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.
Discussion: At present, only N348I has been shown to be involved in resistance to multiple RTIs.
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: Our results support the hypothesis that the substitutions observed among treatment-naive patients have little impact on therapeutic outcome by themselves in the absence of AZT-associated mutations, although certain substitutions, such as N348I, A376S, and Q509L, are involved in drug resis
Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance.
Abstract: We found that cn mutations G335C/D, N348I, A360I/V, V365I, and A376S decreased primary and secondary RNase H cleavages.
Compensatory role of double mutation N348I/M184V on nevirapine binding landscape: insight from molecular dynamics simulation.
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
Compensatory role of double mutation N348I/M184V on nevirapine binding landscape: insight from molecular dynamics simulation.
Abstract: N348I impaired HIV-1 replication in a cell-type-dependent manner.
Abstract: Acquisition of N348I was frequently observed in AZT- and/or ddI-containing therapy (12.5%; n = 48; P < 0.0001) and was accompanied with thymidine analogue-associated mutations, e.g., T215Y (n = 5/6) and the lamivudine resistance mutation M184V (n = 1/6) in a Japanese cohort.
Abstract: Molecular modeling analysis shows that residue 348 is proximal to the NNRTI-binding pocket and to a flexible hinge region at the base of the p66 thumb that may be affected by the N348I mutation.
Abstract: This resistance is caused by N348I, a mutation at the connection subdomain of human immunodeficiency virus type 1 (HIV-1) reverse t
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.
Compensatory role of double mutation N348I/M184V on nevirapine binding landscape: insight from molecular dynamics simulation.
Abstract: Biochemical analyses of recombinant RT containing N348I provide supporting evidence for the role of this mutation in zidovudine and NNRTI resistance and give some insight into the molecular mechanism of resistance.
Abstract: CONCLUSIONS: This study provides the first in vivo evidence that treatment with RT inhibitors can select a mutation (i.e., N348I) outside the polymerase domain of the HIV-1 RT that confers dual-class resistance.
Abstract: METHODS AND FINDINGS: The prevalence of N348I in clinical isolates, the time taken for it to emerge under selective drug pressure, and its association with changes in viral load, specific drug treatment, and known drug resistance mutations was analysed
HIV mutation literature information.
PMID: 
2009
Antiviral research
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