Functional Interactions of the Influenza Virus Glycoproteins
Identifieur interne : 000D56 ( Istex/Corpus ); précédent : 000D55; suivant : 000D57Functional Interactions of the Influenza Virus Glycoproteins
Auteurs : I. A. Rudneva ; N. A. Il'Yushina ; A. A. Shilov ; N. L. Varich ; B. V. Sinitsyn ; E. A. Kropotkina ; N. V. KaverinSource :
- Molecular Biology [ 0026-8933 ] ; 2003-01-01.
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Abstract
Abstract: Hemagglutinin (HA) and neuraminidase (NA) are functionally related envelope glycoproteins of the influenza virus (Flu). HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.
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DOI: 10.1023/A:1022372427314
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HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>I. A. Rudneva</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>N. A. Il'yushina</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>A. A. Shilov</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>N. L. Varich</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>B. V. Sinitsyn</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>E. A. Kropotkina</name><affiliations><json:string>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</json:string><json:string>E-mail: kaverin@online.ru</json:string></affiliations></json:item><json:item><name>N. V. 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HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.</abstract><qualityIndicators><score>8.308</score><pdfWordCount>3464</pdfWordCount><pdfCharCount>22515</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>237</abstractWordCount><abstractCharCount>1603</abstractCharCount><keywordCount>7</keywordCount></qualityIndicators><title>Functional Interactions of the Influenza Virus Glycoproteins</title><genre><json:string>research-article</json:string></genre><host><title>Molecular 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HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><item><term>influenza virus</term></item><item><term>glycoprotein</term></item><item><term>gene</term></item><item><term>mutation</term></item><item><term>molecular evolution</term></item><item><term>hemagglutinin</term></item><item><term>neuraminidase</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Human Genetics</term></item><item><term>Life Sciences, general</term></item><item><term>Biochemistry, general</term></item></list></keywords></textClass></profileDesc><revisionDesc><change 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“Nauka/Interperiodica”</CopyrightHolderName><CopyrightYear>2003</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11008</JournalID><VolumeIDStart>37</VolumeIDStart><VolumeIDEnd>37</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>1</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>I.</GivenName><GivenName>A.</GivenName><FamilyName>Rudneva</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>N.</GivenName><GivenName>A.</GivenName><FamilyName>Il'yushina</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>A.</GivenName><FamilyName>Shilov</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>N.</GivenName><GivenName>L.</GivenName><FamilyName>Varich</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>B.</GivenName><GivenName>V.</GivenName><FamilyName>Sinitsyn</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>E.</GivenName><GivenName>A.</GivenName><FamilyName>Kropotkina</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>N.</GivenName><GivenName>V.</GivenName><FamilyName>Kaverin</FamilyName></AuthorName><Contact><Email>kaverin@online.ru</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Ivanovsky Institute of Virology</OrgDivision><OrgName>Russian Academy of Medical Sciences</OrgName><OrgAddress><City>Moscow</City><Postcode>123098</Postcode><Country>Russia</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Hemagglutinin (HA) and neuraminidase (NA) are functionally related envelope glycoproteins of the influenza virus (Flu). HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.</Para></Abstract><KeywordGroup Language="En"><Keyword>influenza virus</Keyword><Keyword>glycoprotein</Keyword><Keyword>gene</Keyword><Keyword>mutation</Keyword><Keyword>molecular evolution</Keyword><Keyword>hemagglutinin</Keyword><Keyword>neuraminidase</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Functional Interactions of the Influenza Virus Glycoproteins</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Functional Interactions of the Influenza Virus Glycoproteins</title></titleInfo><name type="personal"><namePart type="given">I.</namePart><namePart type="given">A.</namePart><namePart type="family">Rudneva</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="given">A.</namePart><namePart type="family">Il'yushina</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="given">A.</namePart><namePart type="family">Shilov</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="given">L.</namePart><namePart type="family">Varich</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="given">V.</namePart><namePart type="family">Sinitsyn</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="given">A.</namePart><namePart type="family">Kropotkina</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="given">V.</namePart><namePart type="family">Kaverin</namePart><affiliation>Ivanovsky Institute of Virology, Russian Academy of Medical Sciences, 123098, Moscow, Russia</affiliation><affiliation>E-mail: kaverin@online.ru</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>Kluwer Academic Publishers-Plenum Publishers</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2003-01-01</dateIssued><copyrightDate encoding="w3cdtf">2003</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Hemagglutinin (HA) and neuraminidase (NA) are functionally related envelope glycoproteins of the influenza virus (Flu). HA interacts with terminal sialyl residues of oligosaccharides and ensures the binding of the virus particle to the cell surface. NA is a receptor-destroying enzyme that removes sialyl residues from oligosaccharides contained in cell and virus components and thereby prevents aggregation of virus particles. Analysis of reassortants combining low-functional NA of human Flu with HA of avian Flu showed that sialyl residues are not completely removed in some cases. With high HA affinity for sialyl substrates, such virus particles aggregate, aggregates accumulate on the cell surface, and virus yield decreases. Serial passaging of low-yield aggregating reassortants may lead to selection of high-yield variants, which do not aggregate. The loss of aggregation is due to a decrease in HA affinity for high-molecular-weight sialyl substrates. On evidence of sequencing of the HA gene in original reassortants and their nonaggregating variants, for different HA antigenic subtypes (H2, H3, H4, and H13) the affinity is reduced and aggregation lost through a common mechanism: an increase in the negative charge as a result of an amino acid substitution in the vicinity of the receptor-binding pocket of HA. Taken together, these findings suggest a way of postreassortment adaptation, which improves the functional match of HA and NA. The experimental system employed provides a model of natural processes associated with emergence of Flu variants having a pandemic potential.</abstract><subject lang="en"><topic>influenza virus</topic><topic>glycoprotein</topic><topic>gene</topic><topic>mutation</topic><topic>molecular evolution</topic><topic>hemagglutinin</topic><topic>neuraminidase</topic></subject><relatedItem type="host"><titleInfo><title>Molecular Biology</title></titleInfo><titleInfo type="abbreviated"><title>Molecular Biology</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">2003-01-01</dateIssued><copyrightDate encoding="w3cdtf">2003</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Human Genetics</topic><topic>Life Sciences, general</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0026-8933</identifier><identifier type="eISSN">1608-3245</identifier><identifier type="JournalID">11008</identifier><identifier type="IssueArticleCount">23</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2003</date><detail type="volume"><number>37</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="pages"><start>31</start><end>36</end></extent></part><recordInfo><recordOrigin>MAIK “Nauka/Interperiodica”, 2003</recordOrigin></recordInfo></relatedItem><identifier type="istex">B8960A892D62251C505FC585908F5CABC09E4333</identifier><identifier type="ark">ark:/67375/VQC-BJVNDBJK-S</identifier><identifier type="DOI">10.1023/A:1022372427314</identifier><identifier type="ArticleID">463155</identifier><identifier type="ArticleID">Art7</identifier><accessCondition type="use and reproduction" contentType="copyright">MAIK “Nauka/Interperiodica”, 2003</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>MAIK “Nauka/Interperiodica”, 2003</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-BJVNDBJK-S/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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