Effect of internal cleavage site mutations in human immunodeficiency virus type 1 capsid protein on its structure and function.

ABSTRACT: The capsid protein of the human immunodeficiency virus type 1 has been found to be a substrate of the retroviral protease in vitro, and its processing was predicted to be strongly dependent on a pH-induced conformational change. Several protease cleavage sites have been identified within the capsid protein, but the importance of its cleavage by the viral protease at the early phase of infection is controversial. To confirm the relevance of this process, we aimed to design, produce, and characterize mutant capsid proteins, in which the protein susceptibility toward HIV-1 protease is altered without affecting other steps of the viral life cycle. Our results indicate that while the introduced mutations changed the cleavage rate at the mutated sites of the capsid protein by HIV-1 protease, som

SUBMITTER: Toth F 

PROVIDER: S-EPMC4971840 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature