Introduction: Primary drug resistance mutations that alone confers moderate resistance such as V82A and L90M are initially selected followed by the addition of secondary mutations often located outside of the active site of the PR, such as L10I, M36I, M46I, L63P, or A71V leading to higher levels of resistance.
Genotypic resistance profile and clinical progression of treatment-experienced HIV type 1-infected patients with virological failure.
PMID: 18240962
2008
AIDS research and human retroviruses
Abstract: In multivariable models adjusting for prior AIDS, baseline CD4 counts, HIV-1 RNA, and calendar year, viral resistance variables associated with increased hazards of clinical progression were the presence of reverse transcriptase substitution T215F (p = 0.002) and the presence of three or more protease substitutions among L33F/I/V, V82A/F/L/T, I84V, and L90M (p = 0.003).
The HIV-1 protease substitution K55R: a protease-inhibitor-associated substitution involved in restoring viral replication.
PMID: 18252693
2008
The Journal of antimicrobial chemotherapy
Abstract: RESULTS: The K55R mutation, which is not a natural polymorphism, was identified to be strongly associated with protease mutations M46I/L and to a lesser extent L24I, I54V and V82A/T/S/F.
HIV type 1 pol gene diversity and antiretroviral drug resistance mutations in Santos, Brazil.
PMID: 18327988
2008
AIDS research and human retroviruses
Abstract: Drug resistance mutations identified in common to subtypes B, F, and recombinants B/F were protease inhibitors M46I/L (29%), I54V (24%), A71V (22%), and V82A/F (31%); reverse transcriptase nucleoside resistance mutations M41L (52%), D67N (30%), K70R (26%), M184V (88%), L210W (29%), T215Y/I/F (65%), and K219Q/E/N (28%); and reverse transcriptase nonnucleoside resistance mutation K103N (52%).
Clinically validated mutation scores for HIV-1 resistance to fosamprenavir/ritonavir.
PMID: 18390885
2008
The Journal of antimicrobial chemotherapy
Abstract: Two fosamprenavir/ritonavir mutation scores were constructed: score A (L10F/I/V + L33F + M36I + I54L/M/V/A/T/S + I62V + V82A/F/C/G + I84V + L90M) was based only on mutations associated with a worse VR, whereas score B (L10FIV + L33F + M36I + I54L/M/V/A/T/S + A71V - V77I - N88S + L90M) also took into account favourable mutations.
Impact on replicative fitness of the G48E substitution in the protease of HIV-1: an in vitro and in silico evaluation.
PMID: 18545158
2008
Journal of acquired immune deficiency syndromes (1999)
Abstract: In addition, the G48E and G48E/V82A site-directed mutants were associated with a decrease in fitness, whereas a reversion to the wild type at position 48 was observed in vitro.
Profile of primary resistance in HIV-1-infected treatment-naive individuals from Western India.
PMID: 18593351
2008
AIDS research and human retroviruses
Abstract: The resistance mutation observed in the protease gene was V82A, whereas in the RT gene, M41L, D67N, M184V, and A98G were documented.
Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.
Result: The 80's loop shows intrinsic flexibility as described previously for atomic resolution structures of saquinavir complexes with wild type PR and mutants V82A and I84V and a 9X mutant with indinavir.
HIV drug resistance pattern among HAART-exposed patients with suboptimal virological response in Ouagadougou, Burkina Faso.
PMID: 18667925
2008
Journal of acquired immune deficiency syndromes (1999)
Abstract: Dominant mutations included M46I (37%), 154V (26%), V82A/T/F (30%) in PR; K103N (44%), G190A/S (16%) and T215F/Y (48%) (NRTIs) in RT.
Abstract: Some resistance mutations, notably D67N/G, K70R and L210W (thymidine analogue mutations-TAMs); K101E, V179E in RT, 154V, V82A/T/F and L90M in PR were significantly higher among CRF06_cpx than CRF02_AG strains (P
Active-site mutations in the South african human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study.
Abstract: Study of active-site mutations (the V82A single mutation and the V82F I84V double mutation) in the less-studied South African HIV type 1 subtype C (C-SA) protease indicated that neither mutation had a significant impact on the proteolytic functioning of the protease.
HIV mutation literature information.
PMID: 
2008
Retrovirology
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