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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.</title><author><name sortKey="Jin, H" sort="Jin, H" uniqKey="Jin H" first="H" last="Jin">H. Jin</name></author><author><name sortKey="Leser, G P" sort="Leser, G P" uniqKey="Leser G" first="G P" last="Leser">G P Leser</name></author><author><name sortKey="Zhang, J" sort="Zhang, J" uniqKey="Zhang J" first="J" last="Zhang">J. Zhang</name></author><author><name sortKey="Lamb, R A" sort="Lamb, R A" uniqKey="Lamb R" first="R A" last="Lamb">R A Lamb</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">9135140</idno><idno type="pmc">1169722</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169722</idno><idno type="RBID">PMC:1169722</idno><idno type="doi">10.1093/emboj/16.6.1236</idno><date when="1997">1997</date><idno type="wicri:Area/Pmc/Corpus">000303</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000303</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.</title><author><name sortKey="Jin, H" sort="Jin, H" uniqKey="Jin H" first="H" last="Jin">H. Jin</name></author><author><name sortKey="Leser, G P" sort="Leser, G P" uniqKey="Leser G" first="G P" last="Leser">G P Leser</name></author><author><name sortKey="Zhang, J" sort="Zhang, J" uniqKey="Zhang J" first="J" last="Zhang">J. Zhang</name></author><author><name sortKey="Lamb, R A" sort="Lamb, R A" uniqKey="Lamb R" first="R A" last="Lamb">R A Lamb</name></author></analytic><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><date when="1997">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The cytoplasmic tails of the influenza virus glycoproteins hemagglutinin (HA) and neuraminidase (NA) are highly conserved in sequence for all virus subtypes and it is believed that assembly of this enveloped virus depends on interactions of these domains with cytoplasmic viral components. However, it is possible to rescue altered influenza viruses lacking either the HA or NA cytoplasmic tails. We have obtained an influenza virus that lacks both the cytoplasmic tail of HA and NA. Particle production is reduced approximately 10-fold but these particles, although having a fairly normal protein composition, are greatly elongated and of extended irregular shape. We propose a model in which the interactions of the cytoplasmic tails of HA and NA with an internal viral component are so important for spherical virion shape that there is dual redundancy in the interactions.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">EMBO J</journal-id><journal-title>The EMBO Journal</journal-title><issn pub-type="ppub">0261-4189</issn><issn pub-type="epub">1460-2075</issn></journal-meta><article-meta><article-id pub-id-type="pmid">9135140</article-id><article-id pub-id-type="pmc">1169722</article-id><article-id pub-id-type="doi">10.1093/emboj/16.6.1236</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Jin</surname><given-names>H</given-names></name></contrib><contrib contrib-type="author"><name><surname>Leser</surname><given-names>G P</given-names></name></contrib><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>J</given-names></name></contrib><contrib contrib-type="author"><name><surname>Lamb</surname><given-names>R A</given-names></name></contrib></contrib-group><aff>Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA.</aff><pub-date pub-type="ppub"><day>17</day><month>3</month><year>1997</year></pub-date><volume>16</volume><issue>6</issue><fpage>1236</fpage><lpage>1247</lpage><abstract><p>The cytoplasmic tails of the influenza virus glycoproteins hemagglutinin (HA) and neuraminidase (NA) are highly conserved in sequence for all virus subtypes and it is believed that assembly of this enveloped virus depends on interactions of these domains with cytoplasmic viral components. However, it is possible to rescue altered influenza viruses lacking either the HA or NA cytoplasmic tails. We have obtained an influenza virus that lacks both the cytoplasmic tail of HA and NA. Particle production is reduced approximately 10-fold but these particles, although having a fairly normal protein composition, are greatly elongated and of extended irregular shape. We propose a model in which the interactions of the cytoplasmic tails of HA and NA with an internal viral component are so important for spherical virion shape that there is dual redundancy in the interactions.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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