Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis
Identifieur interne : 000999 ( Main/Exploration ); précédent : 000998; suivant : 000A00Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis
Auteurs : Wentian Chen [République populaire de Chine] ; Shisheng Sun [États-Unis] ; Zheng Li [République populaire de Chine]Source :
- PLoS ONE [ 1932-6203 ] ; 2012.
Abstract
Increasing numbers of H5N1 influenza viruses (IVs) are responsible for human deaths, especially in North Africa and Southeast Asian. The binding of hemagglutinin (HA) on the viral surface to host sialic acid (SA) receptors is a requisite step in the infection process. Phylogenetic analysis reveals that H5N1 viruses can be divided into 10 clades based on their HA sequences, with most human IVs centered from clade 1 and clade 2.1 to clade 2.3. Protein sequence alignment in various clades indicates the high conservation in the receptor-binding domains (RBDs) is essential for binding with the SA receptor. Two glycosylation sites, 158N and 169N, also participate in receptor recognition. In the present work, we attempted to construct a serial H5N1 HA models including diverse glycosylated HAs to simulate the binding process with various SA receptors
Url:
DOI: 10.1371/journal.pone.0038794
PubMed: 22719948
PubMed Central: 3375263
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis</title><author><name sortKey="Chen, Wentian" sort="Chen, Wentian" uniqKey="Chen W" first="Wentian" last="Chen">Wentian Chen</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, People’s Republic of China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an</wicri:regionArea><wicri:noRegion>Xi’an</wicri:noRegion></affiliation></author><author><name sortKey="Sun, Shisheng" sort="Sun, Shisheng" uniqKey="Sun S" first="Shisheng" last="Sun">Shisheng Sun</name><affiliation wicri:level="3"><nlm:aff id="aff2"><addr-line>Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore</wicri:regionArea><placeName><settlement type="city">Baltimore</settlement><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Li, Zheng" sort="Li, Zheng" uniqKey="Li Z" first="Zheng" last="Li">Zheng Li</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, People’s Republic of China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an</wicri:regionArea><wicri:noRegion>Xi’an</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno 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type="wicri:Area/Main/Exploration">000999</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis</title><author><name sortKey="Chen, Wentian" sort="Chen, Wentian" uniqKey="Chen W" first="Wentian" last="Chen">Wentian Chen</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, People’s Republic of China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an</wicri:regionArea><wicri:noRegion>Xi’an</wicri:noRegion></affiliation></author><author><name sortKey="Sun, Shisheng" sort="Sun, Shisheng" uniqKey="Sun S" first="Shisheng" last="Sun">Shisheng Sun</name><affiliation wicri:level="3"><nlm:aff id="aff2"><addr-line>Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore</wicri:regionArea><placeName><settlement type="city">Baltimore</settlement><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Li, Zheng" sort="Li, Zheng" uniqKey="Li Z" first="Zheng" last="Li">Zheng Li</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, People’s Republic of China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an</wicri:regionArea><wicri:noRegion>Xi’an</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Increasing numbers of H5N1 influenza viruses (IVs) are responsible for human deaths, especially in North Africa and Southeast Asian. The binding of hemagglutinin (HA) on the viral surface to host sialic acid (SA) receptors is a requisite step in the infection process. Phylogenetic analysis reveals that H5N1 viruses can be divided into 10 clades based on their HA sequences, with most human IVs centered from clade 1 and clade 2.1 to clade 2.3. Protein sequence alignment in various clades indicates the high conservation in the receptor-binding domains (RBDs) is essential for binding with the SA receptor. Two glycosylation sites, 158N and 169N, also participate in receptor recognition. In the present work, we attempted to construct a serial H5N1 HA models including diverse glycosylated HAs to simulate the binding process with various SA receptors <italic>in silico</italic>. As the SA-α-2,3-Gal and SA-α-2,6-Gal receptor adopted two distinctive topologies, straight and fishhook-like, respectively, the presence of N-glycans at 158N would decrease the affinity of HA for all of the receptors, particularly SA-α-2,6-Gal analogs. The steric clashes of the huge glycans shown at another glycosylation site, 169N, located on an adjacent HA monomer, would be more effective in preventing the binding of SA-α-2,3-Gal analogs.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Zachary, S" uniqKey="Zachary S">S Zachary</name></author><author><name sortKey="Rahul, R" uniqKey="Rahul R">R Rahul</name></author><author><name sortKey="Karthik, V" uniqKey="Karthik V">V Karthik</name></author><author><name sortKey="Ram, S" uniqKey="Ram S">S Ram</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Skehel, Jj" uniqKey="Skehel J">JJ Skehel</name></author><author><name sortKey="Wiley, Dc" uniqKey="Wiley D">DC Wiley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wiley, Dc" uniqKey="Wiley D">DC Wiley</name></author><author><name 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Rota</name></author><author><name sortKey="Oberste, Ms" uniqKey="Oberste M">MS Oberste</name></author><author><name sortKey="Monroe, Ss" uniqKey="Monroe S">SS Monroe</name></author><author><name sortKey="Nix, Wa" uniqKey="Nix W">WA Nix</name></author><author><name sortKey="Campagnoli, R" uniqKey="Campagnoli R">R Campagnoli</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Neu, U" uniqKey="Neu U">U Neu</name></author><author><name sortKey="Woellner, K" uniqKey="Woellner K">K Woellner</name></author><author><name sortKey="Gauglitz, G" uniqKey="Gauglitz G">G Gauglitz</name></author><author><name sortKey="Stehle, T" uniqKey="Stehle T">T Stehle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tsai, B" uniqKey="Tsai B">B Tsai</name></author><author><name sortKey="Gilbert, Jm" uniqKey="Gilbert J">JM Gilbert</name></author><author><name sortKey="Stehle, T" uniqKey="Stehle T">T Stehle</name></author><author><name sortKey="Lencer, W" uniqKey="Lencer W">W Lencer</name></author><author><name sortKey="Benjamin, Tl" uniqKey="Benjamin T">TL Benjamin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lin, T" uniqKey="Lin T">T Lin</name></author><author><name sortKey="Wang, G" uniqKey="Wang G">G Wang</name></author><author><name sortKey="Li, A" uniqKey="Li A">A Li</name></author><author><name sortKey="Zhang, Q" uniqKey="Zhang Q">Q Zhang</name></author><author><name sortKey="Wu, C" uniqKey="Wu C">C Wu</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>République populaire de Chine</li><li>États-Unis</li></country><region><li>Maryland</li></region><settlement><li>Baltimore</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Chen, Wentian" sort="Chen, Wentian" uniqKey="Chen W" first="Wentian" last="Chen">Wentian Chen</name></noRegion><name sortKey="Li, Zheng" sort="Li, Zheng" uniqKey="Li Z" first="Zheng" last="Li">Zheng Li</name></country><country name="États-Unis"><region name="Maryland"><name sortKey="Sun, Shisheng" sort="Sun, Shisheng" uniqKey="Sun S" first="Shisheng" last="Sun">Shisheng Sun</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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