Journal article
Human Immunodeficiency Virus Type 1 Gag Polyprotein Multimerization Requires the Nucleocapsid Domain and RNA and Is Promoted by the Capsid-Dimer Interface and the Basic Region of Matrix Protein
Journal of virology, Vol.73(10), pp.8527-8540
10/1999
DOI: 10.1128/JVI.73.10.8527-8540.1999
PMCID: PMC112873
PMID: 10482606
Abstract
The human immunodeficiency virus type 1 (HIV-1) Gag polyprotein directs the formation of virions from productively infected cells. Many
gag
mutations disrupt virion assembly, but little is known about the biochemical effects of many of these mutations. Protein-protein interactions among Gag monomers are believed to be necessary for virion assembly, and data suggest that RNA may modify protein-protein interactions or even serve as a bridge linking Gag polyprotein monomers. To evaluate the primary sequence requirements for HIV-1 Gag homomeric interactions, a panel of HIV-1 Gag deletion mutants was expressed in bacteria and evaluated for the ability to associate with full-length Gag in vitro. The nucleocapsid protein, the major RNA-binding domain of Gag, exhibited activity comparable to that of the complete polyprotein. In the absence of the nucleocapsid protein, relatively weak activity was observed that was dependent upon both the capsid-dimer interface and basic residues within the matrix domain. The relevance of the in vitro findings was confirmed with an assay in which nonmyristylated mutant Gags were assessed for the ability to be incorporated into virions produced by wild-type Gag expressed in
trans
. Evidence of the importance of RNA for Gag-Gag interaction was provided by the demonstration that RNase impairs the Gag-Gag interaction and that HIV-1 Gag interacts efficiently with Gags encoded by distantly related retroviruses and with structurally unrelated RNA-binding proteins. These results are consistent with models in which Gag multimerization involves indirect contacts via an RNA bridge as well as direct protein-protein interactions.
Details
- Title: Subtitle
- Human Immunodeficiency Virus Type 1 Gag Polyprotein Multimerization Requires the Nucleocapsid Domain and RNA and Is Promoted by the Capsid-Dimer Interface and the Basic Region of Matrix Protein
- Creators
- Mark T Burniston - Departments of MicrobiologyAndrea Cimarelli - Departments of MicrobiologyJohn Colgan - Departments of MicrobiologySean P Curtis - Departments of MicrobiologyJeremy Luban - Departments of Microbiology
- Resource Type
- Journal article
- Publication Details
- Journal of virology, Vol.73(10), pp.8527-8540
- Publisher
- American Society for Microbiology
- DOI
- 10.1128/JVI.73.10.8527-8540.1999
- PMID
- 10482606
- PMCID
- PMC112873
- ISSN
- 0022-538X
- eISSN
- 1098-5514
- Language
- English
- Date published
- 10/1999
- Academic Unit
- Anatomy and Cell Biology; Immunology; Internal Medicine
- Record Identifier
- 9984025564702771
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