ViMRT
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 HIV mutation literature information.


  Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir.
 PMID: 22350569       2012       Journal of computer-aided molecular design
Abstract: Drug resistance arises from an increase in the energetic contribution from the van der Waals interactions between APV and PR (V32I, I50V, and I84V mutant) or a rise in the energetic contribution from the electrostatic interactions between the inhibitor and its target (I54M and I54V mutant).
Abstract: However, the affinities of the drug resistant protease variants V32I, I50V, I54V, I54M, I84V and L90M to amprenavir are decreased 3 to 30-fold compared to the wild-type.


  Low prevalence of transmitted drug resistance in patients newly diagnosed with HIV-1 infection in Sweden 2003-2010.
 PMID: 22448246       2012       PloS one
Method: The following resistance mutations were scored: to nucleoside reverse transcriptase inhibitors (NRTIs): M41L, K65R, D67N/G/E, T69D/insertion, K70R/E, L74V/I, V75M/T/A/S, F77L, Y115F, F116Y, Q151M, M184V/I, L210W, T215Y/F/I/S/C/D/V/E, K219Q/EN/R; to non-nucleoside revers


  Transmitted drug resistance and phylogenetic relationships among acute and early HIV-1-infected individuals in New York City.
 PMID: 22592583       2012       Journal of acquired immune deficiency syndromes (1999)
4Method: ARV resistance was defined by mutations at the following positions: M41L, A62V, K65R, D67N, T69ins, K70R, L74VI, Y115F, F116Y, Q151M, M184VI, T210W, T215YF and K219QE for Nucleoside Reverse Transcriptase Inhibitors (NRTI), L100I, K101EP, K103NS, V106AM


  Impact of lopinavir/ritonavir use on antiretroviral resistance in recent clinical practice.
 PMID: 22733652       2012       The Journal of antimicrobial chemotherapy
Abstract: Mutations in the protease gene significantly selected between baseline and failure were L10V, K20R, L33F, M36I, I47V, I54V, A71V and I85V (P < 0.05).


  Loss of the protease dimerization inhibition activity of tipranavir (TPV) and its association with the acquisition of resistance to TPV by HIV-1.
 PMID: 23015723       2012       Journal of virology
Abstract: HIV(11MIX)(P10) contained various amino acid substitutions, including I54V and V82T.
Abstract: However, the introduction of I54V/V82T into cHIV(B) (cHIV(B)(I54V/V82T)) compromised TPV's dimerization inhibition and cHIV(B)(I54V/V82T) proved to be significantly TPV resistant.
Abstract: The introduction of I54V/V82T into wild-type cHIV(NL4-3) (cHIV(NL4-3(I54V/V82T))) did not block TPV's dimerization inhibition or confer TPV resistance.


  Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.
 PMID: 23144597       2012       Journal of chemical theory and computation
Abstract: Flap+ is a multi-drug-resistant variant of HIV-1 protease with a combination of mutations at the edge of the active site, within the active site, and in the flaps (L10I, G48V, I54V, V82A).
Introduction: Flap+ is a multi-drug-resistant HIV-1 protease variant with a combination of flap and active site mutations (L10I, G48V, I54V, and V82A) that occur simultaneously in sequences of patients undergoing drug therapy (Figure 1).
Method: As described above, Flap+ contains additional mutations of L10I, G48V, I54V, and


  HIV-1 integrase resistance among antiretroviral treatment naive and experienced patients from Northwestern Poland.
 PMID: 23259737       2012       BMC infectious diseases
Result: It must be noted, that three of the patients with developed drug resistance were heavily experienced with reverse transcriptase (RT) and protease (PR) mutations (patient 1: RT: M41L, K103N, M184V, T215S; PR: L10I; patient 2: PR: M41L, V118I, K103N, M184V, L210W, T215S, RT: L10I,


  High HIV type 1 group M pol diversity and low rate of antiretroviral resistance mutations among the uniformed services in Kinshasa, Democratic Republic of the Congo.
 PMID: 20954909       2011       AIDS research and human retroviruses
Abstract: Only one strain harbored a single mutation, I54V, associated with drug resistance to protease inhibitors.


  Differences in reversion of resistance mutations to wild-type under structured treatment interruption and related increase in replication capacity.
 PMID: 21297946       2011       PloS one
Introduction: Mixtures of wild-type and variants T215Y in RT, L10F, I54V and V82A in PR appeared 6 months after the first mixture at position 184 was detected.


  The L76V mutation in HIV-1 protease is potentially associated with hypersusceptibility to protease inhibitors Atazanavir and Saquinavir: is there a clinical advantage?
 PMID: 21314993       2011       AIDS research and therapy
Table: I54V



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