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- Title
HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.
- Authors
Ko, Li-Jung; Yu, Fu-Hsien; Huang, Kuo-Jung; Wang, Chin-Tien
- Abstract
Human immunodeficiency virus type 1 nucleocapsid (NC) basic residues presumably contribute to virus assembly via RNA, which serves as a scaffold for Gag–Gag interaction during particle assembly. To determine whether NC basic residues play a role in Gag cleavage (thereby impacting virus assembly), Gag processing efficiency and virus particle production were analyzed for an HIV-1 mutant NC15A, with alanine serving as a substitute for all NC basic residues. Results indicate that NC15A significantly impaired virus maturation in addition to significantly affecting Gag membrane binding and assembly. Interestingly, removal of the matrix (MA) central globular domain ameliorated the NC15A assembly and processing defects, likely through enhancement of Gag multimerization and membrane binding capacities.
- Subjects
HIV infections; NUCLEOCAPSIDS; SCAFFOLD proteins; GAG proteins; PROTEIN-protein interactions; VIRUS-like particles
- Publication
FEBS Open Bio, 2015, Vol 5, p283
- ISSN
2211-5463
- Publication type
Article
- DOI
10.1016/j.fob.2015.04.003