Discussion: We show here that D30N, N88D/S and L90 M also have high transmissibility and that other SDRMs have higher (M41L, T215Rev and K219E/N/Q/R for NRTIs and K101E/P for the NNRTIs) or lower transmissibility (K70E/R, L74I/V, and T215Y/F for NRTIs; Y181C/I/V for NNRTIs and I84 V and I54A/L/M/S/T/V for protease inhibit
HIV-1 protease inhibitor drug resistance in Kenyan antiretroviral treatment-naive and -experienced injection drug users and non-drug users.
Result: Although major PI resistance mutations was not detected in the non-drug users, three major PI resistance mutations including L90M, M46I and D30N were detected in 4 (5.1 %) IDUs.
Result: In addition, D30N+M46I co-existed with G48E and K20I minor mutations, respectively, in 2 (4.2 %) ART-experienced IDUs.
Result: Interestingly, mutation L90M co-existed with K20R minor mutation in 1 (2.1 %) ART-experienced IDU, while D30N co-existed with T74S+K20R minor mutations in 1 (3.1 %) ART-naive IDU.
Tab
Epidemiological Surveillance of HIV-1 Transmitted Drug Resistance in Spain in 2004-2012: Relevance of Transmission Clusters in the Propagation of Resistance Mutations.
Result: It is noteworthy that several major mutations associated to high level resistance to NRTIs (K65R, L74V, Y115F, M184V and T215Y), to NNRTIs (l100I, K101E, K103N/S, V106M, Y181C, Y188L and G190A) and to PIs (D30N, M46I/L, I54V/T, L76V, V82A, I84V, N88D
Drug-resistant HIV-1 protease regains functional dynamics through cleavage site coevolution.
Abstract: Yet with substrate coevolution, while the wild-type dynamic behavior is restored in both p1-p6 ((LP) (1'F)p1-p6D30N/N88D) and NC-p1 ((AP) (2) (V)NC-p1V82A) bound proteases, the dynamic behavior of the NC-p1 bound protease variants (NC-p1V82A and (AP) (2) (V)NC-p1V82A) rather resemble those of the proteases bound to the other substrates, which is consistent with experimental studies.
Introduction: In the presence of D30N/
Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism.
PMID: 25562662
2015
Journal of molecular graphics & modelling
Introduction: It was found that, the mutations D30N and I50V results in the drug resistance to TMC114; however the changes due to mutations V82A, I84V and L90M are well adapted by TMC114.
Introduction: They found that, loss of H-bonds between Asp30 and TMC114 drives the drug resistance in D30N, while for I50V it is the increased polar solvation energies between TMC114 and two residues Asp30' and Val50'.
Introduction: performed MD simulation studies combined with MM-PBSA to investigate the binding energies of TMC114 to D30N and I50V mutants.
Introduction: utilized the crystallographic study to ana
Molecular basis for reduced cleavage activity and drug resistance in D30N HIV-1 protease.
PMID: 25487655
2015
Chemical biology & drug design
Abstract: Although anti-HIV-1 protease drugs nelfinavir (NFV) and saquinavir (SQV) share common functional groups, D30N is a major resistance mutation against NFV but remains susceptible to SQV.
Abstract: Structural analysis showed that SQV forms two direct hydrogen bonds with the main chain atoms of the residues Asp29 and Asp30 that are not observed in the D30N-NFV complex.
Abstract: These could be the reasons why D30N is not a drug resistance mutation against SQV.
Abstract: We have determined the crystal structure of D30N mutant-tethered HIV-1 protease in complex with SQV to 1.79 A resolution.
2014 Update of the drug resistance mutations in HIV-1.
Result: Recently, we showed by DEER studies that addition of M36I/D30N to A71V restores a predominant semi-open conformation with additional flap curling and open-like states; conformations seen in crystal structures of PR20.
Result: This observation is similar to what we recently observed for MDR769 and V6 as well as for accumulating D30N/M36I/A71V mutations, where cross drug resistance is associated with increases in open-like conformations.
New insights into the in silico prediction of HIV protease resistance to nelfinavir.
Abstract: The D30V mutation triggered a subtle change in the PR structure, which was also observed for the well-known Nelfinavir resistance mutation D30N, while the V32E exchange presented a much more dramatic impact over the PR flap dynamics.
Natural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.
Result: We modelled the proteins with unusual mutations (L5F, D29V, L63G, L63R, P79L and T91V), natural polymorphisms (L63H andL63S), and drug-resistant mutant PRs with single mutations or patterns of mutations (D30N, V32I, M36I, M46I, I47V, G48V, I50V, I50L, I54M, Q58E, T74P, L76V, V82A
HIV mutation literature information.
PMID: 
2015
AIDS (London, England)
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