The effect of clade-specific sequence polymorphisms on HIV-1 protease activity and inhibitor resistance pathways.

ABSTRACT: The majority of HIV-1 infections around the world result from non-B clade HIV-1 strains. The CRF01_AE (AE) strain is seen principally in Southeast Asia. AE protease differs by approximately 10% in amino acid sequence from clade B protease and carries several naturally occurring polymorphisms that are associated with drug resistance in clade B. AE protease has been observed to develop resistance through a nonactive-site N88S mutation in response to nelfinavir (NFV) therapy, whereas clade B protease develops both the active-site mutation D30N and the nonactive-site mutation N88D. Structural and biochemical studies were carried out with wild-type and NFV-resistant clade B and AE protease variants. The relationship between clade-specific sequence variations and pathways to inhibitor resistance

SUBMITTER: Bandaranayake RM 

PROVIDER: S-EPMC2937823 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature