Result: E.g., a pathway that the virus uses often to escape from thymidine analogs is by the mutation T215Y (or T215F), followed by M41L, which in turn is followed by L210W.
Result: Figure 3 presents screenshots of outputs from the web page, illustrating the predicted susceptibilities for two patterns of mutations: K65R+M184V (Panel A) and M41L+L210W+T215Y (Panel B).
Result: For example, mutations L210W and T215Y/F are the most deleterious for the thymidine analogues AZT and d4T, although they also reduce the susceptibility to the other NRTIs.
Emergence of multiclass drug-resistance in HIV-2 in antiretroviral-treated individuals in Senegal: implications for HIV-2 treatment in resouce-limited West Africa.
Abstract: HIV-1-associated thymidine analogue mutations (M41L, D67N, K70R, L210W, and T215Y/F) were not observed, with the exception of K70R, which was present together with K65R and Q151M in a strain from 1 patient.
Result: HIV-1-associated thymidine analogue mutations (M41L, D67N, K70R, L210W, T215Y/F, and K219Q/E) were not found, with the exception of K70R, which was present in a strain from 1 patient (in conjunction with K65R
The public health approach to identify antiretroviral therapy failure: high-level nucleoside reverse transcriptase inhibitor resistance among Malawians failing first-line antiretroviral therapy.
Method: NRTI mutations included K65R and K70E (associated with TDF resistance), thymidine analog mutations (TAMs) M41L, D67N, K70R, L210W, T215Y, T215F, K219Q, and K219E, and multinucleoside mutations, including the 69 insertion complex and the 151 complex.
Result: The most frequent TAMs were T215 F/Y (73%), D67N (53%), K70R (36%), M41L (36%), K219 Q/E (23%), and L210W (23%).
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: The excision mechanism is associated with mutations at the polymerase domain, including M41L, D67N, K70R, L210W, T215F/Y and K219E/Q (excision-containing mutations, EEMs, also known as thymidine analogue-associated mutations [TAMs]).
Discussion: The Type I EEMs (M41L, L210W, T215Y and occasionally the D67N mutation) appear twice as frequently as Type II EEMs (D67N, K70R, T215F and K219Q mutation) in subtype B, whereas Type II EEMs are mostly obse
Antiretroviral drug resistance surveillance among treatment-naive human immunodeficiency virus type 1-infected individuals in Angola: evidence for low level of transmitted drug resistance.
PMID: 19433560
2009
Antimicrobial agents and chemotherapy
Abstract: Two (1.6%) unrelated patients harbored nucleoside reverse transcriptase inhibitor- and nonnucleoside reverse transcriptase inhibitor-resistant viruses (mutations: M41L, D67N, M184V, L210W, T215Y or T215F, and K103N).
Virological efficacy and emergence of drug resistance in adults on antiretroviral treatment in rural Tanzania.
Minority variants associated with transmitted and acquired HIV-1 nonnucleoside reverse transcriptase inhibitor resistance: implications for the use of second-generation nonnucleoside reverse transcriptase inhibitors.
PMID: 19734799
2009
Journal of acquired immune deficiency syndromes (1999)
Result: Five samples had one or more NRTI or NNRTI-resistance mutation including 30062 which had four NRTI-resistance mutations: M184V+L210W+T215Y+219Q and 8048 had one NRTI-resistance mutation
Discussion: For example, PID 8048 had the NRTI-resistance mutation K65R and the accessory NNRTI-resistance mutation P225H and PID 30062 contained the NRTI-resistance mutations M184V, L210W, T215Y, and K219Q.
Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance.
PMID: 19812032
2009
The Journal of biological chemistry
Introduction: Mutations M41L, D67N, K70R, L210W, T215F/Y, and K219Q/E/N, which are primary resistance mutations for AZT and stavudine, are called thymidine analog mutations (TAMs), AZTr, or excision-enhancing mutations.
HIV mutation literature information.
PMID: 
2010
Nature structural & molecular biology
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