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: In addition, A371V and Q509L in the RNase H domain emerge under the selective pressure of AZT in cell culture.
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.
Selection of mutations in the connection and RNase H domains of human immunodeficiency virus type 1 reverse transcriptase that increase resistance to 3'-azido-3'-dideoxythymidine.
Abstract: A371V and Q509L also increased cross-resistance with TAMs to lamivudine and abacavir, but not stavudine or didanosine.
Abstract: The first resistance mutations to appear in HIV-1(LAI) were two polymerase domain thymidine analog mutations (TAMs), D67N and K70R, and two novel mutations, A371V in the connection domain and Q509L in the RNase H domain, that together conferred up to 90-fold AZT resistance.
Abstract: The roles of A371V and Q509L in AZT resistance were confirmed by site-directed mutagenesis: A371V and Q509L together increased AZT resistance approximately 10- to 50-fold in combinat
N348I in the connection domain of HIV-1 reverse transcriptase confers zidovudine and nevirapine resistance.
Introduction: Finally, a recent study reported that A371V in the connection domain and Q509L in the RNase H domain of HIV-1 RT were selected in combination with TAMs when virus was passaged under increasing concentrations of AZT.
HIV mutation literature information.
PMID: 
2008
The Journal of biological chemistry
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