The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity
Identifieur interne : 000201 ( Istex/Corpus ); précédent : 000200; suivant : 000202The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity
Auteurs : Linda G. Baum ; James C. PaulsonSource :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Acid glycoprotein, Cell surface receptors, Derivatized, Derivatized erythrocytes, Determinant, Elute, Equal activity, Erythrocyte, Erythrocytes derivatized, Glycoprotein, Hemagglutination, Hemagglutinin, Hemagglutinin specificities, Human influenza, Human influenza virus, Influenza, Influenza virus, Influenza virus neuraminidase, Linkage, Neuac, Neuraminidase, Neuraminidase activity, Neuraminidase specificity, Neuraminidases, Paulson, Preferred receptor determinant, Receptor, Receptor determinants, Selective advantage, Sialic, Sialic acid, Sialic acids, Specificity, Substrate specificity, Viral, Viral neuraminidase activity, Virology, Virus, Virus strains.
Abstract
Abstract: A survey of 10 human influenza A viruses of the N2 serotype, isolated between 1957 and 1987, has revealed a drift in neuraminidase linkage specificity. While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.
Url:
DOI: 10.1016/0042-6822(91)90003-T
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ISTEX:2289D9041E455BB2D34C592075597920331B17EDLe document en format XML
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Paulson</name><affiliation><mods:affiliation>Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">180</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="10">10</biblScope><biblScope unit="page" to="15">15</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Acid glycoprotein</term><term>Cell surface receptors</term><term>Derivatized</term><term>Derivatized erythrocytes</term><term>Determinant</term><term>Elute</term><term>Equal activity</term><term>Erythrocyte</term><term>Erythrocytes derivatized</term><term>Glycoprotein</term><term>Hemagglutination</term><term>Hemagglutinin</term><term>Hemagglutinin specificities</term><term>Human influenza</term><term>Human influenza virus</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Linkage</term><term>Neuac</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Neuraminidase specificity</term><term>Neuraminidases</term><term>Paulson</term><term>Preferred receptor determinant</term><term>Receptor</term><term>Receptor determinants</term><term>Selective advantage</term><term>Sialic</term><term>Sialic acid</term><term>Sialic acids</term><term>Specificity</term><term>Substrate specificity</term><term>Viral</term><term>Viral neuraminidase activity</term><term>Virology</term><term>Virus</term><term>Virus strains</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A survey of 10 human influenza A viruses of the N2 serotype, isolated between 1957 and 1987, has revealed a drift in neuraminidase linkage specificity. While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>receptor</json:string><json:string>erythrocyte</json:string><json:string>derivatized</json:string><json:string>viral</json:string><json:string>paulson</json:string><json:string>glycoprotein</json:string><json:string>hemagglutinin</json:string><json:string>sialic</json:string><json:string>neuraminidases</json:string><json:string>influenza</json:string><json:string>neuac</json:string><json:string>hemagglutination</json:string><json:string>linkage</json:string><json:string>neuraminidase activity</json:string><json:string>elute</json:string><json:string>virology</json:string><json:string>determinant</json:string><json:string>neuraminidase specificity</json:string><json:string>receptor determinants</json:string><json:string>influenza virus</json:string><json:string>derivatized erythrocytes</json:string><json:string>sialic acid</json:string><json:string>acid glycoprotein</json:string><json:string>influenza virus neuraminidase</json:string><json:string>sialic acids</json:string><json:string>human influenza virus</json:string><json:string>cell surface receptors</json:string><json:string>preferred receptor determinant</json:string><json:string>virus strains</json:string><json:string>selective advantage</json:string><json:string>equal activity</json:string><json:string>virus</json:string><json:string>substrate specificity</json:string><json:string>academic press</json:string><json:string>viral neuraminidase activity</json:string><json:string>human influenza</json:string><json:string>erythrocytes derivatized</json:string><json:string>hemagglutinin specificities</json:string><json:string>specificity</json:string></teeft></keywords><author><json:item><name>Linda G. Baum</name><affiliations><json:string>Department of Pathology, UCLA School of Medicine, Los Angeles, California 90024, USA</json:string></affiliations></json:item><json:item><name>James C. Paulson</name><affiliations><json:string>Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-X8WT0TK2-7</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: A survey of 10 human influenza A viruses of the N2 serotype, isolated between 1957 and 1987, has revealed a drift in neuraminidase linkage specificity. While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.</abstract><qualityIndicators><score>7.468</score><pdfWordCount>3524</pdfWordCount><pdfCharCount>24032</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>162</abstractWordCount><abstractCharCount>1095</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity</title><pmid><json:string>1984642</json:string></pmid><pii><json:string>0042-6822(91)90003-T</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0256-5</json:string></pii><volume>180</volume><issue>1</issue><pages><first>10</first><last>15</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1972</json:string><json:string>30s</json:string><json:string>1991</json:string><json:string>1967</json:string></date><geogName></geogName><orgName><json:string>Children’s Research Hospital, Memphis, Tennessee</json:string><json:string>National Foundation for Infectious Diseases</json:string><json:string>Cytel, Inc.</json:string><json:string>The Rockefeller University</json:string><json:string>Cooke Engineering Co.</json:string><json:string>Academic Press, Inc.</json:string><json:string>American Type Culture Collection</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Peter Colman</json:string><json:string>Rhode Island</json:string><json:string>Hong Kong</json:string><json:string>R. G. Webster</json:string><json:string>Yoshihiro Kawaoka</json:string><json:string>In</json:string><json:string>Al Victorial</json:string><json:string>Sorge Kelm</json:string><json:string>Purnell Choppin</json:string><json:string>J. C. Paulson</json:string><json:string>N. Couceiro</json:string><json:string>Robert Webster</json:string><json:string>L. G. Baum</json:string><json:string>Y. Kawaoka</json:string></persName><placeName><json:string>Specificity</json:string><json:string>Los Angeles</json:string><json:string>Japan</json:string><json:string>Tokyo</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Ogawa and Ueda, 1981</json:string><json:string>Choppin and Tamm (1960)</json:string><json:string>Colman and Ward, 1985</json:string><json:string>Dourmash- kian and Tyrrell, 1970</json:string><json:string>Choppin and Tamm, 1960</json:string><json:string>Stone and Ada (1952)</json:string><json:string>Carroll et al. (1981)</json:string><json:string>Baum and Paulson, 1990</json:string><json:string>Liu, 1954</json:string><json:string>Stone and Ada, 1952</json:string><json:string>Breg et al., 1987</json:string><json:string>Palese et al., 1974</json:string><json:string>Warren, 1959</json:string><json:string>Rogers and Paulson, 1983</json:string><json:string>Gottschalk, 1957</json:string><json:string>Griffin et al., 1983</json:string><json:string>Schulman and Palese (1977)</json:string><json:string>Pritchett, 1987</json:string><json:string>Higa and Paulson, 1985</json:string><json:string>Carroll et al., 1981</json:string><json:string>Burnet and Stone, 1947</json:string><json:string>Rogers et al., 1983</json:string><json:string>Hirst, 1942</json:string><json:string>Burnet et al. 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While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.</p></abstract></profileDesc><revisionDesc><change when="1991">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X8WT0TK2-7/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YVIRO</jid><aid>9190003T</aid><ce:pii>0042-6822(91)90003-T</ce:pii><ce:doi>10.1016/0042-6822(91)90003-T</ce:doi><ce:copyright type="unknown" year="1991"></ce:copyright></item-info><head><ce:title>The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity</ce:title><ce:author-group><ce:author><ce:given-name>Linda G.</ce:given-name><ce:surname>Baum</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>James C.</ce:given-name><ce:surname>Paulson</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Pathology, UCLA School of Medicine, Los Angeles, California 90024, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom reprint requests should be addressed.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>2</ce:label><ce:note-para>Present address: Cytel, Inc., 11099 Torrey Pines Road, La Jolla, CA 92037.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="27" month="6" year="1990"></ce:date-received><ce:date-accepted day="31" month="8" year="1990"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>A survey of 10 human influenza A viruses of the N2 serotype, isolated between 1957 and 1987, has revealed a drift in neuraminidase linkage specificity. While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity</title></titleInfo><name type="personal"><namePart type="given">Linda G.</namePart><namePart type="family">Baum</namePart><affiliation>Department of Pathology, UCLA School of Medicine, Los Angeles, California 90024, USA</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">James C.</namePart><namePart type="family">Paulson</namePart><affiliation>Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024, USA</affiliation><description>Present address: Cytel, Inc., 11099 Torrey Pines Road, La Jolla, CA 92037.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" 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>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: A survey of 10 human influenza A viruses of the N2 serotype, isolated between 1957 and 1987, has revealed a drift in neuraminidase linkage specificity. While the earliest N2 strains examined exhibit strict specificity for cleavage of the NeuAcα2,3Gal sequence, N2 isolates from 1967 to 1968 also show limited activity towards the NeuAcα2,6Gal linkage. In strains isolated in 1972 and later, the N2 neuraminidase has approximately equal activity towards both types of linkages. The NeuAcα2,6Gal linkage cleaved by the later N2 neuraminidases is the preferred receptor determinant of human H2 and H3 hemagglutinins. Thus, the acquired neuraminidase specificity of the later isolates allows elution of bound virus from erythrocytes derivatized to contain the NeuAcα2,6Gal linkage, while earlier isolates, which cleave only the NeuAcα2,3Gal sequence, fail to elute from these erythrocytes. These results suggest that the observed drift in N2 neuraminidase specificity in the direction of the preferred H2 and H3 receptor determinant may facilitate release of progeny virus from host cells.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</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>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0256-5</identifier><part><date>1991</date><detail type="volume"><number>180</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>465</end></extent><extent unit="pages"><start>10</start><end>15</end></extent></part></relatedItem><identifier type="istex">2289D9041E455BB2D34C592075597920331B17ED</identifier><identifier type="ark">ark:/67375/6H6-X8WT0TK2-7</identifier><identifier type="DOI">10.1016/0042-6822(91)90003-T</identifier><identifier type="PII">0042-6822(91)90003-T</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X8WT0TK2-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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