Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity.

ABSTRACT: Other than cleavage site mutations, there is little data on specific positions within Gag that impact on HIV protease inhibitor susceptibility. We have recently shown that non-cleavage site mutations in gag, particularly within matrix protein can restore replication capacity and further reduce protease inhibitor drug susceptibility when coexpressed with a drug-resistant (mutant) protease. The matrix protein of this patient-derived virus was studied in order to identify specific changes responsible for this phenotype. Three amino acid changes in matrix (R76K, Y79F, and T81A) had an impact on replication capacity as well as drug susceptibility. Introduction of these three changes into wild-type (WT) matrix resulted in an increase in the replication capacity of the protease mutant virus to a

SUBMITTER: Parry CM 

PROVIDER: S-EPMC3067102 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature