scholarly journals A uniquely prevalent nonnucleoside reverse transcriptase inhibitor resistance mutation in Russian subtype A HIV-1 viruses

AIDS ◽  
2014 ◽  
Vol 28 (17) ◽  
pp. F1-F8 ◽  
Author(s):  
Anna N. Kolomeets ◽  
Vici Varghese ◽  
Philippe Lemey ◽  
Marina R. Bobkova ◽  
Robert W. Shafer
Keyword(s):  
Reverse Transcriptase ◽  
Resistance Mutation ◽  
Transcriptase Inhibitor ◽  
Nonnucleoside Reverse Transcriptase Inhibitor ◽  
Inhibitor Resistance ◽  
Subtype A ◽  
Reverse Transcriptase Inhibitor ◽  
Hiv 1

scholarly journals High nonnucleoside reverse transcriptase inhibitor resistance levels in HIV-1-infected Zambian mother–infant pairs

AIDS ◽  
2020 ◽  
Vol 34 (12) ◽  
pp. 1833-1842
Author(s):  
Sydney J. Bennett ◽  
Catherine Chunda-Liyoka ◽  
Lisa K. Poppe ◽  
Katie Meinders ◽  
Chisanga Chileshe ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Transcriptase Inhibitor ◽  
Nonnucleoside Reverse Transcriptase Inhibitor ◽  
Inhibitor Resistance ◽  
Reverse Transcriptase Inhibitor ◽  
Hiv 1

scholarly journals L74V increases the reverse transcriptase content of HIV-1 virions with non-nucleoside reverse transcriptase drug-resistant mutations L100I+K103N and K101E+G190S, which results in increased fitness

2013 ◽  
Vol 94 (7) ◽  
pp. 1597-1607 ◽  
Author(s):  
Jiong Wang ◽  
Dongge Li ◽  
Robert A. Bambara ◽  
Hongmei Yang ◽  
Carrie Dykes
Keyword(s):  
Reverse Transcriptase ◽  
Resistance Mutation ◽  
Transcriptase Inhibitor ◽  
Rnase H ◽  
Drug Resistant ◽  
Resistance Mutations ◽  
Nnrti Resistance ◽  
Reverse Transcriptase Inhibitor ◽  
Subsequent Addition ◽  
Hiv 1

The fitness of non-nucleoside reverse transcriptase inhibitor (NNRTI) drug-resistant reverse transcriptase (RT) mutants of HIV-1 correlates with the amount of RT in the virions and the RNase H activity of the RT. We wanted to understand the mechanism by which secondary NNRTI-resistance mutations, L100I and K101E, and the nucleoside resistance mutation, L74V, alter the fitness of K103N and G190S viruses. We measured the amount of RT in virions and the polymerization and RNase H activities of mutant RTs compared to wild-type, K103N and G190S. We found that L100I, K101E and L74V did not change the polymerization or RNase H activities of K103N or G190S RTs. However, L100I and K101E reduced the amount of RT in the virions and subsequent addition of L74V restored RT levels back to those of G190S or K103N alone. We conclude that fitness changes caused by L100I, K101E and L74V derive from their effects on RT content.

Inhibition of HIV-1 replication by a nonnucleoside reverse transcriptase inhibitor

Science ◽  
1990 ◽  
Vol 250 (4986) ◽  
pp. 1411-1413 ◽  
Author(s):  
V. Merluzzi ◽  
K. Hargrave ◽  
M Labadia ◽  
K Grozinger ◽  
M Skoog ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Transcriptase Inhibitor ◽  
Nonnucleoside Reverse Transcriptase Inhibitor ◽  
Reverse Transcriptase Inhibitor ◽  
Hiv 1
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