Glycans as receptors for influenza pathogenesis
Identifieur interne : 001414 ( Istex/Corpus ); précédent : 001413; suivant : 001415Glycans as receptors for influenza pathogenesis
Auteurs : Karthik Viswanathan ; Aarthi Chandrasekaran ; Aravind Srinivasan ; Rahul Raman ; V. Sasisekharan ; Ram SasisekharanSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 2010-08-01.
English descriptors
Abstract
Abstract: Influenza A viruses, members of the Orthomyxoviridae family, are responsible for annual seasonal influenza epidemics and occasional global pandemics. The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis.
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DOI: 10.1007/s10719-010-9303-4
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Sasisekharan</name><affiliation><mods:affiliation>Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</mods:affiliation></affiliation></author><author><name sortKey="Sasisekharan, Ram" sort="Sasisekharan, Ram" uniqKey="Sasisekharan R" first="Ram" last="Sasisekharan">Ram Sasisekharan</name><affiliation><mods:affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Koch Institute of Cancer Research, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: rams@mit.edu</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Glycoconjugate Journal</title><title level="j" type="sub">Official Journal of the International Glycoconjugate Organization</title><title level="j" type="abbrev">Glycoconj J</title><idno type="ISSN">0282-0080</idno><idno type="eISSN">1573-4986</idno><imprint><publisher>Springer US; http://www.springer-ny.com</publisher><pubPlace>Boston</pubPlace><date type="published" when="2010-08-01">2010-08-01</date><biblScope unit="volume">27</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="561">561</biblScope><biblScope unit="page" to="570">570</biblScope></imprint><idno type="ISSN">0282-0080</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0282-0080</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Glycan binding preference</term><term>Hemagglutinin</term><term>Multivalency</term><term>Sialylated glyans</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Influenza A viruses, members of the Orthomyxoviridae family, are responsible for annual seasonal influenza epidemics and occasional global pandemics. The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Karthik Viswanathan</name><affiliations><json:string>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</json:string></affiliations></json:item><json:item><name>Aarthi Chandrasekaran</name><affiliations><json:string>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</json:string></affiliations></json:item><json:item><name>Aravind Srinivasan</name><affiliations><json:string>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</json:string></affiliations></json:item><json:item><name>Rahul Raman</name><affiliations><json:string>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</json:string></affiliations></json:item><json:item><name>V. 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The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. 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Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Hemagglutinin</term></item><item><term>Multivalency</term></item><item><term>Sialylated glyans</term></item><item><term>Glycan binding preference</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Pathology</term></item><item><term>Biochemistry, general</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2008-06-10">Created</change><change 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REVIEW</ArticleCategory><ArticleFirstPage>561</ArticleFirstPage><ArticleLastPage>570</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2010</Year><Month>7</Month><Day>19</Day></RegistrationDate><Received><Year>2008</Year><Month>6</Month><Day>10</Day></Received><Revised><Year>2008</Year><Month>10</Month><Day>15</Day></Revised><Accepted><Year>2010</Year><Month>7</Month><Day>18</Day></Accepted><OnlineDate><Year>2010</Year><Month>8</Month><Day>24</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer Science+Business Media, LLC</CopyrightHolderName><CopyrightYear>2010</CopyrightYear></ArticleCopyright><ArticleGrants Type="OpenChoice"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="OpenAccess"></BodyPDFGrant><BodyHTMLGrant Grant="OpenAccess"></BodyHTMLGrant><BibliographyGrant Grant="OpenAccess"></BibliographyGrant><ESMGrant Grant="OpenAccess"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Karthik</GivenName><FamilyName>Viswanathan</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Aarthi</GivenName><FamilyName>Chandrasekaran</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Aravind</GivenName><FamilyName>Srinivasan</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Rahul</GivenName><FamilyName>Raman</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>V.</GivenName><FamilyName>Sasisekharan</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff2 Aff3" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Ram</GivenName><FamilyName>Sasisekharan</FamilyName></AuthorName><Contact><Email>rams@mit.edu</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Department of Biological Engineering</OrgDivision><OrgName>Massachusetts Institute of Technology</OrgName><OrgAddress><City>Cambridge</City><State>MA</State><Postcode>02139</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Harvard-MIT Division of Health Sciences and Technology</OrgDivision><OrgName>Massachusetts Institute of Technology</OrgName><OrgAddress><City>Cambridge</City><State>MA</State><Postcode>02139</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Koch Institute of Cancer Research</OrgDivision><OrgName>Massachusetts Institute of Technology</OrgName><OrgAddress><City>Cambridge</City><State>MA</State><Postcode>02139</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>Influenza A viruses, members of the <Emphasis Type="Italic">Orthomyxoviridae</Emphasis> family, are responsible for annual seasonal influenza epidemics and occasional global pandemics. The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic <Emphasis Type="Italic">umbrella-like</Emphasis> structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis.</Para></Abstract><KeywordGroup Language="En" OutputMedium="All"><Heading>Keywords</Heading><Keyword>Hemagglutinin</Keyword><Keyword>Multivalency</Keyword><Keyword>Sialylated glyans</Keyword><Keyword>Glycan binding preference</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Glycans as receptors for influenza pathogenesis</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Glycans as receptors for influenza pathogenesis</title></titleInfo><name type="personal"><namePart type="given">Karthik</namePart><namePart type="family">Viswanathan</namePart><affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Aarthi</namePart><namePart type="family">Chandrasekaran</namePart><affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Aravind</namePart><namePart type="family">Srinivasan</namePart><affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Rahul</namePart><namePart type="family">Raman</namePart><affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.</namePart><namePart type="family">Sasisekharan</namePart><affiliation>Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Ram</namePart><namePart type="family">Sasisekharan</namePart><affiliation>Department of Biological Engineering, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><affiliation>Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><affiliation>Koch Institute of Cancer Research, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA</affiliation><affiliation>E-mail: rams@mit.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Springer US; http://www.springer-ny.com</publisher><place><placeTerm type="text">Boston</placeTerm></place><dateCreated encoding="w3cdtf">2008-06-10</dateCreated><dateIssued encoding="w3cdtf">2010-08-01</dateIssued><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Influenza A viruses, members of the Orthomyxoviridae family, are responsible for annual seasonal influenza epidemics and occasional global pandemics. The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis.</abstract><note>MINI REVIEW</note><subject lang="en"><genre>Keywords</genre><topic>Hemagglutinin</topic><topic>Multivalency</topic><topic>Sialylated glyans</topic><topic>Glycan binding preference</topic></subject><relatedItem type="host"><titleInfo><title>Glycoconjugate Journal</title><subTitle>Official Journal of the International Glycoconjugate Organization</subTitle></titleInfo><titleInfo type="abbreviated"><title>Glycoconj J</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2010-08-15</dateIssued><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Pathology</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0282-0080</identifier><identifier type="eISSN">1573-4986</identifier><identifier type="JournalID">10719</identifier><identifier type="IssueArticleCount">7</identifier><identifier type="VolumeIssueCount">9</identifier><part><date>2010</date><detail type="volume"><number>27</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="pages"><start>561</start><end>570</end></extent></part><recordInfo><recordOrigin>Springer Science+Business Media, LLC, 2010</recordOrigin></recordInfo></relatedItem><identifier type="istex">E721B9E52365DCC9457BC53443E369F23A724ED9</identifier><identifier type="ark">ark:/67375/VQC-JTRDCDL3-B</identifier><identifier type="DOI">10.1007/s10719-010-9303-4</identifier><identifier type="ArticleID">9303</identifier><identifier type="ArticleID">s10719-010-9303-4</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer Science+Business Media, LLC, 2010</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer Science+Business Media, LLC, 2010</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-JTRDCDL3-B/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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