Phenotypic characterization of drug resistance-associated mutations in HIV-1 RT connection and RNase H domains and their correlation with thymidine analogue mutations.
PMID: 21393163
2011
The Journal of antimicrobial chemotherapy
Abstract: RESULTS: Subtype B-infected patient database analysis showed that mutations N348I, A360V/T, T377M and D488E were found to be selected independently of TAMs, whereas mutations R358K, G359S, A371V, A400T, K451R and K512R increased in frequency with the number of TAMs in a dose-dependent fashion.
Failure of initial therapy with two nucleosides and efavirenz is not associated with early emergence of mutations in the C-terminus of HIV-1 reverse transcriptase.
PMID: 21350368
2011
Journal of acquired immune deficiency syndromes (1999)
Introduction: Other connection domain mutations, including G333D/E, G335C/D, A360I/V, A365I and A376S have been shown to decrease ZDV susceptibility in the presence of thymidine analog mutations (TAMs), and mutation T369I increases resistance to NNRTI in the presence of NNRTI-resistance mutations.
Discussion: These studies have identified a number of mutations in the C-terminus of RT that are more frequent in ART-experienced patients compared to ART-naive including E312Q, G333D/E, G335C/D, N348I,
HIV-1 reverse transcriptase connection domain mutations: dynamics of emergence and implications for success of combination antiretroviral therapy.
Abstract: A360V was not associated with specific drug combinations and was found to emerge later than M184V or thymidine analogue mutations.
Abstract: RESULTS: The connection domain mutations N348I, R356K, R358K, A360V, and A371V were more frequently observed in ART-exposed than ART-naive patients, of which only N348I and A360V were nonpolymorphic (with a prevalence of <1.5% in untreated patients).
Connection domain mutations in treatment-experienced patients in the OPTIMA trial.
PMID: 20130473
2010
Journal of acquired immune deficiency syndromes (1999)
Abstract: Frequencies of E312Q, Y318F, G333D, G333E, G335C, G335D, N348I, A360I, A360V, V365I, A371V, A376S, and E399G were compared with a treatment-naive population.
Clinical relevance of substitutions in the connection subdomain and RNase H domain of HIV-1 reverse transcriptase from a cohort of antiretroviral treatment-naive patients.
Introduction: also recently reported that the A360V and A371V mutations are frequently observed in AZT-treated patients.
Result: None of the clinical isolates of our cohort had the G333D, G335C, N348I, A360I/V, and Q509L mutations.
Discussion: Furthermore, the G333D, G335C, N348I, A360I/V and Q509L substitutions were not observed in our cohort, and were also rarely observed among treatment-naive patients (less than 1%) in the Stanford HIV Drug Resistance Database.
Discussion: However, site directed mutagenesis studies showed that PMID: 19067547
2008
Biochemistry
Discussion: have proposed a similar model for the N348I and A360V connection domain mutations.
HIV-1 reverse transcriptase connection subdomain mutations reduce template RNA degradation and enhance AZT excision.
Abstract: We found that cn mutations G335C/D, N348I, A360I/V, V365I, and A376S decreased primary and secondary RNase H cleavages.
Zidovudine (AZT) monotherapy selects for the A360V mutation in the connection domain of HIV-1 reverse transcriptase.
PMID: 18547911
2008
The Journal of biological chemistry
Abstract: Here, we focused on connection mutations N348I and A360V that are frequently observed in clinical samples of treatment-experienced patients.
Abstract: The TAMs/N348I/A360V mutant accumulates transiently formed, shorter hybrids that can rebind to RT before the template is irreversibly degraded.
Abstract: These hybrids dissociate selectively from the RNase H-competent complex, whereas binding in the polymerase-competent mode is either not affected with N348I or modestly improved with A360V.
Abstract: We show that both N348I and A360V, in combination with TAMs, decrease the efficiency of RNase H cleavage and increase
Mutations in the connection domain of HIV-1 reverse transcriptase increase 3'-azido-3'-deoxythymidine resistance.
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.
HIV mutation literature information.
PMID: 
2011
The Journal of antimicrobial chemotherapy
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