literature

HIV mutation literature information.

Detection of Gag C-terminal mutations among HIV-1 non-B subtypes in a subset of Cameroonian patients.

PMID: 35082353 2022 Scientific reports

Discussion: More precisely, Gag mutation P453L positively correlated with seven major protease resistance mutations (

Discussion: Several studies have shown a positive correlation of Gag P453L mutation with some protease major resistance mutations such as I50V and I84V.

Discussion: The strong correlation of this mutation with PI resistance mutations has been confirmed by the dendrogram; where P453L Gag mutation clustered with two major protease resistance mutations (M46I and I84V).

Gag-Protease Sequence Evolution Following Protease Inhibitor Monotherapy Treatment Failure in HIV-1 Viruses Circulating in East Africa.

PMID: 26258548 2015 AIDS research and human retroviruses

Introduction: At the C terminus, 17/23 patients had amino acid changes versus consensus M including mutations L449P, S451N, and P453L that previously were associated with PI exposure and/or resistance.

Introduction: Mutation P453L was present in 4/11 subtype A patients, but again is not a consensus residue in subtypes A, C, or D.

Introduction: Of particular interest, two CSMs developed in two separate patients at the time of failure:

HIV-1 Gag C-terminal amino acid substitutions emerging under selective pressure of protease inhibitors in patient populations infected with different HIV-1 subtypes.

PMID: 25253273 2014 Retrovirology

Result: Patients failing an ATV/r-based regimen developed Gag substitution patterns: P453L or V374A + R387K + S451G + P453Ins.

Table: P453L/T

Table: P453L

Gag drug resistance mutations in HIV-1 subtype C patients, failing a protease inhibitor inclusive treatment regimen, with detectable lopinavir levels.

PMID: 25397528 2014 Journal of the International AIDS Society

Abstract: These mutations are K436R (n=4), I437V (n=1), L449P (n=5), R452K (n=4) and P453LT (n=9).

Within-host co-evolution of Gag P453L and protease D30N/N88D demonstrates virological advantage in a highly protease inhibitor-exposed HIV-1 case.

PMID: 21338625 2011 Antiviral research

Abstract: Furthermore, database analysis indicated that the P453L(Gag)/D30N(PR)/N88D(PR) association was not specific only to our clinical case, but was common among AIDS patients.

Abstract: Homology modeling analysis suggested that hydrogen bonds between the 30th

Abstract: The results showed that P453L(Gag) has the potential to improve replication capacity and the Gag processing efficiency of viruses with D30N(PR)/N88D(PR) but has little effect on nelfinavir susceptibility.

Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss.

PMID: 19300491 2009 PLoS pathogens

Introduction: Substitution P453L is a polymorphism found in some inhibitor-naive viruses.

A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism.

PMID: 17227139 2007 PLoS medicine

Discussion: Changes at the p1/p6 cleavage site (L449F or P453L), which on their own do not confer resistance, were associated with reduced sensitivity in the background of the I50V in protease.

Compensatory mutations at the HIV cleavage sites p7/p1 and p1/p6-gag in therapy-naive and therapy-experienced patients.

PMID: 17302250 2006 Antiviral therapy

Abstract:

Abstract: Mutagenetic trees constructed form this cross-sectional data showed an ordered accumulation of the most prominent CS mutations along two pathways L90M-I84V-P453L and I54-V82-A431V followed by either M46L or L24I.

Abstract: RESULTS: Multiple mutations within the CS p7/p1 and p1/p6-gag accumulated in therapy-experienced isolates (p7/p1: A431V-K436R-I437V and p1/p6-gag: L449F/V-P452S-P453L/A).

Changes in human immunodeficiency virus type 1 Gag at positions L449 and P453 are linked to I50V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro.

PMID: 12097552 2002 Journal of virology

Abstract: In both single- and multiple-cycle assay systems and in the context of I50V, the L449F and P453L changes consistently increased the 50% inhibitory concentration of APV, while the CS changes alone had no measurable effect on inhibitor sensitivity.

Abstract: In population-based sequence analyses the I50V mutant was invariably linked to either L449F or P453L.

Abstract: Purified I50V protease catalyzed cleavage of decapeptides incorporating the L449F or P453L change 10-fold and 22-fold more efficiently than cleavage of the wild-type substrate, respectively.

Polymorphism of HIV type 1 gag p7/p1 and p1/p6 cleavage sites: clinical significance and implications for resistance to protease inhibitors.

PMID: 10957718 2000 AIDS research and human retroviruses

Abstract: Natural polymorphism P453L might direct the PR resistance pathway through I84V instead of V82 mutation.

Abstract: Natural polymorphism P453L was strongly associated with the selection of PR I84V (OR 49.5; 95% CI 12-212) and selected against V82 mutation (OR 0.15; 95% CI 0.02-1.

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