trp that plays a crucial role
in calcium-dependent binding of calmodulin. Maize Zm-LTP affinity for binding
lipids is reduced in the presence of calmodulin. This is explained by the fact
that the calmodulin binding site of the protein contains the Arg46 residue
involved in the binding of lipids. At the same time, the calmodulin binding
site in the bok choy (<italic>Brassica rapa subsp. chinensis</italic>
) protein,
termed BP-10, and arabidopsis (<italic>Arabidopsis thaliana</italic>
) LTP1 is
located in the C-terminal region (amino acid residues 69–81) and has no
structural similarity with any of the known calmodulin binding sites
[<xref rid="R23" ref-type="bibr">23</xref>
]. The BP-10-calmodulin complex formation
increases the efficiency of lipid binding. The cause of this effect is believed
to be the residue Tyr81 located in the calmodulin binding site of the LTP
protein and playing an important role in the interaction with a lipid ligand.
</p>
<p>Plant LTPs not only bind lipids, but also transfer them between membranes in
experiments <italic>in vitro</italic>
. They transfer phospholipids, such as
phosphatidylcholines (PCs), phosphatidylinositols (PIs), phosphatidylglycerols
(PGs), their derivatives, as well as acyl-CoA [<xref rid="R24" ref-type="bibr">24</xref>
-<xref rid="R26" ref-type="bibr">26</xref>
]. Wheat LTPs were
used to demonstrate that the lipid transfer activity of LTP2s is several times
higher than that of LTP1s [<xref rid="R27" ref-type="bibr">27</xref>
].
</p>
<p>The lipid transfer mechanism involving LTPs remains unclear. Plant LTPs, like
mammalian phosphatidylcholine- specific LTPs, are supposed to transfer lipids
by the shuttle mechanism. A LTP-phospholipid complex interacts with the
membrane, which results in phospholipid exchange between the complex and
membrane [<xref rid="R3" ref-type="bibr">3</xref>
].
</p>
<p>To date, there is no direct evidence of involvement of plant LTPs in the
binding and transfer of lipids <italic>in vivo</italic>
. The only LTP-ligand
complex found in plant cells is a covalent adduct of barley LTP1 and oxylipin
that is formed by reacting the carboxyl group of Asp7 with the allene oxide in
a 9(<italic>S</italic>
),10-epoxy-10,12(<italic>Z</italic>
)-octadecadienoic acid
molecule [<xref rid="R28" ref-type="bibr">28</xref>
, <xref rid="R29" ref-type="bibr">29</xref>
]. The reaction yields
α-ketol-9-hydroxy-10-oxo-12(<italic>Z</italic>
)-octadecenoic acid. It
should be noted that the formation of this covalent complex, known as LTP1b,
increases the hydrophobic cavity flexibility and the protein ability to
transfer lipids.
</p>
<p>Some LTPs are not only able to bind and transfer lipids but also to induce
permeabilization of model membranes. For example, the sunflower
(<italic>Helianthus annuus</italic>
) protein termed Ha-AP10 damages liposomes
consisting of PCs and PGs [30]. It is interesting to note the lack of a
correlation between the lipid binding and lipid transfer activity and the LTP
ability to damage membranes. For example, barley LTP binds a wide range of
lipids but has little effect on the properties of model membranes [31]. Onion
Ace-AMP1 does not bind lipids but induces permeabilization of bilayer vesicles
consisting of anionic lipids [14].
</p>
</sec>
<sec><title>BIOSYNTHESIS AND LOCALIZATION</title>
<p>The LTP class belongs to a large family of pathogenesis- related proteins
(PRPs). Induction of the synthesis of these proteins occurs upon exposure of a
plant to abiotic and biotic stress factors and underlies one of the key defense
mechanisms in plants. PRPs are present in all plant organs and accumulated in
the vacuoles and apoplast, as well as in the primary and secondary cell walls.
This localization is consistent with the defense function of PRPs that, along
with antimicrobial peptides (AMPs), create a specific barrier to pathogen
penetration [<xref rid="R32" ref-type="bibr">32</xref>
].
</p>
<p>The family of pathogenesis-related proteins includes, along with LTPs (PRP-14),
proteins of 16 more classes: glucanases (PRP-2), chitinases (PRP-3, 4, 8),
protease inhibitors (PRP-6), homologs of the major birch pollen allergen Bet v
1 (PRP-10), defensins (PRP-12), thionins (PRP-13), etc. [<xref rid="R33" ref-type="bibr">33</xref>
]. Abiotic inducers of the PRP synthesis include UV
radiation, osmotic shock, lack of moisture, low temperatures, and soil
salinity. The PRP synthesis in an infected plant is induced by both primary and
secondary elicitors: non-specific pathogen-associated molecular patterns
(PAMPs) and damage-associated molecular patterns (DAMPs), as well as by
specific effector proteins of pathogens. PRP synthesis inducers include
phytohormones, such as ethylene, auxins, as well as abscisic, jasmonic, and
salicylic acids. At certain stages of ontogeny, activation of synthesis and
tissue-specific accumulation of PRPs also occur in the absence of stressors
[<xref rid="R34" ref-type="bibr">34</xref>
].
</p>
<p>LTPs have been found in various plant organs: seeds, leaves, stems, roots,
flowers, and fruits. Most often, LTPs occur in cuticle-covered epidermal cells
but are also found in embryonic and vessel tissues. LTPs are synthesized in
plant cells as preproteins containing a hydrophobic signal sequence
(21–27 or 27–35 amino acid residues in LTP1s or LTP2s,
respectively) and are secretory proteins with a predominantly extracellular
localization [<xref rid="R35" ref-type="bibr">35</xref>
, <xref rid="R36" ref-type="bibr">36</xref>
]. Some LTPs have an atypical intracellular localization.
For example, LTP from castorbean (<italic>Ricinus communis</italic>
) seeds was
found in glyoxysomes [<xref rid="R37" ref-type="bibr">37</xref>
]; LTP from
cowpea (<italic>Vigna unguiculata</italic>
) seeds was found in vacuoles [<xref rid="R38" ref-type="bibr">38</xref>
]; Ca-LTP(1) from pepper (<italic>Capsicum
annuum</italic>
) seeds was found in vesicles [<xref rid="R39" ref-type="bibr">39</xref>
]. Of particular interest is the question of how LTPs
synthesized as preproteins without appropriate signal sequences occur in these
cell organelles. Sunflower LTP, HaAP10, was found to be relocalized. In dry
seeds, Ha-AP10 occurs in the apoplast; upon imbibition and germination of
seeds, it relocalizes, possibly by endocytosis, to the intracellular organelles
involved in lipid metabolism [<xref rid="R40" ref-type="bibr">40</xref>
].
</p>
<p>In some plants, LTPs termed GPI-anchored lipid transfer proteins (LTPGs) were
found. These proteins are synthesized as precursors containing, in addition to
the N-terminal signal peptide, the C-terminal signal sequence. This sequence
ensures the post-translational attachment of the glycosylphosphatidylinositol
anchor (GPI) to the protein, through which LTPGs can be localized on the outer
side of the cell membrane or secreted to the apoplast after GPI-anchor cleavage
[<xref rid="R41" ref-type="bibr">41</xref>
]. Another group of unusual LTPs with
extracellular localization is constituted by the xylogen from zinnia
(<italic>Zinnia elegans</italic>
) and xylogen-like proteins of other plants
[<xref rid="R42" ref-type="bibr">42</xref>
]. The gene structure of xylogen-like
proteins, which belong to a large family of arabinogalactan proteins (AGPs),
contains a signal peptide, the LTP domain, several AGP domains, and the GPI
anchor attachment signal. During maturation, these proteins undergo a series of
post-translational modifications, including removal of the N-terminal signal
peptide, GPI anchor attachment, proline hydroxylation, and Oglycosylation
[<xref rid="R42" ref-type="bibr">42</xref>
].
</p>
<p>Plant LTPs are encoded by multigene families and, in the plant genome, are
usually represented by a set of genes encoding different isoforms. Expression
of genes of different LTP isoforms is characterized by pronounced tissue
specificity and occurs at certain stages of ontogeny [<xref rid="R36" ref-type="bibr">36</xref>
]. This may be related to the fact that different LTP
isoforms have different functions [<xref rid="R43" ref-type="bibr">43</xref>
].
Differential expression of genes of multiple LTP isoforms also occurs when a
plant is exposed to a variety of abiotic and biotic environmental factors and
may be considered as one of the defensive strategy elements under stress
conditions [<xref rid="R44" ref-type="bibr">44</xref>
]. Differential expression
of isoform genes was shown for LTPs from sesame (<italic>Sesam
umindicum</italic>
) [<xref rid="R45" ref-type="bibr">45</xref>
], arabidopsis
[<xref rid="R43" ref-type="bibr">43</xref>
, <xref rid="R46" ref-type="bibr">46</xref>
], pepper [<xref rid="R47" ref-type="bibr">47</xref>
],
castorbean [<xref rid="R37" ref-type="bibr">37</xref>
], grape (<italic>Vitis
vinifera</italic>
) [<xref rid="R48" ref-type="bibr">48</xref>
], Kashgar
tamarisk (<italic>Tamarix hispida</italic>
) [<xref rid="R49" ref-type="bibr">49</xref>
], and tomato (<italic>Lycopersicon pennellii</italic>
)
[<xref rid="R50" ref-type="bibr">50</xref>
].
</p>
</sec>
<sec><title>BIOLOGICAL ACTIVITY</title>
<p>As mentioned, LTPs constitute one of the classes of defense PRPs, many of which
have antimicrobial and enzymatic activities or are enzyme inhibitors. Various
representatives of the LTP class exhibit antibacterial, antifungal, antiviral,
and antiproliferative activities, and inhibit some enzymes [<xref rid="R36" ref-type="bibr">36</xref>
].
</p>
<p><bold>Antimicrobial activity</bold>
</p>
<p>Many LTPs have antimicrobial activity and inhibit the growth of pathogenic
bacteria and fungi, such as<italic> Clavibacter michiganensis</italic>
,
<italic>Pseudomonas solanacearum</italic>
,<italic> P. syringae</italic>
,
<italic>Alternaria brassicola</italic>
, <italic>Ascochyta
pisi</italic>
,<italic> Colletotrichum lindemuthianum</italic>
, <italic>Fusarium
solani</italic>
, <italic>F. graminearum</italic>
, <italic>F. culmorum</italic>
,
<italic>F. oxysporum</italic>
, <italic>Botrytis cinerea</italic>
,
<italic>Sclerotinia sclerotiorum</italic>
, <italic>Verticillium
dahliae</italic>
, etc. LTPs from pepper and coffee (<italic>Coffe
acanephora</italic>
) are also active against human pathogenic fungal strains
from the <italic>Candida </italic>
genus [<xref rid="R39" ref-type="bibr">39</xref>
, <xref rid="R51" ref-type="bibr">51</xref>
]. The
antimicrobial activity of most plant LTPs is specific and exhibited against a
particular spectrum of microorganisms. LTPs from onion [<xref rid="R52" ref-type="bibr">52</xref>
], radish (<italic>Raphanus sativus</italic>
) [<xref rid="R52" ref-type="bibr">52</xref>
], and arabidopsis [<xref rid="R53" ref-type="bibr">53</xref>
] have pronounced antimicrobial activity at micromolar
concentrations. Most LTPs have a moderate or little effect on the growth of
microorganisms; in some cases, this effect is absent. [<xref rid="R54" ref-type="bibr">54</xref>
] The antimicrobial activity of plant LTPs decreases in high
salt solutions and in the presence of calcium ions, which is a common feature
of other classes of plant AMPs and PRPs [<xref rid="R52" ref-type="bibr">52</xref>
]. Like plant defensins, LTPs are able to act in synergy
with thionins [<xref rid="R55" ref-type="bibr">55</xref>
] and have no toxic
effects on plant cells and mammalian cells, including fibroblasts and red blood
cells [<xref rid="R30" ref-type="bibr">30</xref>
, <xref rid="R52" ref-type="bibr">52</xref>
].
</p>
<p>Disruption of the disulfide bonds stabilizing the structure of plant LTPs leads
to a loss of the ability of the proteins to inhibit the growth of
microorganisms and bind lipids [<xref rid="R56" ref-type="bibr">56</xref>
]. At
the same time, the other amino acid residues that are necessary for exhibiting
the antimicrobial activity remain unknown. The antimicrobial activity of rice
LTP110 was shown to require the presence of the conserved residues Tyr17,
Arg46, and Pro72 that play an important role in the stabilization of the
protein structure in most LTP1s [<xref rid="R57" ref-type="bibr">57</xref>
]. A
study of wheat LTP isoforms demonstrated that difference in one amino acid
residue only (Pro3Ser in TaLt10B6 and TaLt710H24 isoforms and Asn24Ser in
TaLt10F9 and TaBs116G9 isoforms) significantly affects the antimicrobial
activity of the proteins. It is assumed that the replacement of just one amino
acid residue may result in a change in the LTP spatial structure and affect the
positive charge distribution over the molecule surface [<xref rid="R56" ref-type="bibr">56</xref>
].
</p>
<p>To date, the antimicrobial activity of plant LTPs is found not to be related to
their ability to interact with lipids. For example, eight wheat LTP isoforms
were shown to have no correlation between the ability of the proteins to
inhibit the growth of pathogenic microorganisms and to bind lipids [<xref rid="R56" ref-type="bibr">56</xref>
]. Using onion Ace-AMP1 [<xref rid="R52" ref-type="bibr">52</xref>
] and a mutant rice LTP isoform [<xref rid="R57" ref-type="bibr">57</xref>
], it was also shown that this class of
proteins may possess antimicrobial activity but not bind lipid molecules and
vice versa.
</p>
<p>Plant LTPs have not only fungistatic, but also fungicidal activity and, like
other AMPs, are able to induce permeabilization of the model membranes [<xref rid="R30" ref-type="bibr">30</xref>
] and cell membranes of pathogenic fungi
[<xref rid="R30" ref-type="bibr">30</xref>
, <xref rid="R56" ref-type="bibr">56</xref>
]. For example, LTPs from onion [<xref rid="R14" ref-type="bibr">14</xref>
], sunflower [<xref rid="R30" ref-type="bibr">30</xref>
],
and, to a lesser extent, barley [<xref rid="R31" ref-type="bibr">31</xref>
] are
able to induce permeabilization of liposomes consisting of anionic
phospholipids only or a mixture of anionic and neutral phospholipids, causing
fluorescent dye leakage from liposomes. However, it should be noted that this
effect is much weaker than that in other plant AMPs and observed only in
lowionic- strength solutions.
</p>
<p>The mechanism of antimicrobial action of representatives of the LTP class
remains unclear. Nevertheless, the cell membrane is considered as a potential
target for LTP antimicrobial action. Plant LTPs, like other cationic
membrane-active AMPs, are supposed to bind to the cell membrane of the
phytopathogen through electrostatic interactions and cause destabilization and
permeabilization of the membrane. The weaker antimicrobial activity of LTP
isoforms containing a smaller number of basic amino acids is explained by the
attenuation of the electrostatic interaction with the cell membrane of the
phytopathogen [<xref rid="R56" ref-type="bibr">56</xref>
]. A potential cause of
the selective toxicity of plant LTPs is believed to be the differences in the
lipid composition of the cell membranes of bacteria, fungi, plants, and
mammals.
</p>
<p><bold>Antiviral and antiproliferative activities</bold>
</p>
<p>LTPs from Chinese daffodil (<italic>Narcissus tazetta</italic>
) and cole seed
(<italic>Brassica campestris</italic>
) were shown to have antiviral activity
and the ability to inhibit the proliferation of human tumor cells. In
<italic>in vitro </italic>
experiments, <italic>N.tazetta</italic>
LTP,
designated as NTP, significantly inhibited plaque formation of the respiratory
syncytial virus (RSV), the cytopathic effect of the influenza A virus (H1N1),
and the proliferation of the human acutepromyelocytic leukemia cell (HL-60).
<italic>B. campestris </italic>
LTP inhibit the activity of HIV-1 reverse
transcriptase and the proliferation of hepatoma HepG2 and breast cancer MCF7
cells. To date, the mechanism of LTP anti-tumor activity has not been
determined [<xref rid="R58" ref-type="bibr">58</xref>
, <xref rid="R59" ref-type="bibr">59</xref>
].
</p>
<p><bold>Inhibition of enzyme activity</bold>
</p>
<p>Some members of the LTP class, like protease inhibitors (PRP-6) and certain
defensins (PRP-12) [<xref rid="R60" ref-type="bibr">60</xref>
, <xref rid="R61" ref-type="bibr">61</xref>
], can inhibit the activity of proteolytic
enzymes and α-amylases. For example, barley seed LTPs of both subclasses
were found to inhibit cysteine endoproteases [<xref rid="R62" ref-type="bibr">62</xref>
]. Also, LTP1 from the <italic>Ginkgo biloba </italic>
seed
inhibits cysteine (papain), aspartate (pepsin), and serine (trypsin) proteases
[<xref rid="R63" ref-type="bibr">63</xref>
]. LTP1 from seeds of coffee and
pepper inhibit the activity of human α-amylase [<xref rid="R39" ref-type="bibr">39</xref>
, <xref rid="R51" ref-type="bibr">51</xref>
]. LTPs capable
of inhibiting the activity of their own and foreign enzymes are believed to be
involved both in the development and germination of seeds and in the protection
of plants against insects and herbivores.
</p>
</sec>
<sec><title>POTENTIAL LTP FUNCTIONS</title>
<p>LTPs are known to play an important role in plants. Knockout of the genes
encoding these proteins leads to disruption of the vegetative and reproductive
development of plants and a decrease in their resistance to infections
[<xref rid="R43" ref-type="bibr">43</xref>
, <xref rid="R64" ref-type="bibr">64</xref>
,
<xref rid="R65" ref-type="bibr">65</xref>
]. The results of a study of the
inhibition of LTP gene expression support a number of assumptions about the
possible involvement of proteins from this class in the adaptation of plants to
stress, lipid metabolism, embryogenesis, growth and reproduction of plants,
symbiosis, and other processes. Many of these functions are believed to be
associated with the LTP ability to bind and transfer lipid molecules
(<italic><xref ref-type="fig" rid="F3">Fig. 3</xref>
</italic>
).
</p>
<fig id="F3" orientation="portrait" position="float"><label>Fig. 3</label>
<caption><p>Potential LTP functions in plants
</p>
</caption>
<graphic xlink:href="AN20758251-29-047-g003"></graphic>
</fig>
<p><bold>Involvement in lipid metabolism</bold>
</p>
<p>Because plant LTPs are capable of binding and transferring lipids, these
proteins are believed to be involved in a variety of processes that are
accompanied by changes in lipid composition. Extracellular LTPs are supposed to
participate in the formation of a protective cuticle layer whose monomeric
components are formed in epidermal cells and delivered to the biosynthesis
site. Activation of biosynthesis of the cuticle, which plays an important role
in maintaining the water balance and protection of plants from penetration by
pathogens, occurs under the action of a variety of stress factors and is one of
the defense mechanisms in plants. There is no direct evidence of LTP
involvement in this process. However, plant LTPs were shown to occur at high
concentrations in epidermal tissues and of being capable of binding the fatty
acids required for the synthesis of cutin and suberin. Furthermore, induction
of LTP synthesis is accompanied by thickening of the cuticle layer [<xref rid="R66" ref-type="bibr">66</xref>
] and knockout of LTP genes leads to changes
in the lipid composition and density of the cuticle layer [<xref rid="R67" ref-type="bibr">67</xref>
]. Two potential mechanisms of cuticle
component delivery with involvement of LTPs were suggested. According to the
first of them, LTPs enter the cell by receptor-mediated endocytosis and are
loaded by the fusion of vesicles containing LTP and cutin monomers. The second
mechanism suggests shuttling of LTPs between the cell membrane and the cell
wall of plants and the existence of a carrier molecule acting on the inner side
of the cell membrane [<xref rid="R68" ref-type="bibr">68</xref>
]. An
interesting fact is that LTP1s are present in organs covered by a cutin layer
(leaves, stems, flowers), while LTP2s occur in suberin- covered subterranean
organs. This argues for a differential involvement of proteins of the first and
second subclasses in the cutin and suberin layer formation [<xref rid="R35" ref-type="bibr">35</xref>
]. LTPGs having a GPI anchor were
demonstrated to be possibly involved in the biosynthesis and accumulation of
suberin [<xref rid="R41" ref-type="bibr">41</xref>
].
</p>
<p>LTPs found in various intracellular organelles are presumably involved in the
mobilization of lipids through their transfer, e.g., during seed germination.
For example, castorbean LTP found in glyoxysomes binds both free FAs and
acyl-CoA. This protein also increases the activity of acyl-CoA oxidase involved
in the β-oxidation of FAs [<xref rid="R37" ref-type="bibr">37</xref>
].
Sunflower LTP Ha-AP10 entering the cell during seed germination is supposed to
transfer FAs, liberated by cleavage of triacylglycerols, to glyoxysomes for
further β-oxidation [<xref rid="R40" ref-type="bibr">40</xref>
].
</p>
<p>Induction of the expression of genes encoding carrot (<italic>Daucus
carota</italic>
) LTP was demonstrated to occur at the early stages of
embryogenesis when degradation of some lipids and biosynthesis of others, as
well as the protective lipid layer formation around the embryo, takes place
[<xref rid="R69" ref-type="bibr">69</xref>
]. The role of this protein in
embryogenesis is presumably to participate in these processes via the transfer
of relevant lipid molecules.
</p>
<p><bold>Involvement in fertilization of flowering plants</bold>
</p>
<p>Plant LTPs are believed to play an important role in the reproduction of
flowering plants. For example, lily (<italic>Lilium longiflorum</italic>
) LTP1
is a component necessary for pollen adhesion and formation and growth of the
pollen tube [<xref rid="R70" ref-type="bibr">70</xref>
]. LTP1 is supposed to be
capable of acting directly as an adhesive component or as a carrier of the
hydrophobic adhesive component. Also, one of the isoforms of a lipid transfer
protein from arabidopsis, LTP5, was shown to be involved in the growth of the
pollen tube and seed formation [<xref rid="R64" ref-type="bibr">64</xref>
].
</p>
<p>The role of rice LTP OsC6 in postmeiotic pollen development has been
determined. This protein was found to be present in anther tissue and to be
capable of binding FAs. OsC6 is supposed to be involved in the formation of
lipid orbicles and pollen exine through transfer of essential lipids from
tapetum cells to microspores [<xref rid="R65" ref-type="bibr">65</xref>
].
</p>
<p><bold>Involvement in protection and adaptation of plants under stress
conditions</bold>
</p>
<p>The belief that LTPs are involved in the protection and adaptation of plants to
stress is mainly based on the fact of a stress-induced synthesis of these
proteins. For example, the synthesis of LTPs, as well as that of other PRPs, is
induced by wounding, moisture deficit, low temperatures, soil salinity,
infections, and chemical agents [<xref rid="R43" ref-type="bibr">43</xref>
,
<xref rid="R45" ref-type="bibr">45</xref>
, <xref rid="R47" ref-type="bibr">47</xref>
, <xref rid="R50" ref-type="bibr">50</xref>
, <xref rid="R71" ref-type="bibr">71</xref>
, <xref rid="R72" ref-type="bibr">72</xref>
]. Induction of the expression of LTP genes under stress
conditions may be associated with the presence of regulatory elements, which
are also typical of other PRPs, in the promoter region of LTP genes. The
regulation of LTP gene expression involves phytohormones, such as abscisic and
salicylic acids, ethylene, and methyl jasmonate [<xref rid="R36" ref-type="bibr">36</xref>
].
</p>
<p>One of the possible causes behind the induction of LTP gene expression under
stress conditions is believed to be the involvement of these proteins in the
biosynthesis of the cuticle layer [<xref rid="R50" ref-type="bibr">50</xref>
].
The protective function of LTPs in plants is related to their antimicrobial
activity, cryoprotective action, and their ability to inhibit exogenous
enzymes, as well as to their possible involvement in the secretion of other
components of the plant immune system.
</p>
<p>The glandular hairs (trichomes) of plants produce essential oils that are
involved in metabolism, protect plants against pests and overheating, have a
woundhealing effect, and attract insects. Tobacco (<italic>N. tabacum</italic>
)
NtLTP1 was found to be specifically expressed in long glandular trichomes and
to be involved in the secretion, from trichome heads, of essential oil
components (diterpenes, aliphatic hydrocarbons, and aromatic acids) that are
plant protective factors [<xref rid="R73" ref-type="bibr">73</xref>
]. LTP gene
transcripts were also found in the glandular hairs of other plants, such as
pepper mint (<italic>Mentha piperita</italic>
), alfalfa (<italic>Medicago
sativa</italic>
), sweet wormwood (<italic>Artemisia annua</italic>
), hop
(<italic>Humulus lupulus</italic>
), Greek sage (<italic>Salvia
fruticosa</italic>
), and tomato [<xref rid="R73" ref-type="bibr">73</xref>
].
</p>
<p>The resistance of plants to cold is known to be associated with stabilization
of cell membranes and prevention of a protein solubility reduction at lower
temperatures. WAX9 proteins that have a high degree of amino acid sequence
homology with LTPs were identified in the leaves of a cold-acclimated cabbage
(<italic>Brassica oleracea</italic>
). These proteins cannot bind lipids, but,
like β-1,3- glucanases, osmotins, and lectins, they are able to stabilize
thylakoid membranes in cold conditions [<xref rid="R72" ref-type="bibr">72</xref>
]. The mechanism of cryoprotective action of these proteins
is supposed to be associated with a decrease in the fluidity of membrane lipids
upon interaction between LTPs and the thylakoid membrane [<xref rid="R74" ref-type="bibr">74</xref>
].
</p>
<p><bold>Involvement in activation and regulation of signaling cascades</bold>
</p>
<p>LTPs are supposed to be involved in the activation and regulation of various
signaling pathways in plants through the formation of complexes with various
lipid molecules. Oxylipins are one of the classes of signal mediators in
plants. Oxylipins are produced from unsaturated FAs under the action of
reactive oxygen species (ROS) or enzymes and are involved in the regulation of
the growth and development of plants, as well as in triggering defense
responses to stress conditions. In addition, oxylipins regulate the processes
of neutralization of the toxic components formed during stress. As mentioned,
barley LTP1, during seed germination, forms covalent complexes with oxylipin of
9(<italic>S</italic>
),10-epoxy-10,12(<italic>Z</italic>
)-octadecadienoic acid
containing an unstable allene oxide resulting from the sequential action of
lipoxygenase and allene oxide synthase
[<xref rid="R28" ref-type="bibr">28</xref>
, <xref rid="R29" ref-type="bibr">29</xref>
].
This interaction may indicate a joint involvement of LTPs and oxylipins in the
regulation of the signaling pathways that trigger the mechanism preventing
damage to plant cells under stress conditions [<xref rid="R29" ref-type="bibr">29</xref>
].
</p>
<p>LTPs bound to lipid molecules act as endogenous elicitors interacting with
specific receptors on the cell membrane of plant cells and providing for the
development of an immune response to infection
(<italic><xref ref-type="fig" rid="F4">Fig. 4</xref>
</italic>
). For
example, rice and tobacco LTPs were shown to be capable of interacting with elicitin receptors
[<xref rid="R21" ref-type="bibr">21</xref>
, <xref rid="R75" ref-type="bibr">75</xref>
,
<xref rid="R76" ref-type="bibr">76</xref>
]. Elicitins are well-studied plant PAMPs that have a
molecular weight of about 10 kDa and are produced by phytopathogenic oomycetes
(<italic>Phytophthora </italic>
and <italic>Pythium</italic>
) parasitizing on
higher plants. These proteins, due to a hydrophobic cavity in their structure,
can bind sterols and provide phytopathogenic microorganisms with essential
plant-derived lipids. All elicitins have a α-helical structure stabilized
by three disulfide bonds; sterol-associated elicitins are recognized by the
plant by means of receptor-like kinases located on the cell membrane. The
recognition entails activation of plant defense mechanisms, such as the
production of phytoalexins and ROS, as well as the development of a
hypersensitive response (HR) and systemic-acquired resistance (SAR)
[<xref rid="R77" ref-type="bibr">77</xref>
, <xref rid="R78" ref-type="bibr">78</xref>
].
The amino acid sequences of LTPs and elicitins have a low
degree of homology, whereas the spatial structures of the proteins have a
pronounced similarity [<xref rid="R79" ref-type="bibr">79</xref>
]. Lipid bound
plant LTPs act as agonists of elicitins and DAMP, bind to elicitin receptors,
and trigger an immune response. An interesting fact indicating the possibility
of different pathways for the activation of a plant defense response involving
representatives of the two LTP subclasses is the difference in the structure of
a hydrophobic ligand. Sterols act as this ligand for LTP2s
[<xref rid="R75" ref-type="bibr">75</xref>
], while jasmonic acid is the ligand for
LTP1s that have a less flexible hydrophobic cavity
[<xref rid="R21" ref-type="bibr">21</xref>
, <xref rid="R76" ref-type="bibr">76</xref>
].
</p>
<fig id="F4" orientation="portrait" position="float"><label>Fig. 4</label>
<caption><p>A potential mechanism of LTP involvement in plant immune response. LTPs are secreted to the apoplast and
bind to lipid molecules that are either secreted by the plant (e.g., jasmonic acid) or form under the action of enzymes
secreted by phytopathogenic microorganisms. Lipid-bound LTPs interact with receptors, such as receptor-like serine/
threonine protein kinases, located on the cell membrane that contain the extracellular leucine-rich repeat domain (LRR),
transmembrane, and cytoplasmic protein kinase (PK) domains. This interaction may cause signal transduction mediated
by versatile second messengers and a cascade of mitogen-activated protein kinases; activation of several transcription
factors; induction of the synthesis of protective factors, including AMPs and PRPs (possibly, LTP isoforms with a pronounced
antimicrobial activity); and, finally, SAR.
</p>
</caption>
<graphic xlink:href="AN20758251-29-047-g004"></graphic>
</fig>
<p>An unusual LTP2 representative from arabidopsis – termed DIR1 –
that has an isoelectric point in the acidic pH range plays the key role in SAR
development [<xref rid="R80" ref-type="bibr">80</xref>
]. During plant
infection, the protein is supposed to bind to the lipid molecules (oxylipins,
fatty acids, or monoacyl phospholipids) produced by lipases secreted by the
pathogen. Then, the formed complex interacts with a hypothetical receptor,
triggering a signaling cascade that leads to SAR development
[<xref rid="R81" ref-type="bibr">81</xref>
].
</p>
<p>Zinnia xylogen containing the GPI anchor and binding plant sterols was found to
promote the differentiation of uncommitted cells into tracheary elements and,
probably, to be involved in cell-cell interactions and signal transduction. It
is thought that xylogen-like proteins of other plants, whose LTP domains are
highly similar to those of LTP2s, may also be involved in cellcell interactions
and signal transduction, functioning in a complex with a lipid molecule
[<xref rid="R42" ref-type="bibr">42</xref>
].
</p>
<p><bold>Involvement in apoptosis</bold>
</p>
<p>Possible LTP involvement in apoptosis was assumed based on the similarity
between maize LTP and the mammalian pro-apoptotic protein Bid that also has an
internal cavity and binds and transfers lipids [<xref rid="R82" ref-type="bibr">82</xref>
]. Bid occurs in the cytosol and, in the presence of
lysophospholipids generated during programmed cell death, affects mitochondria,
causing the release of apoptogenic factors, including cytochrome
<italic>c</italic>
. In the presence of lysophospholipids, maize LTP also causes
the release of cytochrome <italic>c </italic>
from mitochondria. A possible
mechanism of the destabilizing action of both proteins includes transfer of
lysophospholipids to the outer mitochondrial membrane. The lysophospholipids
modify the membrane properties, thereby facilitating the action of other
pro-apoptotic proteins [<xref rid="R83" ref-type="bibr">83</xref>
].
</p>
<p><bold>Involvement in symbiosis</bold>
</p>
<p>Symbiotic rhizobacteria are known to be able to stimulate the growth of plants
and protect them from soil phytopathogens, causing the development of the
socalled induced systemic resistance (ISR) that is phenotypically and
functionally similar to SAR [<xref rid="R84" ref-type="bibr">84</xref>
].
Alfalfa LTP MtN5 was shown to play an important role in the development of
symbiotic relationships between a plant and nodule bacteria. Namely, the
protein is involved in processes of bacteria penetration into root tissues and
nodule formation [<xref rid="R85" ref-type="bibr">85</xref>
]. The MtN5 function
is supposed to maintain the balance between bacterial invasion and prevention
of infection [<xref rid="R86" ref-type="bibr">86</xref>
].
</p>
<p><bold>Involvement in fruit ripening</bold>
</p>
<p>Tomato LTP was shown to be capable of forming complexes with polygalacturonase,
which is the most significant pectin-degrading enzyme. Upon complex formation,
tomato LTP enhances the hydrolytic activity of the enzyme and may be involved
in the regulation of fruit softening and ripening [<xref rid="R87" ref-type="bibr">87</xref>
].
</p>
</sec>
<sec><title>LTPs AS ALLERGENS</title>
<p>LTPs are antigens involved in the development of allergic reactions of varying
severity to pollen, plant foods, and latex. The structure of these proteins,
stabilized by disulfide bonds, is responsible for their high resistance to
cleavage by digestive enzymes and enables the proteins to reach the human
intestine in native immunogenic form and to cause sensitization
[<xref rid="R88" ref-type="bibr">88</xref>
]. The allergenic capacity of LTPs in
various processed foods (juices, jams, beer, wine, etc) is explained by their
highly stable structure that is practically unsusceptible to thermal
denaturation, as well as chemical and enzymatic degradation
[<xref rid="R89" ref-type="bibr">89</xref>
]. It should be noted that the defined
allergens are mostly members of the first subclass of plant LTPs. For example,
the IUIS allergen database now contains only three LTP2s (tomato, peanut, and
celery) and 42 LTP1s from various plants, apart from their isoforms. The high
structural homology of LTP1s underpins the development of cross-allergic
reactions.
</p>
<p>LTP1s, which are widely distributed in the plant kingdom, are the main
allergens isolated from fruits and grains (peach (<italic>Prunus
persica</italic>
) Pru p 3, cherry (<italic>P. avium</italic>
) Pru av 3, apple
(<italic>Malus domestica</italic>
) Mal d 3, plum (<italic>P.
domestica</italic>
) Pru d 3, orange (<italic>Citrus sinensis</italic>
) Cit s 3,
grape Vit v 1, strawberry (<italic>Fragaria ananassa</italic>
) Fra a 3), nuts
(hazelnut (<italic>Corylus avellana</italic>
) Cor a 8, walnut (<italic>Juglans
regia</italic>
) Jug r 3, chestnut (<italic>Castanea sativa</italic>
) Cas s 8),
vegetables (asparagus (<italic>Asparagus officinalis</italic>
) Aspa o 1,
lettuce (<italic>Lactuca sativa</italic>
) Lec s 1, cabbage Bra o 3, tomato
(<italic>Lycopersicone sculentum</italic>
) Lyc e 3, celery (<italic>Apium
graveolens</italic>
) Api g 2), cereals (maize Zea m 14, rice Ory s 14, wheat
Tri a 14, barley Hor v 14), and legumes (peanut (<italic>Arachis
hypogaea</italic>
) Ara h 9, lentil Len c 3, bean Pha v 3)
[<xref rid="R90" ref-type="bibr">90</xref>
-<xref rid="R92" ref-type="bibr">92</xref>
].
It is important to note that LTPs are accumulated mainly in the skin of fruits,
not in their pulp [<xref rid="R93" ref-type="bibr">93</xref>
], which may be the
cause of anaphylactic reactions in humans upon dermal contact with fruits
[<xref rid="R94" ref-type="bibr">94</xref>
]. A significant contribution to
primary sensitization is also made by pollen allergens of the LTP class: Jewish
pellitory (<italic>Parietaria judaica</italic>
) Par j 2, olive (<italic>Olea
europaea</italic>
) Ole e 7, plane tree (<italic>Platan usacerifolia</italic>
)
Pla a 3, mugwort(<italic>Artemisia vulgaris</italic>
) Art v 3, etc.
[<xref rid="R95" ref-type="bibr">95</xref>
]. Interestingly, LTPs from fruits of
<italic>Rosaceae </italic>
family plants were also found in the pollen of these
trees [<xref rid="R96" ref-type="bibr">96</xref>
]. Peach Pru p 3 is believed to
be the main LTP allergen that plays the major role in sensitization and is
recognized by immunoglobulin E (IgE) in most individuals with allergies
[<xref rid="R97" ref-type="bibr">97</xref>
, <xref rid="R98" ref-type="bibr">98</xref>
].
</p>
<p>In recent years, numerous studies have been conducted to elucidate the causes
of high plant LTP1 allergenicity and development of cross-induced allergic
reactions. For example, IgE-binding B-cell epitopes of Pru p 3 were identified.
These are positively charged moieties on the protein surface that are
associated with the amino acid residues 11–25, 31–45, and
71–80 (<italic><xref ref-type="fig" rid="F1">Fig. 1A</xref>
</italic>
)
[<xref rid="R99" ref-type="bibr">99</xref>
].
The identified antigenic determinants are highly
homologous among various allergenic LTP1s. The key role in the interaction
between Pru p 3 and IgE was found to be played by the residues Arg39, Thr40,
and Arg44 that are typical of most allergenic LTP1s
[<xref rid="R100" ref-type="bibr">100</xref>
].
A polypeptide chain fragment comprising the amino acid
residues 61–80 acts as a T-cell epitope of Pru p 3
[<xref rid="R101" ref-type="bibr">101</xref>
].
Also, the development of a T-cell response to Pru p 3
was shown to be accompanied by increased expression of integrin α4β7
that provides lymphocyte migration to the intestinal wall where the primary
lymphocyte activation occurs [<xref rid="R102" ref-type="bibr">102</xref>
].
</p>
</sec>
<sec><title>EVOLUTION OF GENES</title>
<p>LTP genes are ubiquitous in higher plant genomes: from the most primitive
bryophytes to tracheophytes, including ferns, lycopsids, angiosperms, and
gymnosperms, but they are not found in lower plants, such as algae. In this
regard, it is assumed that the LTPs involved in the protection of plants
against various environmental stress factors could have developed during the
emergence of terrestrial plants, i.e. about 400 million years ago
[<xref rid="R103" ref-type="bibr">103</xref>
].
</p>
<p>As mentioned above, LTPs of one plant are usually encoded by tens of related
genes forming a multigene family. The emergence of multiple LTP isoforms
performing different functions in plants during evolution is believed to be
associated with a number of successive duplications of an ancestral gene and
subsequent mutations [<xref rid="R104" ref-type="bibr">104</xref>
]. During
evolution, most angiosperms are known to undergo one or more duplications of
the whole genome. A phylogenetic analysis of multiple LTP isoforms of rice,
wheat, and arabidopsis indicates that duplication of genes and chromosome
fragments continues at the present time [<xref rid="R105" ref-type="bibr">105</xref>
].
During evolution, mutations in duplicated LTP genes
could lead to gene pseudogenization, subfunctionalization with preservation of
some functions of the ancestral gene, or neofunctionalization, i.e. acquisition
of totally new functions by the gene [<xref rid="R106" ref-type="bibr">106</xref>
].
The last two possibilities might lead to the appearance
of new LTP isoforms with a different spectrum and degree of biological
activity, as well as LTP-like proteins that significantly differ from members
of the LTP class in structure and perform other functions.
</p>
</sec>
<sec><title>PRACTICAL APPLICATIONS</title>
<p><bold>LTPs as drug carriers</bold>
</p>
<p>The LTP ability to bind and transfer lipids creates opportunities for possible
use as ligand-binding proteins in developing drug and cosmetic agent delivery
systems that protect from premature biodegradation or reduce side effects upon
systemic application. The possibility of developing a LTP-based delivery system
depends on a number of LTP properties: a) resistance to heat denaturation and
protease action; b) the hydrophilic surface ensuring biocompatibility of a
LTP-ligand complex and a reduced risk of side reactions; c) protection of a
drug disposed within the LTP hydrophobic cavity from premature biodegradation;
d) the small size of a LTP-ligand complex, ensuring its effective penetration
into tissues; and e) increased affinity to and specificity for LTP-ligand
complex formation, which may be achieved by modifying the protein amino acid
sequence.
</p>
<p>Several studies have demonstrated that plant LTPs form complexes not only with
FAs and phospholipids, but also with other hydrophobic and amphiphilic ligands,
including some drug substances. For example, wheat LTP1 forms complexes with
prostaglandin B2 (PGB2). Upon interaction with LTP1, PGB2 was found to immerse
completely into the hydrophobic cavity of the protein, becoming isolated from
the environment [<xref rid="R17" ref-type="bibr">17</xref>
]. Wheat LTP1 was
shown to bind some components of the skin lipid layer (sphingosines,
sphingomyelins, and cerebrosides), which are used in cosmetics. Thus, wheat
LTP1 may be used in cosmetology as a skin lipids carrier. On the other hand,
wheat LTP1 is able to bind drugs that are active against pathogens of
leishmaniasis and HIV-1 and exhibit antineoplastic properties, but have serious
side effects when administered systemically (e.g., edelfosine, ilmofosine, and
their analogs). Using wheat LTP1 as a delivery vehicle may significantly reduce
the toxicity of these drugs. Furthermore, wheat LTP1 is able to deliver
antifungal agents, such as conazole BD56 and amphotericin B
[<xref rid="R16" ref-type="bibr">16</xref>
]. It should be noted that the
protein binds all these substances with low affinity, which is a
prerequisite for the transport and controlled release of the ligand.
</p>
<p>Screening of maize LTP1 and rice LTP2 using the Comprehensive Medicinal
Chemistry (CMC) database containing information about 7,300 biologically active
compounds demonstrated that the proteins contain not one but two potential drug
binding sites: one site occurs in the hydrophobic cavity, while the second site
is situated on the hydrophilic surface of the protein molecule. In rice LTP2,
the binding site for sterols, such as β-sitosterol or cholesterol, is
located near the hydrophobic cavity; the binding site for triphenylmethane
derivatives, such as diphenyl-4-pyridylmethane, occurs on the protein surface,
near the C-terminal region [<xref rid="R15" ref-type="bibr">15</xref>
].
</p>
<p><bold>LTPs in the food industry</bold>
</p>
<p>Surfactant properties of plant LTPs enable their use in the food industry as
emulsion and foam stabilizers. Beer brewing is one of the food industry sectors
where these LTP properties are widely used. The formation and stability of foam
are known to be important beer quality indicators. Numerous studies demonstrate
that LTPs are the major protein components of barley beer and play the key role
in the formation and stabilization of beer foam
[<xref rid="R35" ref-type="bibr">35</xref>
, <xref rid="R75" ref-type="bibr">75</xref>
].
The main beer components include a barley LTP1 protein that binds lipids and, thereby,
reduces their negative impact on the formation and stability of foam. In the
brewing process, LTP1 glycosylation and acylation occur, which increases
amphiphilicity and the surfactant properties of the protein
[<xref rid="R75" ref-type="bibr">75</xref>
]. LTP1b, a
LTP1-9(<italic>S</italic>
),10-epoxy-10,12(<italic>Z</italic>
)-octadecadienoic
acid covalent complex, forms during fermentation, which was mentioned above
[<xref rid="R107" ref-type="bibr">107</xref>
]. LTP1 and LTP1b are resistant to
high temperatures and retain their structure and ability to interact with
lipids upon heating during beer pasteurization. It should be noted that LTP1,
unlike LTP1b, has antifungal activity, inhibits growth of yeast, and,
therefore, can adversely affect the fermentation process. Therefore, LTP1b
formation and the equilibrium between free and lipid- bound forms of LTP1 in
beer are important for brewing high-quality barley beer.
</p>
<p><bold>Generation of viable transgenic plants</bold>
</p>
<p>Of high interest is the possibility of using LTPs for generating transgenic
plants resistant to various abiotic and biotic stress factors. Transgenic
plants carrying LTP genes possess enhanced resistance to phytopathogenic
microorganisms [<xref rid="R108" ref-type="bibr">108</xref>
], pests
[<xref rid="R73" ref-type="bibr">73</xref>
], high temperatures
[<xref rid="R109" ref-type="bibr">109</xref>
], soil salinity
[<xref rid="R108" ref-type="bibr">108</xref>
], drought
[<xref rid="R110" ref-type="bibr">110</xref>
], etc.
</p>
<p><bold>LTPs in allergology</bold>
</p>
<p>Another promising application for natural and recombinant plant LTPs is the
development of modern test systems for component-resolved allergy diagnostics
and vaccines for preventive allergen-specific immunotherapy (ASIT).
</p>
<p>The main methods of allergy diagnostics include skin-provocative tests and
elimination diet, together with enzyme immunoassay or immunofluorescent
analysis aimed at assessing the total and specific IgE and IgG antibodies
levels. Classical allergy diagnostics uses crude allergen extracts yielding
poorly reproducible, and sometimes even false, results due to the lack of a
possibility to standardize them and fluctuations in the content of allergenic
proteins and non-protein components. The current direction in allergy
diagnostics development is based on the replacement of crude extracts by
individual allergic components, which can be used to produce a molecular
profile of the patient’s sensitivity and to study cross-reactivity
[<xref rid="R111" ref-type="bibr">111</xref>
]. Modern microarray-based test systems
designed for component- resolved diagnostics use several natural and
recombinant pollen (mugwort Art v 3, plane tree Pla a 3, pellitory Par j 2, and
olive Ole e 7) and food (peach Pru p 3, hazel Cor a 8, walnut Jug r 3, peanut
Ara h 9, and wheat Tri a 14) allergenic LTPs.
</p>
<p>A modern method for reducing the reactivity of an organism is allergen-specific
immunotherapy (ASIT), where the patient is administered gradually increased
allergen doses [<xref rid="R112" ref-type="bibr">112</xref>
]. However,
classical ASIT uses crude extracts or allergoids that have a low efficacy and a
high risk of systemic allergic reactions. The most safe and promising ASIT
approach involves the design and development of vaccines on the basis of
individual natural and recombinant allergens and their hypoallergenic analogs.
These analogs should have low allergenicity but quite high immunogenicity to
avoid adverse allergic reactions and reduce the hypersensitivity for a long
time [<xref rid="R113" ref-type="bibr">113</xref>
]. Hypoallergenic forms are
developed mainly using methods of rational design and site-directed mutagenesis
by replacing amino acid residues constituting B-cell epitopes. To date, several
hypoallergenic analogs of major pollen and food allergens from different
classes are undergoing clinical trials [<xref rid="R114" ref-type="bibr">114</xref>
].
So far, hypoallergenic forms of some plant LTPs have been produced: e.g.,
pellitory Par j 2 [<xref rid="R115" ref-type="bibr">115</xref>
]
and peach Pru p 3 [<xref rid="R116" ref-type="bibr">116</xref>
].
However, there are no vaccines on the basis of hypoallergenic
forms of plant LTPs among the drugs under clinical trials.
</p>
</sec>
<sec><title>CONCLUSION</title>
<p>LTPs are widespread in the plant kingdom and present in almost all plant
tissues and organs, have intraor extracellular localization, and play an
important physiological role. LTPs encoded by a multigene family in plants are
represented by a set of multiple isoforms differentially expressed in various
tissues and organs under the influence of various stress environmental factors.
In addition, various LTP-like proteins with very different structures and
functional activities have been found in plants. The emergence of multiple
isoforms of LTPs and LTP-like proteins during evolution is assumed to result
from the need to expand the range of functions of these proteins.
</p>
<p>The biological role of LTPs in plants is poorly understood. LTPs have been
demonstrated to be involved in many processes, which might be largely
associated with their ability to bind and transfer a variety of lipid molecules.
</p>
<p>LTPs have been reliably ascertained to belong to molecular factors of the plant
innate immune system. As components of the PRP family, LTPs belong to the plant
defense system that enables them to adapt quickly and survive under stress
conditions. The defense function of LTPs is associated with their antimicrobial
activity and ability to inhibit foreign enzymes, involvement in the transfer of
signaling mediators and protective and building lipids, as well as with their
properties as endogenous elicitors whose complexes with lipids are recognized
by specific receptors and trigger an immune response.
</p>
<p>LTPs play an important role in human life. Their widespread occurrence and a
similar spatial organization make these proteins one of the most important
classes of cross-reactive plant allergens that are a frequent cause of allergic
reactions of varying severity. Their surfactant and allergenic properties, as
well as the LTP ability to bind and transfer hydrophobic ligands, make it
possible to use these proteins in pharmacy for designing drug and cosmetic
agent delivery systems; in allergology, for developing modern diagnostic test
kits and vaccines for ASIT; in the food industry, for brewing high-quality
beers; and in agriculture, for generating stress-resistant plants.
</p>
</sec>
</body>
<back><ack><p>This work was supported by the Russian Science Foundation (project No.
14-50-00131).
</p>
</ack>
<glossary><def-list><title>Abbreviations</title>
<def-item><term id="G01">LTP</term>
<def><p>lipid transfer protein</p>
</def>
</def-item>
<def-item><term id="G02">FA</term>
<def><p>fatty acid</p>
</def>
</def-item>
<def-item><term id="G03">PC</term>
<def><p>phosphatidylcholine</p>
</def>
</def-item>
<def-item><term id="G04">PI</term>
<def><p>phosphatidylinositol;</p>
</def>
</def-item>
<def-item><term id="G05">PG</term>
<def><p>phosphatidylglycerol</p>
</def>
</def-item>
<def-item><term id="G06">PRP</term>
<def><p>pathogenesis-related protein</p>
</def>
</def-item>
<def-item><term id="G07">AMP</term>
<def><p>antimicrobial peptide</p>
</def>
</def-item>
<def-item><term id="G08">PAMP</term>
<def><p>pathogen associated molecular pattern</p>
</def>
</def-item>
<def-item><term id="G09">DAMP</term>
<def><p>damage associated molecular pattern</p>
</def>
</def-item>
<def-item><term id="G10">GPI anchor</term>
<def><p>glycosylphosphatidylinositol anchor</p>
</def>
</def-item>
<def-item><term id="G11">ROS</term>
<def><p>reactive oxygen species</p>
</def>
</def-item>
<def-item><term id="G12">SAR</term>
<def><p>systemic acquired resistance</p>
</def>
</def-item>
<def-item><term id="G13">HR</term>
<def><p>hypersensitive response</p>
</def>
</def-item>
<def-item><term id="G14">ASIT</term>
<def><p>allergen-specific immunotherapy</p>
</def>
</def-item>
</def-list>
</glossary>
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