Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus
The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a to...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1982-11, Vol.79 (22), p.6817-6821 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6821 |
|---|---|
| container_issue | 22 |
| container_start_page | 6817 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 79 |
| creator | Shaw, Michael W. Lamb, Robert A. Erickson, Bruce W. Briedis, Dalius J. Choppin, Purnell W. |
| description | The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved. |
| doi_str_mv | 10.1073/pnas.79.22.6817 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_347224</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>12979</jstor_id><sourcerecordid>12979</sourcerecordid><originalsourceid>FETCH-LOGICAL-c492t-5236a52bd427e3b0fc1e8afe467cc844c0e8bb3f4fc411038c2ab891a834b9773</originalsourceid><addsrcrecordid>eNqFkTtvFDEURi0ECpuQGgkJNBWpZuPXjO0iRbKCEBFBAaG1PN5rMpFnvLE9EeHX481uHjQgFy7O-a7u1YfQa4LnBAt2uBpNmgs1p3TeSiKeoRnBitQtV_g5mmFMRS055S_RbkpXGGPVSLyDdlqqeNvwGfq8CMPKQ4bqy2Q9hNwvofoG1xOMFqrgqnxZEEzRDP3YL02C6hTGO3I2Ol-036Y6qX70cUqv0AtnfIL97b-HLj5--L74VJ9_PT1bHJ_Xliua64ay1jS0W3IqgHXYWQLSOOCtsFZybjHIrmOOO8sJwUxaajqpiJGMd0oItoeONnNXUzfA0sKYo_F6FfvBxFsdTK__JmN_qX-GG824oJSX_PttPoZyaMp66JMF780IYUpaYspUef8VSdNQItumiIcb0caQUgT3sAzBet2TXvekhdKU6nVPJfH26Q0P_raYwg-2fB28p48DtJu8z_ArF_PdP80ivNkIVymH-LgZVUKxPxvVsH0</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15521865</pqid></control><display><type>article</type><title>Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Shaw, Michael W. ; Lamb, Robert A. ; Erickson, Bruce W. ; Briedis, Dalius J. ; Choppin, Purnell W.</creator><creatorcontrib>Shaw, Michael W. ; Lamb, Robert A. ; Erickson, Bruce W. ; Briedis, Dalius J. ; Choppin, Purnell W.</creatorcontrib><description>The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.79.22.6817</identifier><identifier>PMID: 6294654</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino acids ; Base Sequence ; Cercopithecine herpesvirus 1 ; Cloning, Molecular ; Codons ; DNA ; DNA Restriction Enzymes ; Generally accepted auditing standards ; Genes ; Genes, Viral ; HeLa Cells ; Humans ; Influenza A virus ; influenza B virus ; Messenger RNA ; Neuraminidase - genetics ; Nucleic Acid Hybridization ; Nucleotide sequences ; Nucleotides ; Orthomyxoviridae - enzymology ; Orthomyxoviridae - genetics ; RNA, Messenger - genetics ; Virion - genetics ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1982-11, Vol.79 (22), p.6817-6821</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-5236a52bd427e3b0fc1e8afe467cc844c0e8bb3f4fc411038c2ab891a834b9773</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/79/22.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/12979$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/12979$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6294654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shaw, Michael W.</creatorcontrib><creatorcontrib>Lamb, Robert A.</creatorcontrib><creatorcontrib>Erickson, Bruce W.</creatorcontrib><creatorcontrib>Briedis, Dalius J.</creatorcontrib><creatorcontrib>Choppin, Purnell W.</creatorcontrib><title>Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.</description><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Cercopithecine herpesvirus 1</subject><subject>Cloning, Molecular</subject><subject>Codons</subject><subject>DNA</subject><subject>DNA Restriction Enzymes</subject><subject>Generally accepted auditing standards</subject><subject>Genes</subject><subject>Genes, Viral</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Influenza A virus</subject><subject>influenza B virus</subject><subject>Messenger RNA</subject><subject>Neuraminidase - genetics</subject><subject>Nucleic Acid Hybridization</subject><subject>Nucleotide sequences</subject><subject>Nucleotides</subject><subject>Orthomyxoviridae - enzymology</subject><subject>Orthomyxoviridae - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>Virion - genetics</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkTtvFDEURi0ECpuQGgkJNBWpZuPXjO0iRbKCEBFBAaG1PN5rMpFnvLE9EeHX481uHjQgFy7O-a7u1YfQa4LnBAt2uBpNmgs1p3TeSiKeoRnBitQtV_g5mmFMRS055S_RbkpXGGPVSLyDdlqqeNvwGfq8CMPKQ4bqy2Q9hNwvofoG1xOMFqrgqnxZEEzRDP3YL02C6hTGO3I2Ol-036Y6qX70cUqv0AtnfIL97b-HLj5--L74VJ9_PT1bHJ_Xliua64ay1jS0W3IqgHXYWQLSOOCtsFZybjHIrmOOO8sJwUxaajqpiJGMd0oItoeONnNXUzfA0sKYo_F6FfvBxFsdTK__JmN_qX-GG824oJSX_PttPoZyaMp66JMF780IYUpaYspUef8VSdNQItumiIcb0caQUgT3sAzBet2TXvekhdKU6nVPJfH26Q0P_raYwg-2fB28p48DtJu8z_ArF_PdP80ivNkIVymH-LgZVUKxPxvVsH0</recordid><startdate>19821101</startdate><enddate>19821101</enddate><creator>Shaw, Michael W.</creator><creator>Lamb, Robert A.</creator><creator>Erickson, Bruce W.</creator><creator>Briedis, Dalius J.</creator><creator>Choppin, Purnell W.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19821101</creationdate><title>Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus</title><author>Shaw, Michael W. ; Lamb, Robert A. ; Erickson, Bruce W. ; Briedis, Dalius J. ; Choppin, Purnell W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-5236a52bd427e3b0fc1e8afe467cc844c0e8bb3f4fc411038c2ab891a834b9773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Amino acids</topic><topic>Base Sequence</topic><topic>Cercopithecine herpesvirus 1</topic><topic>Cloning, Molecular</topic><topic>Codons</topic><topic>DNA</topic><topic>DNA Restriction Enzymes</topic><topic>Generally accepted auditing standards</topic><topic>Genes</topic><topic>Genes, Viral</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Influenza A virus</topic><topic>influenza B virus</topic><topic>Messenger RNA</topic><topic>Neuraminidase - genetics</topic><topic>Nucleic Acid Hybridization</topic><topic>Nucleotide sequences</topic><topic>Nucleotides</topic><topic>Orthomyxoviridae - enzymology</topic><topic>Orthomyxoviridae - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>Virion - genetics</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shaw, Michael W.</creatorcontrib><creatorcontrib>Lamb, Robert A.</creatorcontrib><creatorcontrib>Erickson, Bruce W.</creatorcontrib><creatorcontrib>Briedis, Dalius J.</creatorcontrib><creatorcontrib>Choppin, Purnell W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shaw, Michael W.</au><au>Lamb, Robert A.</au><au>Erickson, Bruce W.</au><au>Briedis, Dalius J.</au><au>Choppin, Purnell W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1982-11-01</date><risdate>1982</risdate><volume>79</volume><issue>22</issue><spage>6817</spage><epage>6821</epage><pages>6817-6821</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6294654</pmid><doi>10.1073/pnas.79.22.6817</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1982-11, Vol.79 (22), p.6817-6821 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_347224 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Base Sequence Cercopithecine herpesvirus 1 Cloning, Molecular Codons DNA DNA Restriction Enzymes Generally accepted auditing standards Genes Genes, Viral HeLa Cells Humans Influenza A virus influenza B virus Messenger RNA Neuraminidase - genetics Nucleic Acid Hybridization Nucleotide sequences Nucleotides Orthomyxoviridae - enzymology Orthomyxoviridae - genetics RNA, Messenger - genetics Virion - genetics Viruses |
| title | Complete Nucleotide Sequence of the Neuraminidase Gene of Influenza B Virus |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T14%3A22%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Complete%20Nucleotide%20Sequence%20of%20the%20Neuraminidase%20Gene%20of%20Influenza%20B%20Virus&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Shaw,%20Michael%20W.&rft.date=1982-11-01&rft.volume=79&rft.issue=22&rft.spage=6817&rft.epage=6821&rft.pages=6817-6821&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.79.22.6817&rft_dat=%3Cjstor_pubme%3E12979%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15521865&rft_id=info:pmid/6294654&rft_jstor_id=12979&rfr_iscdi=true |