Genotypic prediction of resistant mutation in HIV-1 pol gene towards the antiretroviral drugs.
PMID: 21441094
2011
International journal of bioinformatics research and applications
Abstract: Two sequences of protease show the major mutation with mutations sites of I54V and V82A and 8 sequences shown other mutations.
Transmission of HIV drug resistance and non-B subtype distribution in the Spanish cohort of antiretroviral treatment naive HIV-infected individuals (CoRIS).
Abstract: The most prevalent resistance mutations were: T215 revertants (3.8%), D67NG (1.3%), K219QENR (1.2%) and M41L (1%), for NRTIs; K103N (3.2%), for NNRTIs; I54VLMSAT, M46I and L90M (0.7%), for PIs.
Lopinavir/ritonavir resistance in patients infected with HIV-1: two divergent resistance pathways?
Abstract: L90M, I54V and Q58E were associated with L76V in a multivariate analysis (P < 0.0001, P = 0.002, and P = 0.008, respectively).
Abstract: In contrast, I54V, G73S and L90M were less prevalent in viruses L76V positive than L76V negative (I54V, 42% vs. 83%, P = 0.01; G73S, 0% vs. 33%, P = 0.02; L90M, 25% vs. 83%, P = 0.0006).
Abstract: One contains the L76V and Q58E mutations and the other contains the L90M and I54V mutations.
The new and less toxic protease inhibitor saquinavir-NO maintains anti-HIV-1 properties in vitro indistinguishable from those of the parental compound saquinavir.
Abstract: Our analysis identified mutations V82A, I54V, K20I and I62V, which were associated with reduced viral response and mutations I15V and V91S which determined lopinavir/r hypersensitivity.
Result: Both the LASSO and the LAR/LASSO models only include a maximum of 3 main effects: pre-TCE viral load and mutation V82A (LAR) and pre-TCE viral load and mutations I54V and V82A (LASSO) as well as their interactions with viral load.
Result: When we used the best subset selector, LSE estimates of the coefficients and 10-fold CV to identify our model potentially leading to a novel LPV/r score, besides pre-TCE viral load, 5 mutations were selected: I15V
Correlation between resistance profile and immunosuppression in heavily treated HIV-1 infected Romanian patients.
PMID: 22180722
2011
Romanian biotechnological letters
Abstract: A significantly higher total number of mutations were encountered in severely immunosuppressed patients, who presented also major mutations in the protease gene (V82A, I54V, G48V) and the major M184V mutation associated with type 2 thymidine analogs mutations in reverstranscriptase gene.CONCLUSION: A good immune status seems to be associated with a low range of mutations, indicating the impact of immune restoration or preservation on the therapeutic success rate.
Result: Five out of the 21 patients with severe immunosuppression harbored major PI mutations V82A, I54V, and G48V associated with phenotypic resistance to ritonavir.
Does GSS still maintain relevance on HAART outcome after the introduction of newest active antiretroviral drugs? 48 weeks results.
Abstract: About 60% of tests reported L10FIRVC, M36ILV, M46IL, I54VLAMTS, V82AFTSLI, and L90M mutations in the protease region.
A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
Abstract: For the unliganded double mutant protease molecular dynamics simulations revealed a contraction of the ligand binding pocket, which is enhanced by the I54V mutation.
Abstract: In the present work we investigated the structural properties of a triple mutant (I54V-V82A-L90M) and a double mutant (V82A-L90M) that both confer strong resistance to ritonavir (RTV), but not to amprenavir (APV).
Decomposing the energetic impact of drug resistant mutations in HIV-1 protease on binding DRV.
PMID: 20543885
2010
Journal of chemical theory and computation
Abstract: Two drug-resistant protease variants FLAP+ (L10I, G48V, I54V, V82A) and ACT (V82T, I84V) decrease the binding affinity with DRV by 1.0 kcal/mol and 1.6 kcal/mol respectively.
Introduction: In this study, the binding of DRV was investigated with wild-type HIV-1 protease and two drug-resistant variants: FLAP+ (Figure 1B) with L10I, G48V, I54V, V82A which are a combination of flap and active site mutations, and ACT (Figure 1C) with V82T, I84V which are active site mutations.
HIV mutation literature information.
PMID: 
2011
International journal of bioinformatics research and applications
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