HIV mutation literature information.


  Distinct resistance mutation and polymorphism acquisition in HIV-1 protease of subtypes B and F1 from children and adult patients under virological failure.
 PMID: 18992847       2009       Infection, genetics and evolution
Method: Mutations D30N (NFV), V32I (LPV), M46I/L (IDV/RTV), I47V/A (LPV/RTV), G48V (SQV), I50L/V (APV), V82A/F/T/S (LPV/IDV/RTV), I84V (APV/IDV/RTV) and L90M (SQV/NFV) were considered as major resistance mutations and were analyzed separately for each PI as well as quantitatively all together.
Result: Of note, M46I was more frequent than M46L in subtype B isolates, while M46L was more frequent than M46I in subtype F1 isolates (Table 3).
Table: M46L


  Discordant genotypic interpretation and phenotypic role of protease mutations in HIV-1 subtypes B and G.
 PMID: 19136678       2009       The Journal of antimicrobial chemotherapy
Abstract: Indinavir-associated mutations M46I/L, I84V and V82A/F/T developed earlier in subtype B across the time of exposure to that drug when compared with subtype G counterparts.


  The prevalence of resistance-associated mutations to protease and reverse transcriptase inhibitors in treatment-naive (HIV1)-infected individuals in Casablanca, Morocco.
 PMID: 19759509       2009       Journal of infection in developing countries
Abstract: Only two major mutations, M46L and V82L, were separately found in three individuals of 71 (4.2%) with one carrying both mutations.


  Antiretroviral genotypic resistance mutations in HIV-1 infected Korean patients with virologic failure.
 PMID: 19949656       2009       Journal of Korean medical science
Abstract: M184V/I mutation was observed in 36 patients (87.7%) followed by T215Y/F (41.5%) and M46I/L (34%).
Result: M184V/I mutation was observed in 36 patients (87.7%) followed by T215Y/F (17/41, 41.5%) and M46I/L (14/41, 34.2%).


  Molecular characterization of human immunodeficiency virus type 1 (HIV-1) and HIV-2 in Yaounde, Cameroon: evidence of major drug resistance mutations in newly diagnosed patients infected with subtypes other than subtype B.
 PMID: 17855574       2008       Journal of clinical microbiology
Abstract: M46L (n = 2), a major resistance mutation associated with resistance to protease inhibitors, was observed in 2/75 (2.6%) group M samples.


  Resampling-based analyses of the effects of combinations of HIV genetic mutations on drug susceptibility.
 PMID: 18186529       2008       Statistics in medicine
Abstract: Analysis of the data from the Stanford HIV database shows that while M46I/L mutations are associated with drug resistance, addition of the L88D/S mutation leads to hypersusceptible virus.


  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%).


  Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.
 PMID: 18597780       2008       Journal of molecular biology
Introduction: Previously, we have analyzed the structures, activities, inhibition and stability of PR variants with the single substitutions of flap residues M46L, G48V, I50V, and F53L.


  Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir.
 PMID: 18808097       2008       Journal of medicinal chemistry
Introduction: An unusual second binding site for DRV was observed in the two high-resolution crystal structures of complexes with HIV-1 PR mutants with the single substitutions of V32I (0.84 A) and M46L (1.22 A).



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