Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
Identifieur interne : 001061 ( Ncbi/Merge ); précédent : 001060; suivant : 001062Posttranslational 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.
Url:
PubMed: 3279048
PubMed Central: 2115101
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<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>
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<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>
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<issn pub-type="ppub">0021-9525</issn>
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<title-group><article-title>Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers</article-title>
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<pub-date pub-type="ppub"><day>1</day>
<month>3</month>
<year>1988</year>
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<volume>106</volume>
<issue>3</issue>
<fpage>629</fpage>
<lpage>639</lpage>
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<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>
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