Kagan Ron M, Sista Prakash, Pattery Theresa, Bacheler Lee, Schwab Dale A
Department of Infectious Diseases, Quest Diagnostics Nichols Institute, San Juan Capistrano, California 92675, USA.
AIDS. 2009 Jul 31;23(12):1602-5. doi: 10.1097/QAD.0b013e32832d8771.
We investigated the phenotypic impact of a number of uncommon amino acid substitutions at HIV-1 reverse transcriptase positions 103 and 138, which are not part of the etravirine resistance score and were found in combination with the high-impact mutation K101P. Etravirine phenotypic fold changes were 380-1400 for K101P + E138A/G/Q + K103N/S/T + V179I and 12-130 for K101P + (K103S +/- V179I) in the absence of E138A/G/Q. Although the effect of K103S is unclear, additional position 138 substitutions seem important for etravirine susceptibility.
我们研究了HIV-1逆转录酶第103位和138位一些不常见氨基酸替代的表型影响，这些位置不属于依曲韦林耐药评分的一部分，且发现它们与高影响突变K101P同时出现。对于K101P + E138A/G/Q + K103N/S/T + V179I，依曲韦林表型倍数变化为380 - 1400；对于K101P + (K103S +/- V179I)且不存在E138A/G/Q时，表型倍数变化为12 - 130。虽然K103S的影响尚不清楚，但138位的其他替代似乎对依曲韦林敏感性很重要。
