Discussion: In some nonsubtype-B HIV-1, D30N is selected less frequently than are other PI mutations.
Restriction fragment mass polymorphism (RFMP) analysis based on MALDI-TOF mass spectrometry for detecting antiretroviral resistance in HIV-1 infected patients.
PMID: 23480551
2013
Clinical microbiology and infection
Abstract: The concordance rates between the RFMP and direct sequencing assays for the examined codons were 97% (K65R), 97% (T69Ins/D), 97% (L74VI), 97% (K103N), 96% (V106AM), 97% (Q151M), 97% (Y181C), 97% (M184VI) and 94% (T215YF) in the reverse transcriptase coding region, and 100% (D30N), 100% (M46I), 100% (G48V), 100% (I50V), 100% (I54LS), 99% (V82A), 99% (I84V) and 100% (L90M) in th
Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.
Abstract: Here, we show that accumulation of mutations in a drug-resistant HIV-1 protease (HIV-1 PR) variant, D30N/M36I/A71V, changes the fractional occupancy of the equilibrium conformational sampling ensemble.
Introduction: D30N occurs specifically in response to nelfinavir treatment, whereas M36I and A71V, along with other non-active site substitutions, appear as a result of selective pressure of treatments using various protease inhibitors.
Introduction: In particular, SDSL-DEER was used to understand the effects of the accumulation of primary, D30N, and secondary mutations M36I and
Antiviral resistance and correlates of virologic failure in the first cohort of HIV-infected children gaining access to structured antiretroviral therapy in Lima, Peru: a cross-sectional analysis.
Method: The OLA was conducted according to the NIH protocol for mutations at HIV-1B protease positions D30N, I50V, V82A, V82S, V82T, I84V, N88D, and L90M as well as reverse transcriptase positions K103N, Y181C, K65R, T215F, T215Y, M184V, and Q151M.
Result: The protease mutation D30N was detected in 43% of RNA genotyping samples and in
Novel P2 tris-tetrahydrofuran group in antiviral compound 1 (GRL-0519) fills the S2 binding pocket of selected mutants of HIV-1 protease.
PMID: 23298236
2013
Journal of medicinal chemistry
Discussion: D30N mutation is the major mutation associated with resistance to NFV, which has been suggested to arise from the change of conformational entropy upon inhibitor binding.
Discussion: Considering the positive association of mutation D30N and N88D, it would be interesting to study how N88D influences the structure of D30N in complex with this new inhibitor 1.
Discussion: Our structural analysis also showed that mutation D30N introduced changes in its interactions with neighboring residues Thr74 and Asn88.
Discussion: Similarly, our study suggests that viral strains containing D30N or I50V are likely to show resistance to inhibitor 1 given their Ki values of 8.9 and 30.9 nM for
"Description of the L76V resistance protease mutation in HIV-1 B and ""non-B"" subtypes."
Method: In our study, samples with at least one of the major PI RAM of the IAS-USA list as follows: D30N, V32I, M46I/L, I47A/V, G48V, I50L/V, I54L/M, Q58E, T74P, L76V, V82A/F/L/T/S, N83D, I84V, N88S, L90M were considered as PI-resistant issued from PI-experienced patients.
Extreme multidrug resistant HIV-1 protease with 20 mutations is resistant to novel protease inhibitors with P1'-pyrrolidinone or P2-tris-tetrahydrofuran.
PMID: 23590295
2013
Journal of medicinal chemistry
Introduction: Recently, we characterized a clinically derived HIV-1 protease (PR20) bearing 20 mutations [Q7K, L10F, I13V, I15V, D30N, V32I, L33F, E35D, M36I, S37N, I47V, I54L, Q58E, I62V, L63P, A71V, I84V, N88D, L89T and L90M] and extremely resist
Trends in Genotypic HIV-1 Antiretroviral Resistance between 2006 and 2012 in South African Patients Receiving First- and Second-Line Antiretroviral Treatment Regimens.
Method: The following non-polymorphic ARV-selected mutations were classified as drug resistance mutations (DRM): (i) the NRTI resistance mutations M41L, A62V, K65RN, D67NG, T69D, T69 insertions, T69 deletion, K70REGQ, L74VI, V75MT, F77L, Y115F, F116Y, Q151M, M184VI, L210W, T215YFSDCIV, and K219QENR; (ii) the
Significantly improved HIV inhibitor efficacy prediction employing proteochemometric models generated from antivirogram data.
Result: For the PIs mutations that are accurately reproduced include D30N, I50L, V82S, and I84, while the I64L and I93M mutations are assigned less importance than in previous work.
Increasing trends in primary NNRTI resistance among newly HIV-1-diagnosed individuals in Buenos Aires, Argentina.
PMID: 24093951
2013
Journal of the International AIDS Society
Method: Sequences were analyzed to identify mutations associated with reduced susceptibility to protease and RT inhibitors, as reported by the International AIDS Society-USA in 2010: RT-M41L, A62V, K65R, D67N, 69 insert, K70R, L74V,V75I, F77L, L100I, K101P, K103N, V106A, V106M, V108I, Y115F, F116Y,
HIV mutation literature information.
PMID: 
2014
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