literature

HIV mutation literature information.

Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.

PMID: 21030679 2010 Proc Natl Acad Sci U S A

Abstract: Furthermore, our structures predict physical proximity and an interaction between HIV-1 IN mutant residues His148 and Ser/Ala140, rationalizing the coevolution of Q148H and G140S/A mutations in drug-resistant viral strains.

Effect of raltegravir resistance mutations in HIV-1 integrase on viral fitness.

PMID: 20634701 2010 Journal of acquired immune deficiency syndromes (1999)

Discussion: A third study found the G140A mutation in place of G140S in viruses that carried G148R substitution.

Discussion: It would be interesting to compare the fitness of the G140A and S mutants in combination with the different codon 148 mutants.

Study of the Conformational Dynamics of the Catalytic Loop of WT and G140A/G149A HIV-1 Integrase Core Domain Using Reversible Digitally Filtered Molecular Dynamics.

PMID: 26610114 2009 Journal of chemical theory and computation

Abstract: In this study, the enhanced sampling technique, Reversible Digitally Filtered Molecular Dynamics (RDFMD), has been applied to the catalytic domain of the WT and G140A/G149A HIV-1 IN enzymes and has highlighted significant differences between the behavior of the catalytic loop which may explain the decrease of activity observed in experimental studies for this mutant.

The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation.

PMID: 19129221 2009 Nucleic acids research

Result: Interestingly, two other mutations of the catalytic loop (G149A and G149A/G140A) display similar post DNA-binding defects.

Characterization and structural analysis of HIV-1 integrase conservation.

PMID: 19290031 2009 AIDS reviews

Abstract: All primary signature mutations emerging in patients failing raltegravir (Y143R, Q148H/K/R, N155H) or elvitegravir (T66I, E92Q, S147G, Q148H/K/R, N155H), as well as secondary mutations (H51Y, T66A/K, E138K, G140S/A/C, Y143C/H, K160N, R166S, E170A, S230R, D232N, R263K) were complete

The dynamics of appearance and disappearance of HIV-1 integrase mutations during and after withdrawal of raltegravir therapy.

PMID: 19571721 2009 AIDS (London, England)

Abstract: Mutations Q148R (2 months) followed by G140A/Q148R and then G140A/Y143CHR/Q148R/G163R were detected in the virus from one patient, and these reverted to wild type when treatment was withdrawn, although clonal analysis identified maintenance of RAL resistance minority species at this time point.

HIV-1 IN alternative molecular recognition of DNA induced by raltegravir resistance mutations.

PMID: 19623602 2009 Journal of molecular recognition

Abstract: Virologic failure during treatment with raltegravir, the first effective drug targeting HIV integrase, is associated with two exclusive pathways involving either Q148H/R/K, G140S/A or N155H mutations.

Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants.

PMID: 18702518 2008 Biochemistry

Introduction: Additional mutations have been reported (L74M, E92Q, E138K, G140S/A and G163R).

Preliminary mapping of a putative inhibitor-binding pocket for human immunodeficiency virus type 1 integrase inhibitors.

PMID: 16377678 2006 Antimicrobial agents and chemotherapy

Abstract: Specifically, the single mutations E92K, Q148A, K156A, K156R, G140S, and G149S, as well as the double mutations C65S-K156N and H67D-G140A were evaluated for their effects on enzymatic activity and inhibitor susceptibility.

The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity.

PMID: 10413462 1999 Biochemistry

Abstract: X-ray structures of the catalytic domain mutants G149A and G140A/G149A show further rigidity of alpha4 and the adjoining loop.

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