High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga Boodlea coacta Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses*
Identifieur interne : 001395 ( Main/Exploration ); précédent : 001394; suivant : 001396High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga Boodlea coacta Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses*
Auteurs : Yuichiro Sato ; Makoto Hirayama ; Kinjiro Morimoto ; Naoki Yamamoto ; Satomi Okuyama ; Kanji HoriSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2011.
Abstract
The complete amino acid sequence of a lectin from the green alga
Url:
DOI: 10.1074/jbc.M110.216655
PubMed: 21460211
PubMed Central: 3103324
Affiliations:
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<author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name>
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<author><name sortKey="Okuyama, Satomi" sort="Okuyama, Satomi" uniqKey="Okuyama S" first="Satomi" last="Okuyama">Satomi Okuyama</name>
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<author><name sortKey="Hori, Kanji" sort="Hori, Kanji" uniqKey="Hori K" first="Kanji" last="Hori">Kanji Hori</name>
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<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>
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<author><name sortKey="Sato, Yuichiro" sort="Sato, Yuichiro" uniqKey="Sato Y" first="Yuichiro" last="Sato">Yuichiro Sato</name>
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<author><name sortKey="Hirayama, Makoto" sort="Hirayama, Makoto" uniqKey="Hirayama M" first="Makoto" last="Hirayama">Makoto Hirayama</name>
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<author><name sortKey="Morimoto, Kinjiro" sort="Morimoto, Kinjiro" uniqKey="Morimoto K" first="Kinjiro" last="Morimoto">Kinjiro Morimoto</name>
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<author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name>
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</affiliation>
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<author><name sortKey="Okuyama, Satomi" sort="Okuyama, Satomi" uniqKey="Okuyama S" first="Satomi" last="Okuyama">Satomi Okuyama</name>
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<author><name sortKey="Hori, Kanji" sort="Hori, Kanji" uniqKey="Hori K" first="Kanji" last="Hori">Kanji Hori</name>
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<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>
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<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>
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<affiliations><list></list>
<tree><noCountry><name sortKey="Hirayama, Makoto" sort="Hirayama, Makoto" uniqKey="Hirayama M" first="Makoto" last="Hirayama">Makoto Hirayama</name>
<name sortKey="Hori, Kanji" sort="Hori, Kanji" uniqKey="Hori K" first="Kanji" last="Hori">Kanji Hori</name>
<name sortKey="Morimoto, Kinjiro" sort="Morimoto, Kinjiro" uniqKey="Morimoto K" first="Kinjiro" last="Morimoto">Kinjiro Morimoto</name>
<name sortKey="Okuyama, Satomi" sort="Okuyama, Satomi" uniqKey="Okuyama S" first="Satomi" last="Okuyama">Satomi Okuyama</name>
<name sortKey="Sato, Yuichiro" sort="Sato, Yuichiro" uniqKey="Sato Y" first="Yuichiro" last="Sato">Yuichiro Sato</name>
<name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name>
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