An assembly domain of the Rous sarcoma virus Gag protein required late in budding
- PMID: 8083996
- PMCID: PMC237081
- DOI: 10.1128/JVI.68.10.6605-6618.1994
An assembly domain of the Rous sarcoma virus Gag protein required late in budding
Abstract
The Gag protein of Rous sarcoma virus has the ability to direct particle assembly at the plasma membrane in the absence of all the other virus-encoded components. An extensive deletion analysis has revealed that very large regions of this protein can be deleted without impairing budding and has suggested that the essential functions map to three discrete regions. In the studies reported here, we establish the location of assembly domain 2 (AD2) within the proline-rich p2b sequence of this Gag protein. AD2 mutants lacking the p2b sequence were completely defective for particle release even though their Gag proteins were tightly associated with the membrane fraction and exhibited high levels of protease activity. Mutations that inactivate the viral protease did not restore budding to wild-type levels for these mutants, indicating that the defect is not due simply to a loss of protease regulation. AD2 mutants could be rescued into dense particles in genetic complementation assays, indicating that their defect is not due to a gross alteration of the overall conformation of the protein and that the assembly function is not needed on every Gag molecule in the population. Several mutants with amino acid substitutions in the p2b sequence were found to have an intermediate capacity for budding. Inactivation of the protease of these mutants stabilized the Gag polyprotein within the cells and allowed an increase in particle release; however, the rate of budding remained slow. We favor the idea that AD2 is a dynamic region of movement, perhaps serving as a molecular hinge to allow the particle to emerge from the surface of the cell during budding.
Similar articles
-
Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins.J Virol. 1995 Sep;69(9):5455-60. doi: 10.1128/JVI.69.9.5455-5460.1995. J Virol. 1995. PMID: 7636991 Free PMC article.
-
Altered Rous sarcoma virus Gag polyprotein processing and its effects on particle formation.J Virol. 1997 Mar;71(3):2083-91. doi: 10.1128/JVI.71.3.2083-2091.1997. J Virol. 1997. PMID: 9032340 Free PMC article.
-
Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release.J Virol. 1993 Sep;67(9):5550-61. doi: 10.1128/JVI.67.9.5550-5561.1993. J Virol. 1993. PMID: 8394460 Free PMC article.
-
Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly.J Virol. 1991 Jan;65(1):272-80. doi: 10.1128/JVI.65.1.272-280.1991. J Virol. 1991. PMID: 1845888 Free PMC article.
-
Analysis of deletions and thermosensitive mutations in Rous sarcoma virus gag protein p10.J Virol. 1993 Jul;67(7):3826-34. doi: 10.1128/JVI.67.7.3826-3834.1993. J Virol. 1993. PMID: 7685400 Free PMC article.
Cited by
-
The Rous sarcoma virus Gag Polyprotein Forms Biomolecular Condensates Driven by Intrinsically-disordered Regions.J Mol Biol. 2023 Aug 15;435(16):168182. doi: 10.1016/j.jmb.2023.168182. Epub 2023 Jun 14. J Mol Biol. 2023. PMID: 37328094 Free PMC article.
-
The multifaceted interactions between pathogens and host ESCRT machinery.PLoS Pathog. 2023 May 4;19(5):e1011344. doi: 10.1371/journal.ppat.1011344. eCollection 2023 May. PLoS Pathog. 2023. PMID: 37141275 Free PMC article. Review.
-
Comparative Analysis of the Simian Varicella Virus and Varicella Zoster Virus Genomes.Viruses. 2022 Apr 19;14(5):844. doi: 10.3390/v14050844. Viruses. 2022. PMID: 35632586 Free PMC article. Review.
-
Characterization of Bovine Foamy Virus Gag Late Assembly Domain Motifs and Their Role in Recruiting ESCRT for Budding.Viruses. 2022 Mar 3;14(3):522. doi: 10.3390/v14030522. Viruses. 2022. PMID: 35336929 Free PMC article.
-
Advances in HIV-1 Assembly.Viruses. 2022 Feb 26;14(3):478. doi: 10.3390/v14030478. Viruses. 2022. PMID: 35336885 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources