Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses
Identifieur interne : 000F57 ( Istex/Corpus ); précédent : 000F56; suivant : 000F58Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses
Auteurs : Ping Yang ; Anju Bansal ; Chongguang Liu ; Gillian M. AirSource :
- Virology [ 0042-6822 ] ; 1997.
English descriptors
- Teeft :
- Amino, Amino acids, Antiserum, Cdna, Cdna clones, Cell surface, Clone, Coding information, Confluent mdck cells, Deletion, Fragment, Gene, Gene fragments, Gene segments, Hemagglutinin, Hemagglutinin activity, High levels, Immunoprecipitation, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Laver, Mdck, Mdck cells, Micromonospora viridifaciens, Mouse antiserum, Mutant, Mutant viruses, Neuraminidase, Nucleotide, Nuss, Other viruses, Palese, Peptide, Polymerase, Promega, Promoter, Rabbit antisera, Reading frame, Reassortant, Reassortant virus, Receptor, Receptor binding, Recombinant vaccinia virus, Replication, Rna, Second change, Sequencing, Sialic, Sialic acid, Sialic acids, Subgenomic, Subgenomic rnas, Terminal primers, Viral, Viridifaciens, Virion, Virology, Virology influenza viruses, Virus, Virus stock.
Abstract
Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.
Url:
DOI: 10.1006/viro.1996.8421
Links to Exploration step
ISTEX:4973C23EA35B5E25A6EE9221002B8F5CD889B17FLe document en format XML
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Air</name><affiliation><mods:affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</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="1997">1997</date><biblScope unit="volume">229</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="155">155</biblScope><biblScope unit="page" to="165">165</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>Amino</term><term>Amino acids</term><term>Antiserum</term><term>Cdna</term><term>Cdna clones</term><term>Cell surface</term><term>Clone</term><term>Coding information</term><term>Confluent mdck cells</term><term>Deletion</term><term>Fragment</term><term>Gene</term><term>Gene fragments</term><term>Gene segments</term><term>Hemagglutinin</term><term>Hemagglutinin activity</term><term>High levels</term><term>Immunoprecipitation</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Laver</term><term>Mdck</term><term>Mdck cells</term><term>Micromonospora viridifaciens</term><term>Mouse antiserum</term><term>Mutant</term><term>Mutant viruses</term><term>Neuraminidase</term><term>Nucleotide</term><term>Nuss</term><term>Other viruses</term><term>Palese</term><term>Peptide</term><term>Polymerase</term><term>Promega</term><term>Promoter</term><term>Rabbit antisera</term><term>Reading frame</term><term>Reassortant</term><term>Reassortant virus</term><term>Receptor</term><term>Receptor binding</term><term>Recombinant vaccinia virus</term><term>Replication</term><term>Rna</term><term>Second change</term><term>Sequencing</term><term>Sialic</term><term>Sialic acid</term><term>Sialic acids</term><term>Subgenomic</term><term>Subgenomic rnas</term><term>Terminal primers</term><term>Viral</term><term>Viridifaciens</term><term>Virion</term><term>Virology</term><term>Virology influenza viruses</term><term>Virus</term><term>Virus stock</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. 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Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.</abstract><qualityIndicators><score>9.58</score><pdfWordCount>7907</pdfWordCount><pdfCharCount>46408</pdfCharCount><pdfVersion>1.1</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>532 x 724 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>215</abstractWordCount><abstractCharCount>1378</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</title><pmid><json:string>9123857</json:string></pmid><pii><json:string>S0042-6822(96)98421-4</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1997</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0133-X</json:string></pii><volume>229</volume><issue>1</issue><pages><first>155</first><last>165</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>35S</json:string><json:string>1957</json:string><json:string>1997</json:string><json:string>1000</json:string><json:string>35S</json:string><json:string>1972</json:string><json:string>02-06-97</json:string><json:string>1460</json:string></date><geogName></geogName><orgName><json:string>Kyowa Hakko Kogyo Co., Tokyo, Japan</json:string><json:string>University of Oklahoma Health Sciences Center, Oklahoma City</json:string><json:string>University of Oklahoma Health Sciences Center</json:string><json:string>University of Pittsburgh</json:string><json:string>Department of Cell Biology and Physiology</json:string><json:string>Department of Microbiology, University of Alabama</json:string><json:string>Department of Biochemistry</json:string><json:string>Grant AI</json:string></orgName><orgName_funder><json:string>Grant AI</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Hong Kong</json:string><json:string>Kazuo Aisaka</json:string><json:string>R. G. Webster</json:string><json:string>The</json:string><json:string>Anita Premkumar</json:string><json:string>George Carden</json:string><json:string>W. G. Laver</json:string><json:string>Susan Hollingshead</json:string><json:string>Aleta Dean</json:string><json:string>Laver</json:string></persName><placeName><json:string>Foster City</json:string><json:string>Birmingham</json:string><json:string>Australia</json:string><json:string>Pittsburgh</json:string><json:string>Oklahoma City</json:string><json:string>Canberra</json:string><json:string>Tokyo</json:string><json:string>CA</json:string><json:string>TN</json:string><json:string>Memphis</json:string><json:string>Capacity</json:string><json:string>OK</json:string><json:string>PA</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Air and Laver, 1995</json:string><json:string>Liu and Air, 1993</json:string><json:string>Baum and Paulson, 1991</json:string><json:string>Air and Laver (1995)</json:string><json:string>Li and Palese, 1994</json:string><json:string>Lentz et al., 1984</json:string><json:string>Sambrook, 1989</json:string><json:string>Mitnaul et al., 1996</json:string><json:string>Webster et al., 1987</json:string><json:string>Choppin and Tamm (1959)</json:string><json:string>Schulze et al., 1994</json:string><json:string>Parvin et al., 1989</json:string><json:string>Fuerst et al., 1986</json:string><json:string>Waterfield et al., 1980</json:string><json:string>Rogers et al., 1985</json:string><json:string>Biggin et al., 1983</json:string><json:string>Nuss et al., 1993</json:string><json:string>Palese et al., 1974</json:string><json:string>Jennings et al., 1983</json:string><json:string>Nuss and Air, 1991</json:string><json:string>von Magnus, 1951</json:string><json:string>Aisaka et al., 1991</json:string><json:string>Lentz et al., 1987</json:string><json:string>Air et al., 1985</json:string><json:string>Ward and de Koning-Ward, 1995</json:string><json:string>Laver et al., 1984</json:string><json:string>Noble and Dimmock, 1995</json:string><json:string>Hofling et al., 1996</json:string><json:string>Fodor et al., 1995</json:string><json:string>Piccone et al., 1993</json:string><json:string>Nayak et al., 1982</json:string><json:string>Wei et al., 1987</json:string><json:string>Katz et al., 1987</json:string><json:string>Seong and Brownlee, 1992</json:string><json:string>Hirst, 1941</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-N3PQGW6S-0</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1006/viro.1996.8421</json:string></doi><id>4973C23EA35B5E25A6EE9221002B8F5CD889B17F</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-N3PQGW6S-0/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-N3PQGW6S-0/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-N3PQGW6S-0/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1997 Academic Press</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1997</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>W. Doerfler, Ed.</note><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</title><author xml:id="author-0000"><persName><forename type="first">Ping</forename><surname>Yang</surname></persName><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Anju</forename><surname>Bansal</surname></persName><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, 35294</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Chongguang</forename><surname>Liu</surname></persName><note type="biography">Present address: Department of Cell Biology and Physiology, University of Pittsburgh, School of Medicine, Pittsburgh, PA 15261.</note><affiliation>Present address: Department of Cell Biology and Physiology, University of Pittsburgh, School of Medicine, Pittsburgh, PA 15261.</affiliation><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Gillian M</forename><surname>Air</surname></persName><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation></author><idno type="istex">4973C23EA35B5E25A6EE9221002B8F5CD889B17F</idno><idno type="ark">ark:/67375/6H6-N3PQGW6S-0</idno><idno type="DOI">10.1006/viro.1996.8421</idno><idno type="PII">S0042-6822(96)98421-4</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0133-X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">229</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="155">155</biblScope><biblScope unit="page" to="165">165</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.</p></abstract></profileDesc><revisionDesc><change when="1996-11-22">Modified</change><change when="1997">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-N3PQGW6S-0/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" xml:lang="en"><item-info><jid>YVIRO</jid><aid>98421</aid><ce:pii>S0042-6822(96)98421-4</ce:pii><ce:doi>10.1006/viro.1996.8421</ce:doi><ce:copyright type="full-transfer" year="1997">Academic Press</ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>W. Doerfler, Ed.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</ce:title><ce:author-group><ce:author><ce:given-name>Ping</ce:given-name><ce:surname>Yang</ce:surname><ce:cross-ref refid="VY968421A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Anju</ce:given-name><ce:surname>Bansal</ce:surname><ce:cross-ref refid="VY968421A1"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Chongguang</ce:given-name><ce:surname>Liu</ce:surname><ce:cross-ref refid="VY968421A0"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="VY968421FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Gillian M</ce:given-name><ce:surname>Air</ce:surname><ce:cross-ref refid="VY968421A0"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="VY968421FN2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="VY968421A0"><ce:label>a</ce:label><ce:textfn>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</ce:textfn></ce:affiliation><ce:affiliation id="VY968421A1"><ce:label>b</ce:label><ce:textfn>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, 35294</ce:textfn></ce:affiliation><ce:footnote id="VY968421FN1"><ce:label>1</ce:label><ce:note-para>Present address: Department of Cell Biology and Physiology, University of Pittsburgh, School of Medicine, Pittsburgh, PA 15261.</ce:note-para></ce:footnote><ce:footnote id="VY968421FN2"><ce:label>2</ce:label><ce:note-para>To whom correspondence and reprint requests should be addressed at the Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, P.O. Box 26901, Oklahoma City, OK 73190. Fax: (405) 271-3205; E-mail: gillian-air@uokhsc.edu.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="9" month="10" year="1996"></ce:date-received><ce:date-revised day="22" month="11" year="1996"></ce:date-revised><ce:date-accepted day="17" month="12" year="1996"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33<ce:inf>HA</ce:inf>-tern/Australia/G70c/75<ce:inf>NA</ce:inf>(H1N9) influenza virus in medium containing neuraminidase from<ce:italic>Micromonospora viridifaciens</ce:italic>and antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Hemagglutinin Specificity and Neuraminidase Coding Capacity of Neuraminidase-Deficient Influenza Viruses</title></titleInfo><name type="personal"><namePart type="given">Ping</namePart><namePart type="family">Yang</namePart><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Anju</namePart><namePart type="family">Bansal</namePart><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, 35294</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Chongguang</namePart><namePart type="family">Liu</namePart><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation><description>Present address: Department of Cell Biology and Physiology, University of Pittsburgh, School of Medicine, Pittsburgh, PA 15261.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Gillian M</namePart><namePart type="family">Air</namePart><affiliation>Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73190</affiliation><description>To whom correspondence and reprint requests should be addressed at the Department of Biochemistry & Molecular Biology, University of Oklahoma Health Sciences Center, P.O. Box 26901, Oklahoma City, OK 73190. Fax: (405) 271-3205; E-mail: gillian-air@uokhsc.edu.</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">1997</dateIssued><dateModified encoding="w3cdtf">1996-11-22</dateModified><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Neuraminidase (NA)-deficient mutant virus stocks have been obtained by passaging A/NWS/33HA-tern/Australia/G70c/75NA(H1N9) influenza virus in medium containing neuraminidase fromMicromonospora viridifaciensand antiserum against the influenza NA. Growth of the resulting mutants is dependent on addition of bacterial neuraminidase to the medium. Nucleotide sequence analysis showed large single deletions in the NA genes, with both ends of the NA gene segments conserved. These RNA fragments all have the capacity to code for a peptide that contains the N-terminal “tail” and membrane-anchoring region of the NA, but the presence of this peptide has not been demonstrated in virions or infected cells. In contrast to the ease of selection of NA-deficient mutants from the H1N9 virus, no mutants were selected from three other viruses. The HA-coding segments of parental H1N9 and mutant NWSc-Mvi predict a change of Pro to His at residue 227 (H3 numbering), close to the receptor-binding site of H3 HA, compared to the HA of an H1N2 reassortant that contains the NWS/33 HA gene. This change may contribute to an altered HA specificity that allows selection of mutants that can infect cells in the presence of high levels of NA activity. It appears that the role of NA in influenza infection is to remove sialic acid from the HA rather than to destroy receptors on cells.</abstract><note>W. Doerfler, Ed.</note><note type="content">Section title: Regular Article</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">1997</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0133-X</identifier><part><date>1997</date><detail type="volume"><number>229</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>308</end></extent><extent unit="pages"><start>155</start><end>165</end></extent></part></relatedItem><identifier type="istex">4973C23EA35B5E25A6EE9221002B8F5CD889B17F</identifier><identifier type="ark">ark:/67375/6H6-N3PQGW6S-0</identifier><identifier type="DOI">10.1006/viro.1996.8421</identifier><identifier type="PII">S0042-6822(96)98421-4</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Academic Press</accessCondition><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><recordOrigin>Academic Press, ©1997</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-N3PQGW6S-0/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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