Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
Identifieur interne : 000999 ( Pmc/Curation ); précédent : 000998; suivant : 000A00Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
Auteurs :Source :
- The Journal of Cell Biology [ 0021-9525 ] ; 1988.
Abstract
The influenza virus hemagglutinin (HA) is a well-characterized integral membrane glycoprotein composed of three identical subunits. We have analyzed the formation of mixed trimers in cells expressing two different HA gene products. The results show efficient and essentially random assembly of functional hybrid trimers provided that the HAs are from the same HA subtype. Trimerization is thus a posttranslational event, and subunits are recruited randomly from a common pool of monomers in the endoplasmic reticulum. Mixed trimers were not observed between HAs derived from different subtypes, indicating that the trimerization event is sequence specific. Mixed trimers containing mutant subunits were, moreover, used to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event.
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PubMed: 3279048
PubMed Central: 2115101
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers</title></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">3279048</idno><idno type="pmc">2115101</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115101</idno><idno type="RBID">PMC:2115101</idno><date when="1988">1988</date><idno type="wicri:Area/Pmc/Corpus">000999</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000999</idno><idno type="wicri:Area/Pmc/Curation">000999</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000999</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers</title></analytic><series><title level="j">The Journal of Cell Biology</title><idno type="ISSN">0021-9525</idno><idno type="eISSN">1540-8140</idno><imprint><date when="1988">1988</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The influenza virus hemagglutinin (HA) is a well-characterized integral membrane glycoprotein composed of three identical subunits. We have analyzed the formation of mixed trimers in cells expressing two different HA gene products. The results show efficient and essentially random assembly of functional hybrid trimers provided that the HAs are from the same HA subtype. Trimerization is thus a posttranslational event, and subunits are recruited randomly from a common pool of monomers in the endoplasmic reticulum. Mixed trimers were not observed between HAs derived from different subtypes, indicating that the trimerization event is sequence specific. Mixed trimers containing mutant subunits were, moreover, used to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event.</p></div></front></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Cell Biol</journal-id><journal-id journal-id-type="iso-abbrev">J. Cell Biol</journal-id><journal-title-group><journal-title>The Journal of Cell Biology</journal-title></journal-title-group><issn pub-type="ppub">0021-9525</issn><issn pub-type="epub">1540-8140</issn><publisher><publisher-name>The Rockefeller University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">3279048</article-id><article-id pub-id-type="pmc">2115101</article-id><article-id pub-id-type="publisher-id">88153893</article-id><article-categories><subj-group subj-group-type="heading"><subject>Articles</subject></subj-group></article-categories><title-group><article-title>Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers</article-title></title-group><pub-date pub-type="ppub"><day>1</day><month>3</month><year>1988</year></pub-date><volume>106</volume><issue>3</issue><fpage>629</fpage><lpage>639</lpage><permissions><license license-type="openaccess"><license-p>This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see <ext-link ext-link-type="uri" xlink:href="http://www.rupress.org/terms">http://www.rupress.org/terms</ext-link>). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc-sa/4.0/">http://creativecommons.org/licenses/by-nc-sa/4.0/</ext-link>).</license-p></license></permissions><abstract><p>The influenza virus hemagglutinin (HA) is a well-characterized integral membrane glycoprotein composed of three identical subunits. We have analyzed the formation of mixed trimers in cells expressing two different HA gene products. The results show efficient and essentially random assembly of functional hybrid trimers provided that the HAs are from the same HA subtype. Trimerization is thus a posttranslational event, and subunits are recruited randomly from a common pool of monomers in the endoplasmic reticulum. Mixed trimers were not observed between HAs derived from different subtypes, indicating that the trimerization event is sequence specific. Mixed trimers containing mutant subunits were, moreover, used to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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