Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
Identifieur interne : 000194 ( Istex/Corpus ); précédent : 000193; suivant : 000195Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
Auteurs : M. N. Matrosovich ; A. S. Gambaryan ; M. P. ChumakovSource :
- Virology [ 0042-6822 ] ; 1992.
English descriptors
- Teeft :
- Academic press, Binding affinity, Carbonyl oxygen, Conjugate concentration, Influenza, Influenza viruses, Lvanovsky institute, Minimum energy conformation, Molecular modeling, Neu5ac, Paulson, Reaction mixture, Same time, Seed stocks, Short communications, Sialic acid, Structural model, Substitution, Virology, Virus.
Abstract
Abstract: Equine α2 macroglobulin (EM), known to contain both Neu5Ac and Neu4,5Ac2 sialic acid residues, was treated with Vibrio cholerae sialidase for the selective removal of Neu5Ac and was compared with the untreated EM for its binding by a panel of influenza viruses. Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.
Url:
DOI: 10.1016/0042-6822(92)90541-V
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N." last="Matrosovich">M. N. Matrosovich</name><affiliation><mods:affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</mods:affiliation></affiliation></author><author><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name><affiliation><mods:affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</mods:affiliation></affiliation></author><author><name sortKey="Chumakov, M P" sort="Chumakov, M P" uniqKey="Chumakov M" first="M. P." last="Chumakov">M. P. 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Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>influenza viruses</json:string><json:string>neu5ac</json:string><json:string>virology</json:string><json:string>paulson</json:string><json:string>carbonyl oxygen</json:string><json:string>influenza</json:string><json:string>sialic acid</json:string><json:string>binding affinity</json:string><json:string>short communications</json:string><json:string>minimum energy conformation</json:string><json:string>substitution</json:string><json:string>structural model</json:string><json:string>lvanovsky institute</json:string><json:string>same time</json:string><json:string>conjugate concentration</json:string><json:string>reaction mixture</json:string><json:string>molecular modeling</json:string><json:string>seed stocks</json:string><json:string>academic press</json:string><json:string>virus</json:string></teeft></keywords><author><json:item><name>M.N. Matrosovich</name><affiliations><json:string>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</json:string></affiliations></json:item><json:item><name>A.S. Gambaryan</name><affiliations><json:string>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</json:string></affiliations></json:item><json:item><name>M.P. 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At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. 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A. Wharton</json:string><json:string>Hong Kong</json:string><json:string>V. Cholerae</json:string><json:string>M. Shenderovich</json:string><json:string>S. K. Vasilenko</json:string><json:string>J. Skehel</json:string><json:string>N. A. Petrov</json:string><json:string>Ann Arbor</json:string><json:string>M. A. Yakhno</json:string><json:string>T. Dudenus</json:string><json:string>W. Weis</json:string><json:string>S. Wharton</json:string><json:string>V. Levchuk</json:string><json:string>L. Podin</json:string></persName><placeName><json:string>Singapore</json:string><json:string>Chile</json:string><json:string>Bangkok</json:string><json:string>Port Chalmers</json:string><json:string>Taiwan</json:string><json:string>Riga</json:string><json:string>Moscow</json:string><json:string>Philippines</json:string><json:string>Leningrad</json:string><json:string>Novosibirsk</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Levinson et al.</json:string><json:string>Weis et al. 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Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</p></abstract></profileDesc><revisionDesc><change when="1992">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-FHTL5JF9-7/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>9290541V</aid><ce:pii>0042-6822(92)90541-V</ce:pii><ce:doi>10.1016/0042-6822(92)90541-V</ce:doi><ce:copyright type="unknown" year="1992"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Short communication</ce:textfn></ce:dochead><ce:title>Influenza viruses differ in recognition of 4-<ce:italic>O</ce:italic>-acetyl substitution of sialic acid receptor determinant</ce:title><ce:author-group><ce:author><ce:given-name>M.N.</ce:given-name><ce:surname>Matrosovich</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.S.</ce:given-name><ce:surname>Gambaryan</ce:surname></ce:author><ce:author><ce:given-name>M.P.</ce:given-name><ce:surname>Chumakov</ce:surname></ce:author><ce:affiliation><ce:textfn>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</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:author-group><ce:date-received day="7" month="10" year="1991"></ce:date-received><ce:date-accepted day="4" month="3" year="1992"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Equine α<ce:inf>2</ce:inf> macroglobulin (EM), known to contain both Neu5Ac and Neu4,5Ac2 sialic acid residues, was treated with <ce:italic>Vibrio</ce:italic> cholerae sialidase for the selective removal of Neu5Ac and was compared with the untreated EM for its binding by a panel of influenza viruses. Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-<ce:italic>0</ce:italic>-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac<ce:inf>2</ce:inf> moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis <ce:italic>et al.</ce:italic> (1988) <ce:italic>Nature</ce:italic> 333, 426–431) predicts that the 4-<ce:italic>0</ce:italic>-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Influenza viruses differ in recognition of 4-</title></titleInfo><name type="personal"><namePart type="given">M.N.</namePart><namePart type="family">Matrosovich</namePart><affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.S.</namePart><namePart type="family">Gambaryan</namePart><affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.P.</namePart><namePart type="family">Chumakov</namePart><affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782, Russian Republic Russia</affiliation><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">1992</dateIssued><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Equine α2 macroglobulin (EM), known to contain both Neu5Ac and Neu4,5Ac2 sialic acid residues, was treated with Vibrio cholerae sialidase for the selective removal of Neu5Ac and was compared with the untreated EM for its binding by a panel of influenza viruses. Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</abstract><note type="content">Section title: Short communication</note><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">1992</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0433-3</identifier><part><date>1992</date><detail type="volume"><number>188</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>417</start><end>975</end></extent><extent unit="pages"><start>854</start><end>858</end></extent></part></relatedItem><identifier type="istex">FDD06B9D857461945014F05A3F65118AA3EC6964</identifier><identifier type="ark">ark:/67375/6H6-FHTL5JF9-7</identifier><identifier type="DOI">10.1016/0042-6822(92)90541-V</identifier><identifier type="PII">0042-6822(92)90541-V</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-FHTL5JF9-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
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