Role of receptor binding specificity in influenza A virus transmission and pathogenesis
Identifieur interne : 000398 ( Istex/Corpus ); précédent : 000397; suivant : 000399Role of receptor binding specificity in influenza A virus transmission and pathogenesis
Auteurs : Miranda De Graaf ; Ron A M. FouchierSource :
- The EMBO Journal [ 0261-4189 ] ; 2014-04-16.
Abstract
The recent emergence of a novel avian A/H7N9 influenza virus in poultry and humans in China, as well as laboratory studies on adaptation and transmission of avian A/H5N1 influenza viruses, has shed new light on influenza virus adaptation to mammals. One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, in vitro assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (HA) protein. Avian and human influenza viruses typically have a different sialic acid (SA)‐binding preference and only few amino acid changes in the HA protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of HA have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus HA and SA receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.
Recent cases of humans carrying avian Influenza strains highlight the importance of unraveling the role of virus‐receptor interactions in cross‐species adaptation. de Graaf and Fouchier review how virus hemagglutinin binding to host receptors governs virus pathogenesis, transmission and host spectrum.
Url:
DOI: 10.1002/embj.201387442
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ISTEX:D850D247DF3F16806DCFF3C87D20704C5DCD9A0DLe document en format XML
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One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, in vitro assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (HA) protein. Avian and human influenza viruses typically have a different sialic acid (SA)‐binding preference and only few amino acid changes in the HA protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of HA have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus HA and SA receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.</div><div type="abstract">Recent cases of humans carrying avian Influenza strains highlight the importance of unraveling the role of virus‐receptor interactions in cross‐species adaptation. de Graaf and Fouchier review how virus hemagglutinin binding to host receptors governs virus pathogenesis, transmission and host spectrum.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Miranda de Graaf</name><affiliations><json:string>Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands</json:string></affiliations></json:item><json:item><name>Ron A M Fouchier</name><affiliations><json:string>Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands</json:string><json:string>E-mail: r.fouchier@erasmusmc.nl</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>A/H5N1 influenza virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>A/H7N9 influenza virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>airborne transmission</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>pathogenesis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>receptor binding specificity</value></json:item></subject><articleId><json:string>EMBJ201387442</json:string></articleId><arkIstex>ark:/67375/WNG-MN2HR12X-0</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>reviewArticle</json:string></originalGenre><abstract>The recent emergence of a novel avian A/H7N9 influenza virus in poultry and humans in China, as well as laboratory studies on adaptation and transmission of avian A/H5N1 influenza viruses, has shed new light on influenza virus adaptation to mammals. 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One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, <i>in vitro</i> assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (<fc>HA</fc>) protein. Avian and human influenza viruses typically have a different sialic acid (<fc>SA</fc>)‐binding preference and only few amino acid changes in the <fc>HA</fc> protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of <fc>HA</fc> have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus <fc>HA</fc> and <fc>SA</fc> receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.</p></abstract><abstract type="graphical" xml:id="embj201387442-abs-0002"><p>Recent cases of humans carrying avian Influenza strains highlight the importance of unraveling the role of virus‐receptor interactions in cross‐species adaptation. de Graaf and Fouchier review how virus hemagglutinin binding to host receptors governs virus pathogenesis, transmission and host spectrum.<blockFixed type="graphic" xml:id="embj201387442-blkfxd-0001"><mediaResourceGroup><mediaResource alt="image" href="urn:x-wiley:02614189:embj201387442:embj201387442-toc-0001"></mediaResource></mediaResourceGroup></blockFixed></p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Role of receptor binding specificity in influenza A virus transmission and pathogenesis</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Role of receptor binding specificity in influenza A virus transmission and pathogenesis</title></titleInfo><name type="personal"><namePart type="given">Miranda</namePart><namePart type="family">de Graaf</namePart><affiliation>Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ron A M</namePart><namePart type="family">Fouchier</namePart><affiliation>Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands</affiliation><affiliation>E-mail: r.fouchier@erasmusmc.nl</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2014-04-16</dateIssued><dateCreated encoding="w3cdtf">2014-02-26</dateCreated><dateCaptured encoding="w3cdtf">2013-11-19</dateCaptured><dateValid encoding="w3cdtf">2014-02-17</dateValid><edition>EMBO J (2014) 33, 823–841</edition><copyrightDate encoding="w3cdtf">2014</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract>The recent emergence of a novel avian A/H7N9 influenza virus in poultry and humans in China, as well as laboratory studies on adaptation and transmission of avian A/H5N1 influenza viruses, has shed new light on influenza virus adaptation to mammals. One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, in vitro assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (HA) protein. Avian and human influenza viruses typically have a different sialic acid (SA)‐binding preference and only few amino acid changes in the HA protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of HA have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus HA and SA receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.</abstract><abstract type="graphical">Recent cases of humans carrying avian Influenza strains highlight the importance of unraveling the role of virus‐receptor interactions in cross‐species adaptation. de Graaf and Fouchier review how virus hemagglutinin binding to host receptors governs virus pathogenesis, transmission and host spectrum.</abstract><note type="funding">EU FP7</note><note type="funding">ANTIGONE</note><note type="funding">EMPERIE</note><note type="funding">NIAID/NIH - No. HHSN266200700010C; </note><note type="funding">Intra European Marie Curie Fellowship - No. PIEF‐GA‐2009‐237505; </note><subject><genre>keywords</genre><topic>A/H5N1 influenza virus</topic><topic>A/H7N9 influenza virus</topic><topic>airborne transmission</topic><topic>pathogenesis</topic><topic>receptor binding specificity</topic></subject><relatedItem type="host"><titleInfo><title>The EMBO Journal</title></titleInfo><titleInfo type="abbreviated"><title>EMBO 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><subject><genre>index-terms</genre><topic authorityURI="http://psi.embo.org/14602075/EMBO23">Microbiology, Virology & Host Pathogen Interaction</topic></subject><subject><genre>article-category</genre><topic>Review</topic><topic>Reviews</topic></subject><identifier type="ISSN">0261-4189</identifier><identifier type="eISSN">1460-2075</identifier><identifier type="DOI">10.1002/(ISSN)1460-2075</identifier><identifier type="PublisherID">EMBJ</identifier><part><date>2014</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><detail type="issue"><caption>no.</caption><number>8</number></detail><extent unit="pages"><start>823</start><end>841</end><total>18</total></extent></part></relatedItem><relatedItem type="references" displayLabel="embj201387442-cit-0001"><titleInfo><title>Entry of influenza virus into a glycosphingolipid‐deficient mouse skin fibroblast cell line</title></titleInfo><name type="personal"><namePart type="given">S</namePart><namePart type="family">Ablan</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">SS</namePart><namePart type="family">Rawat</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R</namePart><namePart type="family">Blumenthal</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A</namePart><namePart type="family">Puri</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ablan S, Rawat SS, Blumenthal R, Puri A (2001) Entry of influenza virus into a glycosphingolipid‐deficient mouse skin fibroblast cell line. 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