Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3'-azido-3'-deoxythymidine through both RNase H-dependent and -independent mechanisms.
PMID: 18547911
2008
The Journal of biological chemistry
Introduction: Most importantly, many of these mutations, including mutations N348I, A360I/V, and A371V, in the connection domain of HIV-1 RT were identified in clinical samples of HIV-infected individuals.
Result: Other mutations (A360I and A360S) were observed only rarely.
HIV-1 reverse transcriptase connection subdomain mutations reduce template RNA degradation and enhance AZT excision.
Abstract: Mutational analysis showed that amino acid substitutions E312Q, G335C/D, N348I, A360I/V, V365I, and A376S were associated strongly with the observed increase in AZT resistance; several of these mutations also decreased RT template switching, suggesting that they alter the predicted balance between nucleotide excision and template RNA degradation.
N348I in the connection domain of HIV-1 reverse transcriptase confers zidovudine and nevirapine resistance.
Introduction: Mutational studies revealed the presence of several connection domain mutations, including E312Q, G335C/D, N348I, A360I/V, V365I, and A376S, that were associated with AZT resistance.