Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase
Identifieur interne : 000068 ( Istex/Corpus ); précédent : 000067; suivant : 000069Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase
Auteurs : W. G. Laver ; G. M. Air ; R. G. Webster ; L. J. MarkoffSource :
- Virology [ 0042-6822 ] ; 1982.
English descriptors
- Teeft :
- Amino, Amino acid sequence, Amino acids, Antigenic, Antigenic drift, Antigenic sites, Antigenic variants, Antigenic variation, Assay, Digestion, Field strains, Glutamic acid, Hemagglutinin, Hong kong, Influenza, Influenza virus, Influenza viruses, Laver, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Monoclonal variants, Neuraminidase, Neuraminidase heads, Neuraminidase inhibition tests, Neuraminidase molecule, Neuraminidase molecules, Nucleotide sequence, Peptide, Pronase, Pronase digestion, Recombinant viruses, Sequence change, Sequence changes, Tryptic peptides, Variant, Virology, Virus.
Abstract
Abstract: Pronase-released neuraminidase heads from six strains of influenza type A virus (of the H2N2 and H3N2 subtypes) isolated between 1957 and 1975 were examined for changes in amino acid sequence. In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, Virology 117, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.
Url:
DOI: 10.1016/0042-6822(82)90244-6
Links to Exploration step
ISTEX:2C344DDEEFD59FA32CF8B3F0451BBC1631F74B01Le document en format XML
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In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, Virology 117, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>antigenic</json:string><json:string>monoclonal</json:string><json:string>laver</json:string><json:string>hemagglutinin</json:string><json:string>monoclonal antibodies</json:string><json:string>virology</json:string><json:string>pronase</json:string><json:string>influenza virus</json:string><json:string>field strains</json:string><json:string>influenza</json:string><json:string>sequence changes</json:string><json:string>digestion</json:string><json:string>neuraminidase molecule</json:string><json:string>antigenic variants</json:string><json:string>amino</json:string><json:string>peptide</json:string><json:string>variant</json:string><json:string>amino acids</json:string><json:string>monoclonal antibody</json:string><json:string>antigenic drift</json:string><json:string>pronase digestion</json:string><json:string>monoclonal variants</json:string><json:string>influenza viruses</json:string><json:string>glutamic acid</json:string><json:string>neuraminidase heads</json:string><json:string>neuraminidase molecules</json:string><json:string>assay</json:string><json:string>virus</json:string><json:string>nucleotide sequence</json:string><json:string>sequence change</json:string><json:string>antigenic variation</json:string><json:string>hong kong</json:string><json:string>recombinant viruses</json:string><json:string>tryptic peptides</json:string><json:string>neuraminidase inhibition tests</json:string><json:string>amino acid sequence</json:string><json:string>antigenic sites</json:string></teeft></keywords><author><json:item><name>W.G. Laver</name><affiliations><json:string>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</json:string></affiliations></json:item><json:item><name>G.M. Air</name><affiliations><json:string>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</json:string></affiliations></json:item><json:item><name>R.G. Webster</name><affiliations><json:string>St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</json:string></affiliations></json:item><json:item><name>L.J. Markoff</name><affiliations><json:string>Laboratory of Infectious Diseases, National Institutes of Health, Building 7, Bethesda, Maryland 20205, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-BXV5B252-Q</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Pronase-released neuraminidase heads from six strains of influenza type A virus (of the H2N2 and H3N2 subtypes) isolated between 1957 and 1975 were examined for changes in amino acid sequence. In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, Virology 117, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.</abstract><qualityIndicators><score>8.735</score><pdfWordCount>3735</pdfWordCount><pdfCharCount>28394</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>305</abstractWordCount><abstractCharCount>1943</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase</title><pmid><json:string>6183823</json:string></pmid><pii><json:string>0042-6822(82)90244-6</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Nat. Acad. Sci. 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Colman</json:string><json:string>Mary Ann</json:string><json:string>Hong Kong</json:string><json:string>P.O. Box</json:string><json:string>R. G. Webster</json:string><json:string>Jean Clark</json:string><json:string>W. G. Laver</json:string><json:string>V. S. Hinshaw</json:string><json:string>Kathryn Newton</json:string></persName><placeName><json:string>Birmingham</json:string><json:string>Miami</json:string><json:string>Bangkok</json:string><json:string>Japan</json:string><json:string>Tokyo</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Huang et al., 1980</json:string><json:string>van Wyke et al., 1980</json:string><json:string>Blok and Air, 1982</json:string><json:string>Wilson and Rafelson, 1963</json:string><json:string>Air and Thompson, 1969</json:string><json:string>Hiti and Nayak, 1982</json:string><json:string>Both and Sleigh, 1981</json:string><json:string>Laver and Valentine, 1969</json:string><json:string>Seto et al., 1966</json:string><json:string>Wiley et al., 1981</json:string><json:string>Webster et al., 1982b</json:string><json:string>Palese et al., 1974</json:string><json:string>Mayron et al., 1961</json:string><json:string>Blok et al., 1982</json:string><json:string>Fields et al., 1981</json:string><json:string>Laver, 1969</json:string><json:string>Laver et al., 1974</json:string><json:string>Webster et al., 1982a</json:string><json:string>Udenfriend et al., 1972</json:string><json:string>Laver et al., 1979</json:string><json:string>Webster et al., 198213</json:string><json:string>Aymard-Henry et al., 1973</json:string><json:string>Ward and Dopheide 1981</json:string><json:string>Webster and Laver, 1973</json:string><json:string>Skehel and Waterfield 1975; Dopheide and Ward, 1981</json:string><json:string>Webster and Laver, 1967</json:string><json:string>Drzeniek et al., 1966</json:string><json:string>Laver, 1978</json:string><json:string>Markoff and Lai, 1982</json:string><json:string>Fang et al., 1981</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-BXV5B252-Q</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>1982</publicationDate><copyrightDate>1982</copyrightDate><doi><json:string>10.1016/0042-6822(82)90244-6</json:string></doi><id>2C344DDEEFD59FA32CF8B3F0451BBC1631F74B01</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-BXV5B252-Q/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-BXV5B252-Q/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-BXV5B252-Q/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Amino acid sequence changes in antigenic variants of type A influenza virus N2 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>1982</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">Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase</title><author xml:id="author-0000"><persName><forename type="first">W.G.</forename><surname>Laver</surname></persName><note type="biography">Author to whom reprint requests should be addressed.</note><affiliation>Author to whom reprint requests should be addressed.</affiliation><affiliation>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</affiliation></author><author xml:id="author-0001"><persName><forename type="first">G.M.</forename><surname>Air</surname></persName><note type="biography">Present address: Department of Microbiology, University of Alabama in Birmingham, Birmingham, Ala. 35294.</note><affiliation>Present address: Department of Microbiology, University of Alabama in Birmingham, Birmingham, Ala. 35294.</affiliation><affiliation>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</affiliation></author><author xml:id="author-0002"><persName><forename type="first">R.G.</forename><surname>Webster</surname></persName><affiliation>St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">L.J.</forename><surname>Markoff</surname></persName><affiliation>Laboratory of Infectious Diseases, National Institutes of Health, Building 7, Bethesda, Maryland 20205, USA</affiliation></author><idno type="istex">2C344DDEEFD59FA32CF8B3F0451BBC1631F74B01</idno><idno type="ark">ark:/67375/6H6-BXV5B252-Q</idno><idno type="DOI">10.1016/0042-6822(82)90244-6</idno><idno type="PII">0042-6822(82)90244-6</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)X0292-9</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1982"></date><biblScope unit="volume">122</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="450">450</biblScope><biblScope unit="page" to="460">460</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1982</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Pronase-released neuraminidase heads from six strains of influenza type A virus (of the H2N2 and H3N2 subtypes) isolated between 1957 and 1975 were examined for changes in amino acid sequence. In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, Virology 117, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.</p></abstract></profileDesc><revisionDesc><change when="1982">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-BXV5B252-Q/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>82902446</aid><ce:pii>0042-6822(82)90244-6</ce:pii><ce:doi>10.1016/0042-6822(82)90244-6</ce:doi><ce:copyright type="unknown" year="1982"></ce:copyright></item-info><head><ce:title>Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase</ce:title><ce:author-group><ce:author><ce:given-name>W.G.</ce:given-name><ce:surname>Laver</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>G.M.</ce:given-name><ce:surname>Air</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>R.G.</ce:given-name><ce:surname>Webster</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>L.J.</ce:given-name><ce:surname>Markoff</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>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Laboratory of Infectious Diseases, National Institutes of Health, Building 7, Bethesda, Maryland 20205, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>Author to whom reprint requests should be addressed.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>2</ce:label><ce:note-para>Present address: Department of Microbiology, University of Alabama in Birmingham, Birmingham, Ala. 35294.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="4" month="5" year="1982"></ce:date-received><ce:date-accepted day="28" month="6" year="1982"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Pronase-released neuraminidase heads from six strains of influenza type A virus (of the H2N2 and H3N2 subtypes) isolated between 1957 and 1975 were examined for changes in amino acid sequence. In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, <ce:italic>Virology</ce:italic> <ce:bold>117</ce:bold>, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Amino acid sequence changes in antigenic variants of type A influenza virus N2 neuraminidase</title></titleInfo><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, Australian National University, Canberra, ACT 2601, Australia</affiliation><description>Author to whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.M.</namePart><namePart type="family">Air</namePart><affiliation>John Curtin School of Medical Research, P.O. Box 334, Australian National University, Canberra, ACT 2601, Australia</affiliation><description>Present address: Department of Microbiology, University of Alabama in Birmingham, Birmingham, Ala. 35294.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.G.</namePart><namePart type="family">Webster</namePart><affiliation>St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">L.J.</namePart><namePart type="family">Markoff</namePart><affiliation>Laboratory of Infectious Diseases, National Institutes of Health, Building 7, Bethesda, Maryland 20205, 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">1982</dateIssued><copyrightDate encoding="w3cdtf">1982</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Pronase-released neuraminidase heads from six strains of influenza type A virus (of the H2N2 and H3N2 subtypes) isolated between 1957 and 1975 were examined for changes in amino acid sequence. In 469 residues 19 changes which occurred during this period were located. Two regions of the neuraminidase molecule were not examined, residues 188–210 which were insoluble, and residues 1–73 (or 76) which formed part of the stalk of the neuraminidase and were removed during Pronase digestion. Neuraminidase heads from seven variants of A/Tokyo/3/67 virus, selected with different monoclonal antibodies to the neuraminidase were also examined for sequence changes. In four of these, a single sequence change at position 344 of arginine to isoleucine was found, in another variant an asparagine residue at position 221 changed to histidine and in another the lysine at position 368 changed to glutamic acid. This last change also occurred in the field strains isolated in 1972 and 1975. In the seventh monoclonal variant the change could not be found and may be in the insoluble region. Some of these sequence changes were clustered into two highly variable regions in the neuraminidase comprising residues 344–347 and 367–370, suggesting that these regions may be involved in antigenic sites on the neuraminidase molecule. An antigenic map of N2 neuraminidase [R. G. Webster, V. S. Hinshaw, and W. G. Laver, Virology 117, 93–104 (1982)] suggested three or four nonoverlapping antigenic areas and the variants with changes at residues 344 and 368 were grouped in one of these antigenic regions. Sequence changes in the region of 344–347 were also associated with changes in the stability of the neuraminidase. The four monoclonal variants with a sequence change of Arg (344) to Ile possessed neuraminidase molecules which were destroyed by Pronase at 37° (but not at 20°) whereas wild-type neuraminidase was stable during digestion at 37°.</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">1982</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0292-9</identifier><part><date>1982</date><detail type="volume"><number>122</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>229</start><end>525</end></extent><extent unit="pages"><start>450</start><end>460</end></extent></part></relatedItem><identifier type="istex">2C344DDEEFD59FA32CF8B3F0451BBC1631F74B01</identifier><identifier type="ark">ark:/67375/6H6-BXV5B252-Q</identifier><identifier type="DOI">10.1016/0042-6822(82)90244-6</identifier><identifier type="PII">0042-6822(82)90244-6</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-BXV5B252-Q/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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