Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
Identifieur interne : 000393 ( Istex/Corpus ); précédent : 000392; suivant : 000394Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
Auteurs : G. M. Air ; L. R. Ritchie ; W. G. Laver ; P. M. ColmanSource :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Amino, Amino acid, Amino acid sequence, Amino acids, Antigenic sites, Buffer gradient, Cdna, Cdna copy, Coding information, Dideoxy method, Ecori sites, Hemagglutinating neuraminidase, Hemagglutinin, Influenza, Influenza virus, Influenza virus neuraminidase, Laver, Neuraminidase, Neuraminidase gene, Nucleic acids, Nucleotide, Nucleotide sequence, Nucleotide sequence coding, Other influenza, Peptide, Plasmid puc9, Primer, Protein sequence, Sequence analysis, Sequencing, Sialic acid binding site, Subtype sequences, Synthetic oligonucleotides, Tryptic peptides, Universal primer, Virology, Virus neuraminidase.
Abstract
Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.
Url:
DOI: 10.1016/0042-6822(85)90206-5
Links to Exploration step
ISTEX:90954EB5614BF3EB8A03386AA4D4528D2A399DB3Le document en format XML
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Box 334, Canberra City, ACT 2601, Australia</mods:affiliation></affiliation></author><author><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. 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Air</name><affiliation><mods:affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</mods:affiliation></affiliation></author><author><name sortKey="Ritchie, L R" sort="Ritchie, L R" uniqKey="Ritchie L" first="L. R." last="Ritchie">L. R. Ritchie</name><affiliation><mods:affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</mods:affiliation></affiliation></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name><affiliation><mods:affiliation>John Curtin School of Medical Research, P.O. Box 334, Canberra City, ACT 2601, Australia</mods:affiliation></affiliation></author><author><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name><affiliation><mods:affiliation>Commonwealth Scientific and Industrial Research Organization, Division of Protein Chemistry, 3.43 Royal Parade, Parkville, Victoria 3052, Australia</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="1985">1985</date><biblScope unit="volume">145</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="117">117</biblScope><biblScope unit="page" to="122">122</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 acid</term><term>Amino acid sequence</term><term>Amino acids</term><term>Antigenic sites</term><term>Buffer gradient</term><term>Cdna</term><term>Cdna copy</term><term>Coding information</term><term>Dideoxy method</term><term>Ecori sites</term><term>Hemagglutinating neuraminidase</term><term>Hemagglutinin</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Laver</term><term>Neuraminidase</term><term>Neuraminidase gene</term><term>Nucleic acids</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Nucleotide sequence coding</term><term>Other influenza</term><term>Peptide</term><term>Plasmid puc9</term><term>Primer</term><term>Protein sequence</term><term>Sequence analysis</term><term>Sequencing</term><term>Sialic acid binding site</term><term>Subtype sequences</term><term>Synthetic oligonucleotides</term><term>Tryptic peptides</term><term>Universal primer</term><term>Virology</term><term>Virus neuraminidase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>laver</json:string><json:string>cdna</json:string><json:string>primer</json:string><json:string>sequencing</json:string><json:string>influenza</json:string><json:string>virology</json:string><json:string>hemagglutinin</json:string><json:string>influenza virus</json:string><json:string>cdna copy</json:string><json:string>influenza virus neuraminidase</json:string><json:string>protein sequence</json:string><json:string>nucleotide sequence</json:string><json:string>nucleotide</json:string><json:string>peptide</json:string><json:string>amino</json:string><json:string>amino acids</json:string><json:string>nucleic acids</json:string><json:string>tryptic peptides</json:string><json:string>other influenza</json:string><json:string>plasmid puc9</json:string><json:string>subtype sequences</json:string><json:string>coding information</json:string><json:string>amino acid sequence</json:string><json:string>buffer gradient</json:string><json:string>sequence analysis</json:string><json:string>neuraminidase gene</json:string><json:string>ecori sites</json:string><json:string>synthetic oligonucleotides</json:string><json:string>hemagglutinating neuraminidase</json:string><json:string>amino acid</json:string><json:string>dideoxy method</json:string><json:string>sialic acid binding site</json:string><json:string>nucleotide sequence coding</json:string><json:string>antigenic sites</json:string><json:string>virus neuraminidase</json:string><json:string>universal primer</json:string></teeft></keywords><author><json:item><name>G.M. Air</name><affiliations><json:string>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</json:string></affiliations></json:item><json:item><name>L.R. Ritchie</name><affiliations><json:string>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</json:string></affiliations></json:item><json:item><name>W.G. Laver</name><affiliations><json:string>John Curtin School of Medical Research, P.O. Box 334, Canberra City, ACT 2601, Australia</json:string></affiliations></json:item><json:item><name>P.M. Colman</name><affiliations><json:string>Commonwealth Scientific and Industrial Research Organization, Division of Protein Chemistry, 3.43 Royal Parade, Parkville, Victoria 3052, Australia</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-GKFBQNWC-W</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>184</abstractWordCount><abstractCharCount>1118</abstractCharCount><keywordCount>0</keywordCount><score>6.275</score><pdfWordCount>2067</pdfWordCount><pdfCharCount>16970</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize></qualityIndicators><title>Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</title><pmid><json:string>4013081</json:string></pmid><pii><json:string>0042-6822(85)90206-5</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>80</volume><pages><first>3963</first><last>3965</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1985</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0604-6</json:string></pii><volume>145</volume><issue>1</issue><pages><first>117</first><last>122</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1985</json:string></date><geogName></geogName><orgName><json:string>AIR Institutes</json:string><json:string>Research Organization, Division of Protein Chemistry</json:string><json:string>Australia Received</json:string><json:string>Grants AIAI-19084</json:string></orgName><orgName_funder><json:string>Grants AIAI-19084</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>G. M. Air</json:string><json:string>Rodney Tucker</json:string><json:string>Randy Owens</json:string><json:string>Jeff Engler</json:string><json:string>R. G. Webster</json:string><json:string>P. M. Colman</json:string><json:string>W. G. Laver</json:string><json:string>Derrick Mann</json:string><json:string>V. S. Hinshaw</json:string></persName><placeName><json:string>Birmingham</json:string><json:string>Australia</json:string><json:string>Canberra City</json:string><json:string>Tokyo</json:string><json:string>SUHl</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Blok and Air, 1982</json:string><json:string>Colman and Ward, 1985</json:string><json:string>A/Tokyo/3/67; Lentz et cd, 1984</json:string><json:string>Hiebert et &, 1985</json:string><json:string>Newton et al, 1983</json:string><json:string>Varghese et ah, 1983</json:string><json:string>Biggin et ak, 1983</json:string><json:string>Colman et al, 1983</json:string><json:string>dAGCAAAAGCAGG; Blok and Air, 1982</json:string><json:string>Viera and Messing, 1982</json:string><json:string>Both and Air, 1979</json:string><json:string>Varghese et al., 1983</json:string><json:string>Shaw et al, 1982</json:string><json:string>Sanger et al, 1977</json:string><json:string>B/LeeNO; Shaw et al, 1982</json:string><json:string>reviewed by Colman and Ward, 1985</json:string><json:string>Lentz et ab, 1984</json:string><json:string>Air, 1979</json:string><json:string>Webster, 1970</json:string><json:string>Skehel and Hay, 1978</json:string><json:string>Laver et al., 1978</json:string><json:string>Norrander et al, 1983</json:string><json:string>Laver, 1978</json:string><json:string>Laver et aL, 1984</json:string><json:string>Birnboim and Doly 1979; Maniatis et cd, 1982</json:string><json:string>Laver et al, 1984</json:string><json:string>Lentz et al, 1984</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-GKFBQNWC-W</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><json:string>4 - industries agroalimentaires</json:string></inist></categories><publicationDate>1985</publicationDate><copyrightDate>1985</copyrightDate><doi><json:string>10.1016/0042-6822(85)90206-5</json:string></doi><id>90954EB5614BF3EB8A03386AA4D4528D2A399DB3</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-GKFBQNWC-W/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-GKFBQNWC-W/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-GKFBQNWC-W/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1985</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></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</title><author xml:id="author-0000"><persName><forename type="first">G.M.</forename><surname>Air</surname></persName><note type="biography">Author to whom requests for reprints should be addressed.</note><affiliation>Author to whom requests for reprints should be addressed.</affiliation><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">L.R.</forename><surname>Ritchie</surname></persName><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">W.G.</forename><surname>Laver</surname></persName><affiliation>John Curtin School of Medical Research, P.O. Box 334, Canberra City, ACT 2601, Australia</affiliation></author><author xml:id="author-0003"><persName><forename type="first">P.M.</forename><surname>Colman</surname></persName><affiliation>Commonwealth Scientific and Industrial Research Organization, Division of Protein Chemistry, 3.43 Royal Parade, Parkville, Victoria 3052, Australia</affiliation></author><idno type="istex">90954EB5614BF3EB8A03386AA4D4528D2A399DB3</idno><idno type="ark">ark:/67375/6H6-GKFBQNWC-W</idno><idno type="DOI">10.1016/0042-6822(85)90206-5</idno><idno type="PII">0042-6822(85)90206-5</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)X0604-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1985"></date><biblScope unit="volume">145</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="117">117</biblScope><biblScope unit="page" to="122">122</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1985</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</p></abstract></profileDesc><revisionDesc><change when="1985">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-GKFBQNWC-W/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>85902065</aid><ce:pii>0042-6822(85)90206-5</ce:pii><ce:doi>10.1016/0042-6822(85)90206-5</ce:doi><ce:copyright type="unknown" year="1985"></ce:copyright></item-info><head><ce:title>Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</ce:title><ce:author-group><ce:author><ce:given-name>G.M.</ce:given-name><ce:surname>Air</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>L.R.</ce:given-name><ce:surname>Ritchie</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>W.G.</ce:given-name><ce:surname>Laver</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>P.M.</ce:given-name><ce:surname>Colman</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>John Curtin School of Medical Research, P.O. Box 334, Canberra City, ACT 2601, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Commonwealth Scientific and Industrial Research Organization, Division of Protein Chemistry, 3.43 Royal Parade, Parkville, Victoria 3052, Australia</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>Author to whom requests for reprints should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="2" month="4" year="1985"></ce:date-received><ce:date-accepted day="24" month="4" year="1985"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity <ce:cross-ref refid="BIB12">(W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984)</ce:cross-ref>, <ce:italic>Virology</ce:italic>, <ce:bold>137</ce:bold>, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using <ce:italic>Sal</ce:italic>I linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity</title></titleInfo><name type="personal"><namePart type="given">G.M.</namePart><namePart type="family">Air</namePart><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation><description>Author to whom requests for reprints should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">L.R.</namePart><namePart type="family">Ritchie</namePart><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.G.</namePart><namePart type="family">Laver</namePart><affiliation>John Curtin School of Medical Research, P.O. Box 334, Canberra City, ACT 2601, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.M.</namePart><namePart type="family">Colman</namePart><affiliation>Commonwealth Scientific and Industrial Research Organization, Division of Protein Chemistry, 3.43 Royal Parade, Parkville, Victoria 3052, Australia</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">1985</dateIssued><copyrightDate encoding="w3cdtf">1985</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: An influenza virus neuraminidase (NA) of the N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R. G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology, 137, 314–323). To determine sequence relationships between this NA and other known NA and HA subtype sequences, and as a necessary step toward a complete structure determination, we have cloned a full-length copy of the coding sequence of the N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using SalI linkers. The gene was sequenced by directed subcloning into the single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy procedure. Most of the NA sequence was also obtained by direct protein sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared to N1 or N2 sequences, respectively. There is no significant homology to any known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the other NA molecules, the N9 NA is anchored in the membrane by an N-terminal hydrophobic region, from which biologically active heads can be released by pronase.</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">1985</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0604-6</identifier><part><date>1985</date><detail type="volume"><number>145</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>201</end></extent><extent unit="pages"><start>117</start><end>122</end></extent></part></relatedItem><identifier type="istex">90954EB5614BF3EB8A03386AA4D4528D2A399DB3</identifier><identifier type="ark">ark:/67375/6H6-GKFBQNWC-W</identifier><identifier type="DOI">10.1016/0042-6822(85)90206-5</identifier><identifier type="PII">0042-6822(85)90206-5</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-GKFBQNWC-W/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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