The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
Identifieur interne : 001444 ( Istex/Corpus ); précédent : 001443; suivant : 001445The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?
Auteurs : Tony VelkovSource :
- Journal of Molecular Recognition [ 0952-3499 ] ; 2013-10.
English descriptors
- Teeft :
- Accession, Adaption, Amino, Analog, Asialyl, Asialyl sugars, Assay, Assay ganglioside, Avian, Avian receptor analog lsta, Avian receptor analogs, Binding data, Binding pocket, Carbone, Consensus model, Copyright, Crystal structure, Determinant, Elisa, Gambaryan, Ganagliosides, Ganglioside, Gangliosides, Genbank, Genbank accession, Glycan, Glycans, Glycosidic linkage, Glycosylation, Glycosylation site, Govorkova, Hemagglutinin, Hemagglutinin receptors, Hydrogen bonds, John wiley sons, Krystal, Lsta, Lstc, Lugovtsev, Matrosovich, Mdck, Mutation, Receptor, Receptor binding, Receptor binding characteristics, Receptor binding data, Receptor binding pocket, Receptor probe, Receptor recognition, Recognit, Saito, Selectivity, Side chain, Side chains, Strong preference, Sulfated, Suzuki, Velkov, Viral, Virol, Virology, Virus, Virus hemagglutinin, Wang.
Abstract
The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl‐glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg‐adapted variants. Overall, the review serves as an up‐to‐date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright © 2013 John Wiley & Sons, Ltd.
It remains contentious whether the influenza B hemagglutinin (HA) preferentially binds to α2,6‐linked human type receptors or equally well to α2,3‐linked type avian receptors, and how or if in fact any receptor selectivity plays a role in the viruses infectivity of humans. For the first time, the present review forms a treatise that unifies the receptor binding data and provides a consensus for the modalities that determine the receptor binding selectivity of the influenza B HA.
Url:
DOI: 10.1002/jmr.2293
Links to Exploration step
ISTEX:E6C98E87E410878110EE70CA486D604496A6F143Le document en format XML
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<lineatedText><line>Correspondence to: Tony Velkov, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, Victoria, Australia.</line><line>E‐mail: <email>Tony.Velkov@monash.edu</email></line></lineatedText></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JMR.JMR2293.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?</title><title type="short">INFLUENZA B HEMAGGLUTININ RECEPTORS</title><title type="shortAuthors">T. VELKOV</title></titleGroup><creators><creator creatorRole="author" xml:id="jmr2293-cr-0001" affiliationRef="#jmr2293-aff-0001" corresponding="yes"><personName><givenNames>Tony</givenNames><familyName>Velkov</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="AU" type="organization" xml:id="jmr2293-aff-0001"><orgDiv>Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences</orgDiv><orgName>Monash University</orgName><address><street>381 Royal Parade</street><city>Parkville</city><postCode>3052</postCode><countryPart>Victoria</countryPart><country>Australia</country></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="jmr2293-kwd-0001">influenza B</keyword><keyword xml:id="jmr2293-kwd-0002">hemagglutinin</keyword><keyword xml:id="jmr2293-kwd-0003">receptor specificity</keyword></keywordGroup><supportingInformation xml:id="jmr2293-supinf-0001"><p>Supporting information may be found in the online version of this paper</p><supportingInfoItem xml:id="jmr2293-supitem-0001"><mediaResource alt="supplementary data" mimeType="application/pdf" rendition="webOriginal" href="urn-x:wiley:09523499:media:jmr2293:jmr2293_Suppl_Info"></mediaResource><caption>Supplementary Figure 1</caption></supportingInfoItem></supportingInformation><abstractGroup><abstract type="main"><p>The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl‐glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg‐adapted variants. Overall, the review serves as an up‐to‐date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright © 2013 John Wiley & Sons, Ltd.</p></abstract><abstract type="graphical"><p>It remains contentious whether the influenza B hemagglutinin (HA) preferentially binds to α2,6‐linked human type receptors or equally well to α2,3‐linked type avian receptors, and how or if in fact any receptor selectivity plays a role in the viruses infectivity of humans. For the first time, the present review forms a treatise that unifies the receptor binding data and provides a consensus for the modalities that determine the receptor binding selectivity of the influenza B HA.
<blockFixed type="graphic"><mediaResourceGroup><mediaResource alt="image" href="urn:x-wiley:03770486:media:jmr2293:jmr2293-toc-0001"></mediaResource></mediaResourceGroup></blockFixed></p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>INFLUENZA B HEMAGGLUTININ RECEPTORS</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>The specificity of the influenza B virus hemagglutinin receptor binding pocket: what does it bind to?</title></titleInfo><name type="personal"><namePart type="given">Tony</namePart><namePart type="family">Velkov</namePart><affiliation>Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Victoria, 3052, Parkville, Australia</affiliation><affiliation>Correspondence to: Tony Velkov, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville 3052, Victoria, Australia.E‐mail:</affiliation><affiliation>E-mail: Tony.Velkov@monash.edu</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">2013-10</dateIssued><dateCreated encoding="w3cdtf">2013-06-29</dateCreated><dateCaptured encoding="w3cdtf">2013-05-03</dateCaptured><dateValid encoding="w3cdtf">2013-06-16</dateValid><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract>The influenza surface glycoprotein hemagglutinin (HA) binds to sialylglycoproteins and sialylglycolipids on the surface of host cells. These sialyl‐glycans, usually linked to galactose in either α2,6 or α2,3 configurations, are the receptors for the viral HA, the binding to which promotes viral attachment, membrane fusion, and internalization of the virus. This review examines all of the available receptor binding data on the influenza B HA and provides a structure recognition perspective for the receptor binding preferences of influenza B virus HA regional and egg‐adapted variants. Overall, the review serves as an up‐to‐date compendium of the literature binding data, and the presented discussions assist the reader in reaching a consensus understanding of the receptor specificity determinants for the influenza B HA. Copyright © 2013 John Wiley & Sons, Ltd.</abstract><abstract type="graphical">It remains contentious whether the influenza B hemagglutinin (HA) preferentially binds to α2,6‐linked human type receptors or equally well to α2,3‐linked type avian receptors, and how or if in fact any receptor selectivity plays a role in the viruses infectivity of humans. For the first time, the present review forms a treatise that unifies the receptor binding data and provides a consensus for the modalities that determine the receptor binding selectivity of the influenza B HA.</abstract><subject><genre>keywords</genre><topic>influenza B</topic><topic>hemagglutinin</topic><topic>receptor specificity</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Molecular Recognition</title></titleInfo><titleInfo type="abbreviated"><title>J. Mol. 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