National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
HIV-1 protease is responsible for total twelve proteolytic reactions that are required to generate a viable virus. Mutations in gag cleavage and non-cleavage sites have been reported to aid in recovery of diminished replication capacity due to HIV resistance mutations in protease. Duplication of HIV-1 p6 gag proline-rich (PTAP) region, though not exclusively related to drug resistance, may improve the replication of HIV-1. In subtype C, PTAP/PSAP duplications have been reported to be significantly higher than that seen in non-C subtype sequences. We analyzed Indian HIV-1 gag gene amino acid sequences from antiretroviral drug treatment-naïve and treatment-experienced study participant specimens, which included 72 proviral (subtype C = 70; subtype A1= 2) and 56 plasma (subtype C = 55; subtype A1= 1) sequences. Sequences from one treatment-naïve and two PI-exposed study participants exhibited A431V mutation in gag, a mutation associated with PI resistance. The remaining sequences harboring such PI resistance associated mutations in gag were in those who were either treatment-naïve, or had been exposed to NRTIs and NNRTIs only. In the study sequences, the frequency of PTAP/PSAP duplications ranged from 16% in plasma to 20% in proviral DNA, with no statistically significant differences in the prevalence of these duplications between sequences from treatment-naïve and treatment-experienced individuals. There is a need to explore the phenotypic behavior and clinical correlates of mutations and duplications in non-B subtypes in protease cleavage and non-cleavage sites in gag, with relevance to HIV drug resistance.
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