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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga <italic>Boodlea coacta</italic>
Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Sato, Yuichiro" sort="Sato, Yuichiro" uniqKey="Sato Y" first="Yuichiro" last="Sato">Yuichiro Sato</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hirayama, Makoto" sort="Hirayama, Makoto" uniqKey="Hirayama M" first="Makoto" last="Hirayama">Makoto Hirayama</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Morimoto, Kinjiro" sort="Morimoto, Kinjiro" uniqKey="Morimoto K" first="Kinjiro" last="Morimoto">Kinjiro Morimoto</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Okuyama, Satomi" sort="Okuyama, Satomi" uniqKey="Okuyama S" first="Satomi" last="Okuyama">Satomi Okuyama</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hori, Kanji" sort="Hori, Kanji" uniqKey="Hori K" first="Kanji" last="Hori">Kanji Hori</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">21460211</idno>
<idno type="pmc">3103324</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3103324</idno>
<idno type="RBID">PMC:3103324</idno>
<idno type="doi">10.1074/jbc.M110.216655</idno>
<date when="2011">2011</date>
<idno type="wicri:Area/Pmc/Corpus">000442</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000442</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga <italic>Boodlea coacta</italic>
Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Sato, Yuichiro" sort="Sato, Yuichiro" uniqKey="Sato Y" first="Yuichiro" last="Sato">Yuichiro Sato</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hirayama, Makoto" sort="Hirayama, Makoto" uniqKey="Hirayama M" first="Makoto" last="Hirayama">Makoto Hirayama</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Morimoto, Kinjiro" sort="Morimoto, Kinjiro" uniqKey="Morimoto K" first="Kinjiro" last="Morimoto">Kinjiro Morimoto</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Okuyama, Satomi" sort="Okuyama, Satomi" uniqKey="Okuyama S" first="Satomi" last="Okuyama">Satomi Okuyama</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hori, Kanji" sort="Hori, Kanji" uniqKey="Hori K" first="Kanji" last="Hori">Kanji Hori</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2011">2011</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The complete amino acid sequence of a lectin from the green alga <italic>Boodlea coacta</italic>
(BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed the following: 1) <italic>B. coacta</italic>
used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and 2) BCA consisted of three internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of <italic>Galanthus nivalis</italic>
agglutinin-related lectins. Carbohydrate binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type <italic>N</italic>
-glycans but not to the complex-type, hybrid-type core structure of <italic>N</italic>
-glycans or oligosaccharides from glycolipids. This lectin had exclusive specificity for α1–2-linked mannose at the nonreducing terminus. The binding activity was enhanced as the number of terminal α1–2-linked mannose substitutions increased. Mannobiose, mannotriose, and mannopentaose were incapable of binding to BCA. Thus, BCA preferentially recognized the nonreducing terminal α1–2-mannose cluster as a primary target. As predicted from carbohydrate-binding propensity, this lectin inhibited the HIV-1 entry into the host cells at a half-maximal effective concentration of 8.2 n<sc>m</sc>
. A high association constant (3.71 × 10<sup>8</sup>
<sc>m</sc>
<sup>−1</sup>
) of BCA with the HIV envelope glycoprotein gp120 was demonstrated by surface plasmon resonance analysis. Moreover, BCA showed the potent anti-influenza activity by directly binding to viral envelope hemagglutinin against various strains, including a clinical isolate of pandemic H1N1-2009 virus, revealing its potential as an antiviral reagent.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">21460211</article-id>
<article-id pub-id-type="pmc">3103324</article-id>
<article-id pub-id-type="publisher-id">M110.216655</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M110.216655</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Glycobiology and Extracellular Matrices</subject>
</subj-group>
</article-categories>
<title-group><article-title>High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga <italic>Boodlea coacta</italic>
Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
<alt-title alt-title-type="short">Antiviral Activity of High Mannose-binding Green Algal Lectin</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Sato</surname>
<given-names>Yuichiro</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hirayama</surname>
<given-names>Makoto</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Morimoto</surname>
<given-names>Kinjiro</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yamamoto</surname>
<given-names>Naoki</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>¶</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Okuyama</surname>
<given-names>Satomi</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hori</surname>
<given-names>Kanji</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>2</sup>
</xref>
</contrib>
<aff id="aff1">From the<label>‡</label>
Faculty of Pharmacy, Yasuda Women's University, 6-13-1 Yasuhigashi, Asaminami, Hiroshima 731-0153, Japan,</aff>
<aff id="aff2">the<label>§</label>
Graduate School of Biosphere Science, Hiroshima University, Kagamiyama 1-4-4, Higashi-Hiroshima 739-8528, Japan, and</aff>
<aff id="aff3">the<label>¶</label>
Department of Microbiology, Yong Loo Lin School of Medicine, National University of Singapore, 5 Science Drive 2, Block MD4A, Level 5, 117597 Singapore</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>2</label>
To whom correspondence should be addressed: <addr-line>Graduate School of Biosphere Science, Hiroshima University, Kagamiyama 1-4-4, Higashi-Hiroshima 739-8528, Japan.</addr-line>
Tel.: <phone>81-82-424-7931</phone>
; Fax: <fax>81-82-424-7931</fax>
; E-mail: <email>kanhori@hiroshima-u.ac.jp</email>
.</corresp>
<fn fn-type="equal" id="FN3"><label>1</label>
<p>Both authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><day>3</day>
<month>6</month>
<year>2011</year>
</pub-date>
<pub-date pub-type="epub"><day>1</day>
<month>4</month>
<year>2011</year>
</pub-date>
<volume>286</volume>
<issue>22</issue>
<fpage>19446</fpage>
<lpage>19458</lpage>
<history><date date-type="received"><day>27</day>
<month>12</month>
<year>2010</year>
</date>
<date date-type="rev-recd"><day>22</day>
<month>3</month>
<year>2011</year>
</date>
</history>
<permissions><copyright-statement>© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<copyright-year>2011</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc02211019446.pdf"></self-uri>
<abstract><p>The complete amino acid sequence of a lectin from the green alga <italic>Boodlea coacta</italic>
(BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed the following: 1) <italic>B. coacta</italic>
used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and 2) BCA consisted of three internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of <italic>Galanthus nivalis</italic>
agglutinin-related lectins. Carbohydrate binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type <italic>N</italic>
-glycans but not to the complex-type, hybrid-type core structure of <italic>N</italic>
-glycans or oligosaccharides from glycolipids. This lectin had exclusive specificity for α1–2-linked mannose at the nonreducing terminus. The binding activity was enhanced as the number of terminal α1–2-linked mannose substitutions increased. Mannobiose, mannotriose, and mannopentaose were incapable of binding to BCA. Thus, BCA preferentially recognized the nonreducing terminal α1–2-mannose cluster as a primary target. As predicted from carbohydrate-binding propensity, this lectin inhibited the HIV-1 entry into the host cells at a half-maximal effective concentration of 8.2 n<sc>m</sc>
. A high association constant (3.71 × 10<sup>8</sup>
<sc>m</sc>
<sup>−1</sup>
) of BCA with the HIV envelope glycoprotein gp120 was demonstrated by surface plasmon resonance analysis. Moreover, BCA showed the potent anti-influenza activity by directly binding to viral envelope hemagglutinin against various strains, including a clinical isolate of pandemic H1N1-2009 virus, revealing its potential as an antiviral reagent.</p>
</abstract>
<kwd-group><kwd>Antiviral Agents</kwd>
<kwd>Carbohydrate-binding Protein</kwd>
<kwd>Gene Structure</kwd>
<kwd>HIV</kwd>
<kwd>Lectin</kwd>
<kwd>Oligosaccharide</kwd>
<kwd>Protein Domains</kwd>
<kwd>Virus Entry</kwd>
<kwd>Carbohydrate Binding Specificity</kwd>
<kwd>Genetic Code</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>
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