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Multimerizable HIV Gag derivative binds to the liquid-disordered phase in model membranes.
- Source :
-
Cellular microbiology [Cell Microbiol] 2013 Feb; Vol. 15 (2), pp. 237-47. Date of Electronic Publication: 2012 Dec 12. - Publication Year :
- 2013
-
Abstract
- During HIV assembly, a protein coat on the inner leaflet of the plasma membrane drives the formation of virus particles, and appears to induce the preferential accumulation of 'raft' lipids in the viral envelope, although the lipid raft concept mainly proposes microdomains of these lipids in the outer leaflet. The common hypothesis is that Gag preferentially associates with, and thereby probably induces, raft-like domains, because the protein is multimerized and specifically linked to two saturated acyl chains. To test this hypothesis, we constructed a minimal in vitro system in which we analysed the interaction of a Gag derivative, which could be triggered to multimerize, with a domain-forming model membrane resembling the inner leaflet of the plasma membrane. Confirming studies with authentic Gag, this Gag derivative only bound to membranes when it was multimerized, myristoylated and when phosphatidylinositol 4,5-bisphosphate was present in the membrane. Unexpectedly, however, the multimerized Gag derivative was largely excluded from ordered domains in model membranes. This suggests that the mechanism of membrane reorganization during HIV assembly does not simply result from a higher affinity of the clustered Gag membrane binding domain to ordered membrane domains, but involves more complex biophysical interactions or possibly also an additional protein machinery.<br /> (© 2012 Blackwell Publishing Ltd.)
- Subjects :
- Gene Products, gag metabolism
Gene Products, gag ultrastructure
Green Fluorescent Proteins
HEK293 Cells
HIV metabolism
HIV ultrastructure
Humans
Membrane Microdomains metabolism
Models, Biological
Myristic Acid chemistry
Myristic Acid metabolism
Phosphatidylinositol 4,5-Diphosphate chemistry
Phosphatidylinositol 4,5-Diphosphate metabolism
Protein Binding
Protein Multimerization
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins metabolism
Unilamellar Liposomes metabolism
Virion metabolism
Virion ultrastructure
Gene Products, gag chemistry
HIV chemistry
Membrane Microdomains chemistry
Unilamellar Liposomes chemistry
Virion chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1462-5822
- Volume :
- 15
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Cellular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 23121220
- Full Text :
- https://doi.org/10.1111/cmi.12064