Functional balance between haemagglutinin and neuraminidase in influenza virus infections
Identifieur interne : 000482 ( Istex/Corpus ); précédent : 000481; suivant : 000483Functional balance between haemagglutinin and neuraminidase in influenza virus infections
Auteurs : Ralf Wagner ; Mikhail Matrosovich ; Hans-Dieter KlenkSource :
- Reviews in Medical Virology [ 1052-9276 ] ; 2002-05.
English descriptors
- Teeft :
- Amino, Arch virol, Avian, Cell culture, Cellular receptors, Copyright, Embryonated chicken eggs, Functional balance, Glycoprotein, Haemagglutinin, Hemagglutinin, Host cells, Human viruses, Inhibitor, John wiley sons, Mdck cells, Membrane fusion, Molecular species, Mutant, Mutation, Neuraminidase, Neuraminidase activity, Neuraminidase inhibitors, Parent virus, Progeny, Progeny virions, Reassortants, Receptor, Receptor binding, Receptor binding site, Recombinant viruses, Replication, Sialic, Sialic acid, Sialic acid receptors, Sialic acids, Surface glycoproteins, Viral, Virol, Virology, Virus, Virus neuraminidase, Virus reassortants, Virus release, Virus replication.
Abstract
Influenza A and B viruses carry two surface glycoproteins, the haemagglutinin (HA) and the neuraminidase (NA). Both proteins have been found to recognise the same host cell molecule, sialic acid. HA binds to sialic acid‐containing receptors on target cells to initiate virus infection, whereas NA cleaves sialic acids from cellular receptors and extracellular inhibitors to facilitate progeny virus release and to promote the spread of the infection to neighbouring cells. Numerous studies performed recently have revealed that an optimal interplay between these receptor‐binding and receptor‐destroying activities of the surface glycoproteins is required for efficient virus replication. An existing balance between the antagonistic HA and NA functions of individual viruses can be disturbed by various events, such as reassortment, virus transmission to a new host, or therapeutic inhibition of neuraminidase. The resulting decrease in the viral replicative fitness is usually overcome by restoration of the functional balance due to compensatory mutations in HA, NA or both proteins. Copyright © 2002 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/rmv.352
Links to Exploration step
ISTEX:CA5DF7215C4873D815400E284DEA05BBFFDA15DBLe document en format XML
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Copyright © 2002 John Wiley & Sons, Ltd.</p></abstract><textClass><keywords rend="articleCategory"><term>Review Article</term></keywords><keywords rend="tocHeading1"><term>Review Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-9T85ZXDT-G/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Ltd.</publisherName><publisherLoc>Chichester, UK</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1099-1654</doi><issn type="print">1052-9276</issn><issn type="electronic">1099-1654</issn><idGroup><id type="product" value="RMV"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="REVIEWS IN MEDICAL VIROLOGY">Reviews in Medical Virology</title><title type="short">Rev. 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Virol.</title></titleGroup></publicationMeta><publicationMeta level="part" position="30"><doi origin="wiley" registered="yes">10.1002/rmv.v12:3</doi><numberingGroup><numbering type="journalVolume" number="12">12</numbering><numbering type="journalIssue">3</numbering></numberingGroup><coverDate startDate="2002-05">May/June 2002</coverDate></publicationMeta><publicationMeta level="unit" type="reviewArticle" position="5" status="forIssue"><doi origin="wiley" registered="yes">10.1002/rmv.352</doi><idGroup><id type="unit" value="RMV352"></id></idGroup><countGroup><count type="pageTotal" number="8"></count></countGroup><titleGroup><title type="articleCategory">Review Article</title><title type="tocHeading1">Review Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2002 John Wiley & Sons, Ltd.</copyright><eventGroup><event type="manuscriptAccepted" date="2002-02-15"></event><event type="firstOnline" date="2002-04-25"></event><event type="publishedOnlineFinalForm" date="2002-04-25"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-04"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-03"></event></eventGroup><numberingGroup><numbering type="pageFirst">159</numbering><numbering type="pageLast">166</numbering></numberingGroup><correspondenceTo>Institut für Virologie, Philipps‐Universität Marburg, Postfach 2360, 35011Marburg, Germany.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:RMV.RMV352.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="1"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="60"></count></countGroup><titleGroup><title type="main" xml:lang="en">Functional balance between haemagglutinin and neuraminidase in influenza virus infections</title><title type="short" xml:lang="en">Balance between haemagglutinin and neuraminidase</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Ralf</givenNames><familyName>Wagner</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1 #af2"><personName><givenNames>Mikhail</givenNames><familyName>Matrosovich</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Hans‐Dieter</givenNames><familyName>Klenk</familyName></personName><contactDetails><email normalForm="Klenk@mailer.uni-marburg.de">Klenk@mailer.uni‐marburg.de</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="DE" type="organization"><unparsedAffiliation>Institut für Virologie, Philipps‐Universität, 35011 Marburg, Germany</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="RU" type="organization"><unparsedAffiliation>M.P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782 Moscow, Russia</unparsedAffiliation></affiliation></affiliationGroup><fundingInfo><fundingAgency>Deutsche Forschungsgemeinschaft</fundingAgency><fundingNumber>SFB 286</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Fonds der Chemischen Industrie</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Roche Products Ltd, Welwyn Garden City, UK</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Influenza A and B viruses carry two surface glycoproteins, the haemagglutinin (HA) and the neuraminidase (NA). Both proteins have been found to recognise the same host cell molecule, sialic acid. HA binds to sialic acid‐containing receptors on target cells to initiate virus infection, whereas NA cleaves sialic acids from cellular receptors and extracellular inhibitors to facilitate progeny virus release and to promote the spread of the infection to neighbouring cells. Numerous studies performed recently have revealed that an optimal interplay between these receptor‐binding and receptor‐destroying activities of the surface glycoproteins is required for efficient virus replication. An existing balance between the antagonistic HA and NA functions of individual viruses can be disturbed by various events, such as reassortment, virus transmission to a new host, or therapeutic inhibition of neuraminidase. The resulting decrease in the viral replicative fitness is usually overcome by restoration of the functional balance due to compensatory mutations in HA, NA or both proteins. Copyright © 2002 John Wiley & Sons, Ltd.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Functional balance between haemagglutinin and neuraminidase in influenza virus infections</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Balance between haemagglutinin and neuraminidase</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Functional balance between haemagglutinin and neuraminidase in influenza virus infections</title></titleInfo><name type="personal"><namePart type="given">Ralf</namePart><namePart type="family">Wagner</namePart><affiliation>Institut für Virologie, Philipps‐Universität, 35011 Marburg, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mikhail</namePart><namePart type="family">Matrosovich</namePart><affiliation>Institut für Virologie, Philipps‐Universität, 35011 Marburg, Germany</affiliation><affiliation>M.P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782 Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hans‐Dieter</namePart><namePart type="family">Klenk</namePart><affiliation>Institut für Virologie, Philipps‐Universität, 35011 Marburg, Germany</affiliation><affiliation>E-mail: Klenk@mailer.uni‐marburg.de</affiliation><affiliation>Correspondence address: Institut für Virologie, Philipps‐Universität Marburg, Postfach 2360, 35011Marburg, Germany.</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>John Wiley & Sons, Ltd.</publisher><place><placeTerm type="text">Chichester, UK</placeTerm></place><dateIssued encoding="w3cdtf">2002-05</dateIssued><dateValid encoding="w3cdtf">2002-02-15</dateValid><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">1</extent><extent unit="tables">0</extent><extent unit="references">60</extent></physicalDescription><abstract lang="en">Influenza A and B viruses carry two surface glycoproteins, the haemagglutinin (HA) and the neuraminidase (NA). Both proteins have been found to recognise the same host cell molecule, sialic acid. HA binds to sialic acid‐containing receptors on target cells to initiate virus infection, whereas NA cleaves sialic acids from cellular receptors and extracellular inhibitors to facilitate progeny virus release and to promote the spread of the infection to neighbouring cells. Numerous studies performed recently have revealed that an optimal interplay between these receptor‐binding and receptor‐destroying activities of the surface glycoproteins is required for efficient virus replication. An existing balance between the antagonistic HA and NA functions of individual viruses can be disturbed by various events, such as reassortment, virus transmission to a new host, or therapeutic inhibition of neuraminidase. The resulting decrease in the viral replicative fitness is usually overcome by restoration of the functional balance due to compensatory mutations in HA, NA or both proteins. 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