Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.
Identifieur interne : 000381 ( Main/Exploration ); précédent : 000380; suivant : 000382Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.
Auteurs : Philippe Leone [France] ; Laurence Menu-Bouaouiche ; Willy J. Peumans ; Françoise Payan ; Annick Barre ; Alain Roussel ; Els J M. Van Damme ; Pierre RougéSource :
- Biochimie [ 0300-9084 ] ; 2006.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Allergènes (composition chimique), Antifongiques (composition chimique), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Immunoglobuline E (composition chimique), Modèles moléculaires (MeSH), Protéines végétales (composition chimique), Séquence d'acides aminés (MeSH), Épitopes (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
Abstract
The structure of a thaumatin-like protein from banana (Musa acuminata) fruit, an allergen with antifungal properties, was solved at 1.7-A-resolution, by X-ray crystallography. Though the banana protein exhibits a very similar overall fold as thaumatin it markedly differs from the sweet-tasting protein by the presence of a surface exposed electronegative cleft. Due to the presence of this electronegative cleft, the banana thaumatin-like protein (Ban-TLP) acquires a strong (local) electronegative character that eventually explains the observed antifungal activity. Our structural analysis also revealed the presence of conserved residues of exposed epitopic determinants that are presumably responsible for the allergenic properties of banana fruit towards susceptible individuals, and provided evidence that the Ban-TLP shares some structurally highly conserved IgE-binding epitopes with thaumatin-like proteins from fruits or pollen from other plants. In addition, some overlap was detected between the predicted IgE-binding epitopes of the Ban-TLP and IgE-binding epitopes previously identified in the mountain cedar Jun a 3 TLP aeroallergen. The presence of these common epitopes offers a molecular basis for the cross-reactivity between aeroallergens and fruit allergens.
DOI: 10.1016/j.biochi.2005.07.001
PubMed: 16085352
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.</title><author><name sortKey="Leone, Philippe" sort="Leone, Philippe" uniqKey="Leone P" first="Philippe" last="Leone">Philippe Leone</name><affiliation wicri:level="3"><nlm:affiliation>Architecture et fonction des macromolécules biologiques, UMR-CNRS, 31, chemin Joseph-Aiguier, 13402 Marseille cedex 20, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Architecture et fonction des macromolécules biologiques, UMR-CNRS, 31, chemin Joseph-Aiguier, 13402 Marseille cedex 20</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Menu Bouaouiche, Laurence" sort="Menu Bouaouiche, Laurence" uniqKey="Menu Bouaouiche L" first="Laurence" last="Menu-Bouaouiche">Laurence Menu-Bouaouiche</name></author><author><name sortKey="Peumans, Willy J" sort="Peumans, Willy J" uniqKey="Peumans W" first="Willy J" last="Peumans">Willy J. Peumans</name></author><author><name sortKey="Payan, Francoise" sort="Payan, Francoise" uniqKey="Payan F" first="Françoise" last="Payan">Françoise Payan</name></author><author><name sortKey="Barre, Annick" sort="Barre, Annick" uniqKey="Barre A" first="Annick" last="Barre">Annick Barre</name></author><author><name sortKey="Roussel, Alain" sort="Roussel, Alain" uniqKey="Roussel A" first="Alain" last="Roussel">Alain Roussel</name></author><author><name sortKey="Van Damme, Els J M" sort="Van Damme, Els J M" uniqKey="Van Damme E" first="Els J M" last="Van Damme">Els J M. Van Damme</name></author><author><name sortKey="Rouge, Pierre" sort="Rouge, Pierre" uniqKey="Rouge P" first="Pierre" last="Rougé">Pierre Rougé</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16085352</idno><idno type="pmid">16085352</idno><idno type="doi">10.1016/j.biochi.2005.07.001</idno><idno type="wicri:Area/Main/Corpus">000413</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000413</idno><idno type="wicri:Area/Main/Curation">000413</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000413</idno><idno type="wicri:Area/Main/Exploration">000413</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.</title><author><name sortKey="Leone, Philippe" sort="Leone, Philippe" uniqKey="Leone P" first="Philippe" last="Leone">Philippe Leone</name><affiliation wicri:level="3"><nlm:affiliation>Architecture et fonction des macromolécules biologiques, UMR-CNRS, 31, chemin Joseph-Aiguier, 13402 Marseille cedex 20, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Architecture et fonction des macromolécules biologiques, UMR-CNRS, 31, chemin Joseph-Aiguier, 13402 Marseille cedex 20</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Menu Bouaouiche, Laurence" sort="Menu Bouaouiche, Laurence" uniqKey="Menu Bouaouiche L" first="Laurence" last="Menu-Bouaouiche">Laurence Menu-Bouaouiche</name></author><author><name sortKey="Peumans, Willy J" sort="Peumans, Willy J" uniqKey="Peumans W" first="Willy J" last="Peumans">Willy J. Peumans</name></author><author><name sortKey="Payan, Francoise" sort="Payan, Francoise" uniqKey="Payan F" first="Françoise" last="Payan">Françoise Payan</name></author><author><name sortKey="Barre, Annick" sort="Barre, Annick" uniqKey="Barre A" first="Annick" last="Barre">Annick Barre</name></author><author><name sortKey="Roussel, Alain" sort="Roussel, Alain" uniqKey="Roussel A" first="Alain" last="Roussel">Alain Roussel</name></author><author><name sortKey="Van Damme, Els J M" sort="Van Damme, Els J M" uniqKey="Van Damme E" first="Els J M" last="Van Damme">Els J M. Van Damme</name></author><author><name sortKey="Rouge, Pierre" sort="Rouge, Pierre" uniqKey="Rouge P" first="Pierre" last="Rougé">Pierre Rougé</name></author></analytic><series><title level="j">Biochimie</title><idno type="ISSN">0300-9084</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allergens (chemistry)</term><term>Amino Acid Sequence (MeSH)</term><term>Antifungal Agents (chemistry)</term><term>Crystallization (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Epitopes (MeSH)</term><term>Immunoglobulin E (chemistry)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Allergènes (composition chimique)</term><term>Antifongiques (composition chimique)</term><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Immunoglobuline E (composition chimique)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Épitopes (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Allergens</term><term>Antifungal Agents</term><term>Immunoglobulin E</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Allergènes</term><term>Antifongiques</term><term>Immunoglobuline E</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Epitopes</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The structure of a thaumatin-like protein from banana (Musa acuminata) fruit, an allergen with antifungal properties, was solved at 1.7-A-resolution, by X-ray crystallography. Though the banana protein exhibits a very similar overall fold as thaumatin it markedly differs from the sweet-tasting protein by the presence of a surface exposed electronegative cleft. Due to the presence of this electronegative cleft, the banana thaumatin-like protein (Ban-TLP) acquires a strong (local) electronegative character that eventually explains the observed antifungal activity. Our structural analysis also revealed the presence of conserved residues of exposed epitopic determinants that are presumably responsible for the allergenic properties of banana fruit towards susceptible individuals, and provided evidence that the Ban-TLP shares some structurally highly conserved IgE-binding epitopes with thaumatin-like proteins from fruits or pollen from other plants. In addition, some overlap was detected between the predicted IgE-binding epitopes of the Ban-TLP and IgE-binding epitopes previously identified in the mountain cedar Jun a 3 TLP aeroallergen. The presence of these common epitopes offers a molecular basis for the cross-reactivity between aeroallergens and fruit allergens.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16085352</PMID><DateCompleted><Year>2006</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0300-9084</ISSN><JournalIssue CitedMedium="Print"><Volume>88</Volume><Issue>1</Issue><PubDate><Year>2006</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Biochimie</Title><ISOAbbreviation>Biochimie</ISOAbbreviation></Journal><ArticleTitle>Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.</ArticleTitle><Pagination><MedlinePgn>45-52</MedlinePgn></Pagination><Abstract><AbstractText>The structure of a thaumatin-like protein from banana (Musa acuminata) fruit, an allergen with antifungal properties, was solved at 1.7-A-resolution, by X-ray crystallography. Though the banana protein exhibits a very similar overall fold as thaumatin it markedly differs from the sweet-tasting protein by the presence of a surface exposed electronegative cleft. Due to the presence of this electronegative cleft, the banana thaumatin-like protein (Ban-TLP) acquires a strong (local) electronegative character that eventually explains the observed antifungal activity. Our structural analysis also revealed the presence of conserved residues of exposed epitopic determinants that are presumably responsible for the allergenic properties of banana fruit towards susceptible individuals, and provided evidence that the Ban-TLP shares some structurally highly conserved IgE-binding epitopes with thaumatin-like proteins from fruits or pollen from other plants. In addition, some overlap was detected between the predicted IgE-binding epitopes of the Ban-TLP and IgE-binding epitopes previously identified in the mountain cedar Jun a 3 TLP aeroallergen. The presence of these common epitopes offers a molecular basis for the cross-reactivity between aeroallergens and fruit allergens.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Leone</LastName><ForeName>Philippe</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Architecture et fonction des macromolécules biologiques, UMR-CNRS, 31, chemin Joseph-Aiguier, 13402 Marseille cedex 20, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Menu-Bouaouiche</LastName><ForeName>Laurence</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Peumans</LastName><ForeName>Willy J</ForeName><Initials>WJ</Initials></Author><Author ValidYN="Y"><LastName>Payan</LastName><ForeName>Françoise</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Barre</LastName><ForeName>Annick</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Roussel</LastName><ForeName>Alain</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Van Damme</LastName><ForeName>Els J M</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Rougé</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>08</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Biochimie</MedlineTA><NlmUniqueID>1264604</NlmUniqueID><ISSNLinking>0300-9084</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000485">Allergens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C420118">thaumatin-like protein, Musa acuminata</NameOfSubstance></Chemical><Chemical><RegistryNumber>37341-29-0</RegistryNumber><NameOfSubstance UI="D007073">Immunoglobulin E</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000485" MajorTopicYN="N">Allergens</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007073" MajorTopicYN="N">Immunoglobulin E</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>07</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>8</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>2</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>8</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16085352</ArticleId><ArticleId IdType="pii">S0300-9084(05)00177-X</ArticleId><ArticleId IdType="doi">10.1016/j.biochi.2005.07.001</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><noCountry><name sortKey="Barre, Annick" sort="Barre, Annick" uniqKey="Barre A" first="Annick" last="Barre">Annick Barre</name><name sortKey="Menu Bouaouiche, Laurence" sort="Menu Bouaouiche, Laurence" uniqKey="Menu Bouaouiche L" first="Laurence" last="Menu-Bouaouiche">Laurence Menu-Bouaouiche</name><name sortKey="Payan, Francoise" sort="Payan, Francoise" uniqKey="Payan F" first="Françoise" last="Payan">Françoise Payan</name><name sortKey="Peumans, Willy J" sort="Peumans, Willy J" uniqKey="Peumans W" first="Willy J" last="Peumans">Willy J. Peumans</name><name sortKey="Rouge, Pierre" sort="Rouge, Pierre" uniqKey="Rouge P" first="Pierre" last="Rougé">Pierre Rougé</name><name sortKey="Roussel, Alain" sort="Roussel, Alain" uniqKey="Roussel A" first="Alain" last="Roussel">Alain Roussel</name><name sortKey="Van Damme, Els J M" sort="Van Damme, Els J M" uniqKey="Van Damme E" first="Els J M" last="Van Damme">Els J M. Van Damme</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Leone, Philippe" sort="Leone, Philippe" uniqKey="Leone P" first="Philippe" last="Leone">Philippe Leone</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/ThaumatinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000381 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000381 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= ThaumatinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:16085352
|texte= Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16085352" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a ThaumatinV1
| This area was generated with Dilib version V0.6.37. |  |