Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA
Identifieur interne : 000F64 ( Istex/Corpus ); précédent : 000F63; suivant : 000F65Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA
Auteurs : Lewis Markoff ; Ching-Juh LaiSource :
- Virology [ 0042-6822 ] ; 1982.
English descriptors
- Teeft :
- Acid, Acid sequence, Acid sequences, Amino, Amino acid changes, Amino acid homology, Amino acid position, Amino acid sequence, Amino acid sequences, Amino acids, Antigenic, Antigenic shift, Antigenic variation, Avian strain, Base pairs, Complete nucleotide, Complete nucleotide sequence, Complete structure, Cysteine, Cysteine residues, Enzyme activity, Functional sites, Gene, Glycosylation, Graphic matrix comparison, Hemagglutinin, Homology, Hong kong, Human influenza, Human influenza virus, Hydrophobic, Hydrophobic region, Influenza, Influenza cdna, Influenza virus, Influenza virus mrna, Influenza virus neuraminidase, Influenza viruses, Insertion, Laver, Linker residues, Markoff, Matrix comparison, Matrix protein, Membrane fusion, Membrane insertion, Molecular weight, Mrna, Neuraminidase, Neuraminidase gene, Nonviral oligonucleotide, Nucleic acids, Nucleotide, Nucleotide sequence, Nucleotide sequences, Nucleotide sequencing, Palese, Plasmid, Point mutations, Polypeptide, Potential glycosylation sites, Schematic representation, Schulman, Segment encoding, Sense strand, Sequence data, Sequencing, Termination codon, Viral, Virion, Virology.
Abstract
Abstract: A complete nucleotide sequence was determined from cloned full-length DNA of the influenza A/Udorn/72 (H3N2) neuraminidase gene. The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH2 terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.
Url:
DOI: 10.1016/0042-6822(82)90089-7
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ISTEX:4702C104C80E07AF08348B1979BA10F4484F2F1CLe document en format XML
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The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH2 terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>antigenic</json:string><json:string>amino</json:string><json:string>influenza</json:string><json:string>palese</json:string><json:string>cysteine</json:string><json:string>homology</json:string><json:string>amino acids</json:string><json:string>sequencing</json:string><json:string>mrna</json:string><json:string>hemagglutinin</json:string><json:string>virion</json:string><json:string>viral</json:string><json:string>markoff</json:string><json:string>cysteine residues</json:string><json:string>influenza virus</json:string><json:string>schulman</json:string><json:string>plasmid</json:string><json:string>polypeptide</json:string><json:string>amino acid sequences</json:string><json:string>nucleotide</json:string><json:string>glycosylation</json:string><json:string>amino acid sequence</json:string><json:string>virology</json:string><json:string>laver</json:string><json:string>potential glycosylation sites</json:string><json:string>hydrophobic region</json:string><json:string>influenza viruses</json:string><json:string>complete nucleotide sequence</json:string><json:string>neuraminidase gene</json:string><json:string>amino acid homology</json:string><json:string>enzyme activity</json:string><json:string>insertion</json:string><json:string>nucleotide sequence</json:string><json:string>base pairs</json:string><json:string>termination codon</json:string><json:string>antigenic shift</json:string><json:string>nucleotide sequences</json:string><json:string>human influenza</json:string><json:string>molecular weight</json:string><json:string>point mutations</json:string><json:string>nucleic acids</json:string><json:string>hydrophobic</json:string><json:string>acid</json:string><json:string>gene</json:string><json:string>schematic representation</json:string><json:string>sequence data</json:string><json:string>nonviral oligonucleotide</json:string><json:string>membrane insertion</json:string><json:string>antigenic variation</json:string><json:string>matrix comparison</json:string><json:string>acid sequences</json:string><json:string>complete nucleotide</json:string><json:string>human influenza virus</json:string><json:string>amino acid changes</json:string><json:string>amino acid position</json:string><json:string>acid sequence</json:string><json:string>functional sites</json:string><json:string>graphic matrix comparison</json:string><json:string>linker residues</json:string><json:string>avian strain</json:string><json:string>sense strand</json:string><json:string>nucleotide sequencing</json:string><json:string>influenza virus mrna</json:string><json:string>membrane fusion</json:string><json:string>complete structure</json:string><json:string>hong kong</json:string><json:string>influenza cdna</json:string><json:string>segment encoding</json:string><json:string>matrix protein</json:string><json:string>influenza virus neuraminidase</json:string></teeft></keywords><author><json:item><name>Lewis Markoff</name><affiliations><json:string>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</json:string></affiliations></json:item><json:item><name>Ching-Juh Lai</name><affiliations><json:string>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-SCGWBL7Z-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: A complete nucleotide sequence was determined from cloned full-length DNA of the influenza A/Udorn/72 (H3N2) neuraminidase gene. The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH2 terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.</abstract><qualityIndicators><score>9.455</score><pdfWordCount>4455</pdfWordCount><pdfCharCount>31588</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>305</abstractWordCount><abstractCharCount>1960</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</title><pmid><json:string>7080447</json:string></pmid><pii><json:string>0042-6822(82)90089-7</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. 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Buckler</json:string><json:string>P. L. Biochemicals</json:string><json:string>LYS ItE</json:string><json:string>The</json:string><json:string>Jacob V. Maize</json:string><json:string>Salome Kruger</json:string><json:string>JoAnn</json:string></persName><placeName><json:string>Milwaukee</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Huang et al., 1980</json:string><json:string>Kendal and Eckert, 19721</json:string><json:string>Rott et al., 1974</json:string><json:string>Kendal and Eckert, 1972</json:string><json:string>45 lysine and arginine residues versus approximately 38 tryptic peptides detected [Kendal and Kiley, 1973</json:string><json:string>Allen et al., 1980</json:string><json:string>Fields et al., 19811</json:string><json:string>Waterfield et al., 19791</json:string><json:string>Gething et al., 1980</json:string><json:string>Robertson et al., 1981</json:string><json:string>Maxam and 290 MARKOFF AND LA1 Gilbert, 1980</json:string><json:string>Rafelson et al., 1963</json:string><json:string>Caton and Robertson, 1980</json:string><json:string>Lai et al., 1981</json:string><json:string>Krug et al.</json:string><json:string>Min Jou et al., 1980</json:string><json:string>Blok and Air, 1980</json:string><json:string>Palese et al., 1974</json:string><json:string>Seif et al., 1979</json:string><json:string>Palese, 1977</json:string><json:string>Fields et al., 1981</json:string><json:string>Lai et al., 1980</json:string><json:string>Palese and Schulman, 1976</json:string><json:string>Webster et al., 1980</json:string><json:string>Bucher and Palese, 1975</json:string><json:string>Lamb and Lai, 1981</json:string><json:string>Laver, 19781</json:string><json:string>Fields and Winter, 1980</json:string><json:string>Blok and Air (1980)</json:string><json:string>Schulman, 1970</json:string><json:string>Porter et al., 1979</json:string><json:string>Wilson et al., 1981</json:string><json:string>Dhar et al., 1980</json:string><json:string>Laver and Webster, 1973</json:string><json:string>Assaad et al., 1980</json:string><json:string>Lamb and Lai, 1980</json:string><json:string>Markoff et al., 1979</json:string><json:string>Fields et al. (1981)</json:string><json:string>Schulman and Palese, 1977</json:string><json:string>Ward and Dopheide, 1979</json:string><json:string>Fang et al., 1981</json:string><json:string>Grunstein and Hogness, 1975</json:string><json:string>Desselberger and Palese, 1978</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-SCGWBL7Z-J</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 - microbiologie</json:string></inist></categories><publicationDate>1982</publicationDate><copyrightDate>1982</copyrightDate><doi><json:string>10.1016/0042-6822(82)90089-7</json:string></doi><id>4702C104C80E07AF08348B1979BA10F4484F2F1C</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-SCGWBL7Z-J/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-SCGWBL7Z-J/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-SCGWBL7Z-J/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</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">Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</title><author xml:id="author-0000"><persName><forename type="first">Lewis</forename><surname>Markoff</surname></persName><affiliation>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Ching-Juh</forename><surname>Lai</surname></persName><affiliation>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</affiliation></author><idno type="istex">4702C104C80E07AF08348B1979BA10F4484F2F1C</idno><idno type="ark">ark:/67375/6H6-SCGWBL7Z-J</idno><idno type="DOI">10.1016/0042-6822(82)90089-7</idno><idno type="PII">0042-6822(82)90089-7</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)X0274-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1982"></date><biblScope unit="volume">119</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="288">288</biblScope><biblScope unit="page" to="297">297</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: A complete nucleotide sequence was determined from cloned full-length DNA of the influenza A/Udorn/72 (H3N2) neuraminidase gene. The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH2 terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.</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-SCGWBL7Z-J/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>82900897</aid><ce:pii>0042-6822(82)90089-7</ce:pii><ce:doi>10.1016/0042-6822(82)90089-7</ce:doi><ce:copyright type="unknown" year="1982"></ce:copyright></item-info><head><ce:title>Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</ce:title><ce:author-group><ce:author><ce:given-name>Lewis</ce:given-name><ce:surname>Markoff</ce:surname></ce:author><ce:author><ce:given-name>Ching-Juh</ce:given-name><ce:surname>Lai</ce:surname></ce:author><ce:affiliation><ce:textfn>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="15" month="12" year="1981"></ce:date-received><ce:date-accepted day="29" month="1" year="1982"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>A complete nucleotide sequence was determined from cloned full-length DNA of the influenza A/Udorn/72 (H3N2) neuraminidase gene. The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH<ce:inf>2</ce:inf> terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Sequence of the influenza A/Udorn/72 (H3N2) virus neuraminidase gene as determined from cloned full-length DNA</title></titleInfo><name type="personal"><namePart type="given">Lewis</namePart><namePart type="family">Markoff</namePart><affiliation>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ching-Juh</namePart><namePart type="family">Lai</namePart><affiliation>Molecular Viral Biology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 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: A complete nucleotide sequence was determined from cloned full-length DNA of the influenza A/Udorn/72 (H3N2) neuraminidase gene. The neuraminidase DNA has a total length of 1466 bases, excluding G-C linker residues. The cloned segment retained the common sequences known to be present at the 3′ and 5′ termini of virion RNA. Also present was a nonviral oligonucleotide nine bases long at the 5′(+) end of the DNA which represents cellular sequences acquired during influenza mRNA synthesis. The sense strand of the DNA contained a single open-reading frame coding for 469 amino acids. A possible polyadenylation site was noted downstream from the termination codon. No mammalian gene splice sequences and no alternate open-reading frame were present. The deduced amino acid sequence displayed the features of other neuraminidase genes, including the conservation of a sequence of 12 amino acids at the NH2 terminus and the presence of a hydrophobic region from amino acid positions 7 to 34. The data were consistent with the hypothesis that this hydrophobic region of the surface glycoprotein represents the site for membrane insertion. When compared to the complete nucleotide and amino acid sequences of the influenza A/PR/8/34 (H1N1) neuraminidase, the N2 sequence revealed conservation of the positions of cysteine residues and potential glycosylation sites. Regions of homology were detected between N1 and N2 amino acid sequences, if cysteine residues of the two polypeptides were aligned. Nucleotide sequence homology between N1 and N2 was evident to a lesser degree. The data suggest that the N2 gene sequence differs from that of the N1 gene by numerous point mutations, as well as by insertion/deletion, and that the antigenic “shift” in the human neuraminidase antigenic subtype in 1957 is most likely to have occurred by replacement of the human N1 gene with one from the animal reservoir of influenza A viruses through gene reassortment.</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)X0274-7</identifier><part><date>1982</date><detail type="volume"><number>119</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>231</start><end>518</end></extent><extent unit="pages"><start>288</start><end>297</end></extent></part></relatedItem><identifier type="istex">4702C104C80E07AF08348B1979BA10F4484F2F1C</identifier><identifier type="ark">ark:/67375/6H6-SCGWBL7Z-J</identifier><identifier type="DOI">10.1016/0042-6822(82)90089-7</identifier><identifier type="PII">0042-6822(82)90089-7</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-SCGWBL7Z-J/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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