Antigenic, sequence, and crystal variation in influenza B neuraminidase
Identifieur interne : 002108 ( Istex/Corpus ); précédent : 002107; suivant : 002109Antigenic, sequence, and crystal variation in influenza B neuraminidase
Auteurs : Gillian M. Air ; W. Graeme Laver ; Ming Luo ; Stephen J. Stray ; Gayla Legrone ; Robert G. WebsterSource :
- Virology [ 0042-6822 ] ; 1990.
English descriptors
- Teeft :
- Academic press, Acid change, Amino, Amino acid, Amino acid sequence, Amino acid sequence changes, Amino acid sequences, Amino acids, Antibody, Antigenic, Antigenic drift, Antigenic properties, Antigenic variants, Cdna sequences, Cell membrane, Crystal morphology, Diffraction studies, Embryonated eggs, Enzyme activity, Field strains, Hemagglutinin, Hemagglutinin molecule, High variation, Hybridoma, Identical reactivities, Influenza, Influenza type, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Laver, Monoclonal, Monoclonal antibodies, Mutant, Neuraminidase, Nucleotide, Nucleotide changes, Nucleotide sequence, Nucleotide sequences, Parental virus, Reassortant, Reassortant virus, Remarkable differences, Second reading frame, Sequence analysis, Sequence changes, Sequence conservation, Sequence variation, Structure determination, Surface glycoprotein, Vapor diffusion, Variable region, Viral, Virology, Virus, Virus neuraminidase.
Abstract
Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.
Url:
DOI: 10.1016/0042-6822(90)90523-T
Links to Exploration step
ISTEX:5A35221A90A44E77407B2B831155220592B9BE2ELe document en format XML
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Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990">1990</date><biblScope unit="volume">177</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="578">578</biblScope><biblScope unit="page" to="587">587</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Acid change</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence</term><term>Amino acid sequence changes</term><term>Amino acid sequences</term><term>Amino acids</term><term>Antibody</term><term>Antigenic</term><term>Antigenic drift</term><term>Antigenic properties</term><term>Antigenic variants</term><term>Cdna sequences</term><term>Cell membrane</term><term>Crystal morphology</term><term>Diffraction studies</term><term>Embryonated eggs</term><term>Enzyme activity</term><term>Field strains</term><term>Hemagglutinin</term><term>Hemagglutinin molecule</term><term>High variation</term><term>Hybridoma</term><term>Identical reactivities</term><term>Influenza</term><term>Influenza type</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Laver</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Mutant</term><term>Neuraminidase</term><term>Nucleotide</term><term>Nucleotide changes</term><term>Nucleotide sequence</term><term>Nucleotide sequences</term><term>Parental virus</term><term>Reassortant</term><term>Reassortant virus</term><term>Remarkable differences</term><term>Second reading frame</term><term>Sequence analysis</term><term>Sequence changes</term><term>Sequence conservation</term><term>Sequence variation</term><term>Structure determination</term><term>Surface glycoprotein</term><term>Vapor diffusion</term><term>Variable region</term><term>Viral</term><term>Virology</term><term>Virus</term><term>Virus neuraminidase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. 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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>W. Graeme Laver</name><affiliations><json:string>Research Unit, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia</json:string></affiliations></json:item><json:item><name>Ming Luo</name><affiliations><json:string>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</json:string></affiliations></json:item><json:item><name>Stephen J. Stray</name><affiliations><json:string>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</json:string></affiliations></json:item><json:item><name>Gayla Legrone</name><affiliations><json:string>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</json:string></affiliations></json:item><json:item><name>Robert G. Webster</name><affiliations><json:string>St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-ZS8915T7-8</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.</abstract><qualityIndicators><score>8.348</score><pdfWordCount>4440</pdfWordCount><pdfCharCount>31047</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>159</abstractWordCount><abstractCharCount>1145</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Antigenic, sequence, and crystal variation in influenza B neuraminidase</title><pmid><json:string>1695410</json:string></pmid><pii><json:string>0042-6822(90)90523-T</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>87</volume><pages><first>3884</first><last>3888</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1990</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0669-1</json:string></pii><volume>177</volume><issue>2</issue><pages><first>578</first><last>587</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1959</json:string><json:string>1990</json:string></date><geogName></geogName><orgName><json:string>Research Unit, ACT</json:string><json:string>Institute of Virology, Moscow, USSR</json:string><json:string>Jude Children’s Research Hospital</json:string><json:string>University of Wisconsin</json:string><json:string>Medical Research, Australian National University</json:string><json:string>AIR El</json:string><json:string>Australian National University</json:string><json:string>Grants Al</json:string></orgName><orgName_funder><json:string>Grants Al</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Mary Ann</json:string><json:string>Hong Kong</json:string><json:string>Tim Thomas</json:string><json:string>Lili Wong</json:string><json:string>P. Pruett</json:string><json:string>Tennessee Received</json:string><json:string>Anna Browne</json:string></persName><placeName><json:string>Birmingham</json:string><json:string>Singapore</json:string><json:string>Australia</json:string><json:string>Canberra</json:string><json:string>Leningrad</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Bossart et al., 1988</json:string><json:string>Al 27767</json:string><json:string>Laver et al., 1988</json:string><json:string>Els et al., 1985</json:string><json:string>see Air and Laver, 1985</json:string><json:string>Colman and Ward, 1985</json:string><json:string>Williams and Lamb, 1986, 1988</json:string><json:string>Yamashita et al., 1988</json:string><json:string>Krystal et al., 1983</json:string><json:string>Palese et al., 1974</json:string><json:string>Webster and Berton, 1981</json:string><json:string>Tulip et al., 1990</json:string><json:string>Webster et al., 1982, 1988</json:string><json:string>Laver, 1969</json:string><json:string>Oxford et al., 1984</json:string><json:string>Varghese et al., 1983</json:string><json:string>Martinez et al., 1983</json:string><json:string>Colman et al., 1987</json:string><json:string>Lin et al., 1990</json:string><json:string>Blok and Air, 1982a,b</json:string><json:string>Shaw et al. (1982)</json:string><json:string>Baker et al., 1987</json:string><json:string>Air et al., 1990</json:string><json:string>Stoeckle et al. (1987)</json:string><json:string>Hovanec and Air, 1984</json:string><json:string>Williams and Lamb (1988)</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-ZS8915T7-8</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 - immunologie fondamentale</json:string></inist></categories><publicationDate>1990</publicationDate><copyrightDate>1990</copyrightDate><doi><json:string>10.1016/0042-6822(90)90523-T</json:string></doi><id>5A35221A90A44E77407B2B831155220592B9BE2E</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-ZS8915T7-8/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-ZS8915T7-8/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-ZS8915T7-8/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Antigenic, sequence, and crystal variation in influenza B neuraminidase</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>1990</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>Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession Nos. M30631-M30639.</note><note type="content">Section title: Regular article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Antigenic, sequence, and crystal variation in influenza B neuraminidase</title><author xml:id="author-0000"><persName><forename type="first">Gillian M.</forename><surname>Air</surname></persName><note type="biography">To whom reprint requests should be addressed.</note><affiliation>To whom reprint requests 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">W.</forename><surname>Graeme Laver</surname></persName><affiliation>Research Unit, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Ming</forename><surname>Luo</surname></persName><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Stephen J.</forename><surname>Stray</surname></persName><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Gayla</forename><surname>Legrone</surname></persName><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Robert G.</forename><surname>Webster</surname></persName><affiliation>St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation></author><idno type="istex">5A35221A90A44E77407B2B831155220592B9BE2E</idno><idno type="ark">ark:/67375/6H6-ZS8915T7-8</idno><idno type="DOI">10.1016/0042-6822(90)90523-T</idno><idno type="PII">0042-6822(90)90523-T</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)X0669-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990"></date><biblScope unit="volume">177</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="578">578</biblScope><biblScope unit="page" to="587">587</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1990</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.</p></abstract></profileDesc><revisionDesc><change when="1990">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-ZS8915T7-8/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>9090523T</aid><ce:pii>0042-6822(90)90523-T</ce:pii><ce:doi>10.1016/0042-6822(90)90523-T</ce:doi><ce:copyright type="unknown" year="1990"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession Nos. M30631-M30639.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Regular article</ce:textfn></ce:dochead><ce:title>Antigenic, sequence, and crystal variation in influenza B neuraminidase</ce:title><ce:author-group><ce:author><ce:given-name>Gillian M.</ce:given-name><ce:surname>Air</ce:surname><ce:cross-ref refid="COR1"><ce:sup>2</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>W.</ce:given-name><ce:surname>Graeme Laver</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Ming</ce:given-name><ce:surname>Luo</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Stephen J.</ce:given-name><ce:surname>Stray</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Gayla</ce:given-name><ce:surname>Legrone</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Robert G.</ce:given-name><ce:surname>Webster</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>Research Unit, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>2</ce:label><ce:text>To whom reprint requests should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="13" month="12" year="1989"></ce:date-received><ce:date-accepted day="19" month="3" year="1990"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Antigenic, sequence, and crystal variation in influenza B neuraminidase</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Antigenic, sequence, and crystal variation in influenza B neuraminidase</title></titleInfo><name type="personal"><namePart type="given">Gillian M.</namePart><namePart type="family">Air</namePart><affiliation>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.</namePart><namePart type="family">Graeme Laver</namePart><affiliation>Research Unit, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ming</namePart><namePart type="family">Luo</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">Stephen J.</namePart><namePart type="family">Stray</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">Gayla</namePart><namePart type="family">Legrone</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">Robert G.</namePart><namePart type="family">Webster</namePart><affiliation>St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101, USA</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">1990</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.</abstract><note>Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession Nos. M30631-M30639.</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">1990</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0669-1</identifier><part><date>1990</date><detail type="volume"><number>177</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>419</start><end>851</end></extent><extent unit="pages"><start>578</start><end>587</end></extent></part></relatedItem><identifier type="istex">5A35221A90A44E77407B2B831155220592B9BE2E</identifier><identifier type="ark">ark:/67375/6H6-ZS8915T7-8</identifier><identifier type="DOI">10.1016/0042-6822(90)90523-T</identifier><identifier type="PII">0042-6822(90)90523-T</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-ZS8915T7-8/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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