literature

HIV mutation literature information.

Low frequency of genotypic resistance in HIV-1-infected patients failing an atazanavir-containing regimen: a clinical cohort study.

PMID: 23711895 2013 The Journal of antimicrobial chemotherapy

Result: The remaining 43 minor atazanavir mutations were either not detected in this dataset (L10C, K20V, E34Q, F53Y, I54L/M/T/A, A71L, G73C/T, V82F and

Discussion: Although there was a high frequency (7/39) of PI substitutions (including L33I/F and L90M, which we did not observe) in this subgroup, many patients were on NRTI-sparing dual-PI regimens and it is not possible to assess whether the substitutions observed were selected by atazanavir or by the other PI in the regimen.

Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.

PMID: 24079831 2013 Biochemistry

Result: Natural mutations L33F and L63P in PR20 occur at positions that are mutated (L33I, L63I) from the wild type to limit autoproteolysis of PR, and the presence of L63P provided a reasonable hypothesis to account for diminished autoproteolytic activity, since Pro occurs very rarely at the P1 position of substrates cleaved by PR.

Potent antiviral HIV-1 protease inhibitor GRL-02031 adapts to the structures of drug resistant mutants with its P1'-pyrrolidinone ring.

PMID: 22401672 2012 Journal of medicinal chemistry

Method: The HIV-1 PR (GenBank HIVHXB2CG) gene was cloned into pET11a expression vector (Novagen) and further optimized to restrict autoproteolysis (Q7K, L33I and L63I) and cysteine-thiol oxidation (C67A and C95A).

Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.

PMID: 23144597 2012 Journal of chemical theory and computation

Method: For this experiment, protease that contains mutations at the primary auto-proteolysis site and at cysteine sites (Q7K, L33I, L63I, C67A and C95A) wasused, with the amino acid sequence: PQITL WKRPL VTIRI GGQLK EALLD TGADD TVIEE MNLPG KWKPK MIGGI GGFIK VRQYD QIIIE IAGHK AIGTV LVGPT PVNII GRNLL TQIGA TLNF.

The L76V drug resistance mutation decreases the dimer stability and rate of autoprocessing of HIV-1 protease by reducing internal hydrophobic contacts.

PMID: 21446746 2011 Biochemistry

Method: The HIV-1 PR (Genbank HIVHXB2CG) clone optimized for structural and biochemical studies contains mutations Q7K, L33I and L63I to minimize autoproteolysis, and C67A and C95A to prevent cysteine-thiol oxidation.

Differences in reversion of resistance mutations to wild-type under structured treatment interruption and related increase in replication capacity.

PMID: 21297946 2011 PloS one

Method: The final list of mutations included M41L, E44D, D67N, T69D, K70R, L74V, L100I, K103N, V108I, V118I, Y181C, M184V, G190A, L210W, T215F, T215Y and K219Q in RT; and L33F, L33I, M46I, M46L, G48V, <

The L76V mutation in HIV-1 protease is potentially associated with hypersusceptibility to protease inhibitors Atazanavir and Saquinavir: is there a clinical advantage?

PMID: 21314993 2011 AIDS research and therapy

Table: L33I

Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease.

PMID: 19899162 2010 Proteins

Method: An HIV-1 protease construct containing five mutations that retard autoproteolysis and avoid cysteine-thiol oxidation (Q7K, L33I, L63I, C67A and C95A), termed PR, was used.

HIV drug resistance surveillance using pooled pyrosequencing.

PMID: 20174661 2010 PloS one

Result: The L33I was detected in only two Sanger reads and correspondingly the majority of the pyrosequencing reads containing the same mutation cluster around those two sequences ( Figure 6b ).

Table: L33I

Figure: All positive pyrosequencing reads containing L33V (a) and L33I (b) were analyzed with Sanger sequences from the 96 specimens using Neighbour-Joining (K-2-P) with 100 bootstraps.

Cysteine 95 and other residues influence the regulatory effects of Histidine 69 mutations on Human Immunodeficiency Virus Type 1 protease autoprocessing.

PMID: 20331855 2010 Retrovirology

Introduction: A pseudo wild type protease, which bears six point mutations (Q7K, L33I, N37S, L63I, C67A, and C95A) compared to the NL4-3 protease, has been previously optimized for NMR and kinetic studies of protease maturation.

Introduction: Mutations Q7K, L33I, L63I minimize a

Result: Mutations Q7K, L33I, and L63I are known to minimize autoproteolysis; and C67A/C95A mutations prevent aggregation of E.

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