Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human
Identifieur interne : 000626 ( Istex/Corpus ); précédent : 000625; suivant : 000627Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human
Auteurs : A. S. Gambaryan ; S. S. Yamnikova ; D. K. Lvov ; J. S. Robertson ; R. G. Webster ; M. N. MatrosovichSource :
- Molecular Biology [ 0026-8933 ] ; 2002-05-01.
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Abstract
Abstract: The affinity of the duck, chicken, and human influenza viruses to the host cell sialosides was determined, and considerable distinctions between duck and chicken viruses were found. Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.
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DOI: 10.1023/A:1016023700050
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ISTEX:D8E33CF51E8A468E268930C03CAB55C2BB8175E3Le document en format XML
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Robertson</name><affiliation><mods:affiliation>National Institute for Biological Standards and Control, EN6 3QG, Herts, UK</mods:affiliation></affiliation></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 38105-2794, Memphis, Tennessee, USA</mods:affiliation></affiliation></author><author><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. N. Matrosovich</name><affiliation><mods:affiliation>Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782, Moscow Region, Russia</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: gambar@mail.infotel.ru</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Biology</title><title level="j" type="abbrev">Molecular Biology</title><idno type="ISSN">0026-8933</idno><idno type="eISSN">1608-3245</idno><imprint><publisher>Kluwer Academic Publishers-Plenum Publishers</publisher><pubPlace>New York</pubPlace><date type="published" when="2002-05-01">2002-05-01</date><biblScope unit="volume">36</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="429">429</biblScope><biblScope unit="page" to="435">435</biblScope></imprint><idno type="ISSN">0026-8933</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0026-8933</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>evolution</term><term>gangliosides</term><term>influenza viruses</term><term>receptors</term><term>species barrier</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The affinity of the duck, chicken, and human influenza viruses to the host cell sialosides was determined, and considerable distinctions between duck and chicken viruses were found. Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>A. S. Gambaryan</name><affiliations><json:string>Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782, Moscow Region, Russia</json:string><json:string>E-mail: gambar@mail.infotel.ru</json:string></affiliations></json:item><json:item><name>S. S. Yamnikova</name><affiliations><json:string>Ivanovsky Institute of Virology, 123098, Moscow, Russia</json:string></affiliations></json:item><json:item><name>D. K. Lvov</name><affiliations><json:string>Ivanovsky Institute of Virology, 123098, Moscow, Russia</json:string></affiliations></json:item><json:item><name>J. S. 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Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</abstract><qualityIndicators><score>7.944</score><pdfWordCount>3436</pdfWordCount><pdfCharCount>22199</pdfCharCount><pdfVersion>1.4</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>209</abstractWordCount><abstractCharCount>1315</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human</title><genre><json:string>research-article</json:string></genre><host><title>Molecular 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Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><item><term>influenza viruses</term></item><item><term>evolution</term></item><item><term>species barrier</term></item><item><term>receptors</term></item><item><term>gangliosides</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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DisplayOrder="Western"><GivenName>S.</GivenName><GivenName>S.</GivenName><FamilyName>Yamnikova</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>D.</GivenName><GivenName>K.</GivenName><FamilyName>Lvov</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>J.</GivenName><GivenName>S.</GivenName><FamilyName>Robertson</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff4"><AuthorName DisplayOrder="Western"><GivenName>R.</GivenName><GivenName>G.</GivenName><FamilyName>Webster</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>M.</GivenName><GivenName>N.</GivenName><FamilyName>Matrosovich</FamilyName></AuthorName><Contact><Email>gambar@mail.infotel.ru</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Chumakov Institute of Poliomyelitis and Viral Encephalitides</OrgDivision><OrgName>Russian Academy of Medical Sciences</OrgName><OrgAddress><State>Moscow Region</State><Postcode>142782</Postcode><Country>Russia</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgName>Ivanovsky Institute of Virology</OrgName><OrgAddress><City>Moscow</City><Postcode>123098</Postcode><Country>Russia</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgName>National Institute for Biological Standards and Control</OrgName><OrgAddress><City>Herts</City><Postcode>EN6 3QG</Postcode><Country>UK</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgDivision>Department of Virology and Molecular Biology</OrgDivision><OrgName>St. Jude Children's Research Hospital</OrgName><OrgAddress><City>Memphis</City><State>Tennessee</State><Postcode>38105-2794</Postcode><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>The affinity of the duck, chicken, and human influenza viruses to the host cell sialosides was determined, and considerable distinctions between duck and chicken viruses were found. Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</Para></Abstract><KeywordGroup Language="En"><Keyword>influenza viruses</Keyword><Keyword>evolution</Keyword><Keyword>species barrier</Keyword><Keyword>receptors</Keyword><Keyword>gangliosides</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human</title></titleInfo><name type="personal"><namePart type="given">A.</namePart><namePart type="given">S.</namePart><namePart type="family">Gambaryan</namePart><affiliation>Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782, Moscow Region, Russia</affiliation><affiliation>E-mail: gambar@mail.infotel.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="given">S.</namePart><namePart type="family">Yamnikova</namePart><affiliation>Ivanovsky Institute of Virology, 123098, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.</namePart><namePart type="given">K.</namePart><namePart type="family">Lvov</namePart><affiliation>Ivanovsky Institute of Virology, 123098, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="given">S.</namePart><namePart type="family">Robertson</namePart><affiliation>National Institute for Biological Standards and Control, EN6 3QG, Herts, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="given">G.</namePart><namePart type="family">Webster</namePart><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 38105-2794, Memphis, Tennessee, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="given">N.</namePart><namePart type="family">Matrosovich</namePart><affiliation>Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782, Moscow Region, Russia</affiliation><affiliation>E-mail: gambar@mail.infotel.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">2002-05-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: The affinity of the duck, chicken, and human influenza viruses to the host cell sialosides was determined, and considerable distinctions between duck and chicken viruses were found. Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</abstract><subject lang="en"><topic>influenza viruses</topic><topic>evolution</topic><topic>species barrier</topic><topic>receptors</topic><topic>gangliosides</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">2002-05-01</dateIssued><copyrightDate encoding="w3cdtf">2002</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">22</identifier><identifier type="VolumeIssueCount">8</identifier><part><date>2002</date><detail type="volume"><number>36</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="pages"><start>429</start><end>435</end></extent></part><recordInfo><recordOrigin>MAIK “Nauka/Interperiodica”, 2002</recordOrigin></recordInfo></relatedItem><identifier type="istex">D8E33CF51E8A468E268930C03CAB55C2BB8175E3</identifier><identifier type="ark">ark:/67375/VQC-M20NJFXC-7</identifier><identifier type="DOI">10.1023/A:1016023700050</identifier><identifier type="ArticleID">378273</identifier><identifier type="ArticleID">Art22</identifier><accessCondition type="use and reproduction" contentType="copyright">MAIK “Nauka/Interperiodica”, 2002</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”, 2002</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-M20NJFXC-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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