HIV-1 protease mutation 82M contributes to phenotypic resistance to protease inhibitors in subtype G.

Authors: Camacho RJ, Covens K, Palma AC, Snoeck J, Van Laethem K, Vandamme AM
Journal: Journal of Antimicrobial Chemotherapy
Link: http://www.ncbi.nlm.nih.gov/pubmed/?term=HIV-1+protease+mutation+82M+contributes+to+phenotypic+resistance+to+protease+inhibitors+in+subtype+G

OBJECTIVES:
The purpose of this study was the qualitative and quantitative assessment of the in vitro effect of HIV-1 protease (PR) mutation 82M on replication capacity and susceptibility to the eight clinically available PR inhibitors (PIs).
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The rare HIV-1 gp41 mutations 43T and 50V elevate enfuvirtide resistance levels of common enfuvirtide resistance mutations that did not impact susceptibility to sifuvirtide

Mutations that are selected at low frequency and/or reside outside the enfuvirtide target region, amino acid 36-45 of gp41, might still be important determinants for drug resistance.
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Characterization of amino acids Arg, Ser and Thr at position 70 within HIV-1 reverse transcriptase

Authors: Bernatchez J, Camacho RJ, Covens K, De Wit S, Dekeersmaeker N, Götte M, Megens S, Theys K, Van Laethem K, Vandamme AM, Vinken L
Publication Year: 2014
Journal: Acta Clinica Belgica
Link: http://www.ncbi.nlm.nih.gov/pubmed/25103592

The amino acid position 70 in HIV-1 reverse transcriptase (RT) plays an important role in nucleoside RT inhibitor (NRTI) resistance. K70R is part of the thymidine analog mutations, but also other amino acid changes have been associated with NRTI resistance, such as K70E and K70G. In this study, we investigated the in vivo selection of the HIV-1 RT mutations K70S and K70T and their in vitro effect on drug resistance and replication capacity.
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HIV-1 protease mutation 82M contributes to phenotypic resistance to protease inhibitors in subtype G.

The rare HIV-1 gp41 mutations 43T and 50V elevate enfuvirtide resistance levels of common enfuvirtide resistance mutations that did not impact susceptibility to sifuvirtide

Characterization of amino acids Arg, Ser and Thr at position 70 within HIV-1 reverse transcriptase

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