literature

HIV mutation literature information.

Protease polymorphisms in HIV-1 subtype CRF01_AE represent selection by antiretroviral therapy and host immune pressure.

PMID: 20009919 2010 AIDS (London, England)

Abstract: Compared to the subtype B consensus, six additional polymorphisms (I13 V, E35D, M36I, R41K, H69K, L89M) were identified in the CRF01_AE consensus; all but L89M were located within epitopes recognized by HLA class I alleles.

Result: There were six differences between the consensus sequence inferred from our dataset and the subtype B consensus sequence (I13V, E35D, M36I, R41K, H69K and L89M).

Discussion: I13 V and E35D often appear during nelfinavir treatment.|mgd

Mutations associated with virological response to darunavir/ritonavir in HIV-1-infected protease inhibitor-experienced patients.

PMID: 19147519 2009 The Journal of antimicrobial chemotherapy

Abstract: Cochran-Armitage procedure identified eight mutations with a negative impact on the virological response, namely K14R, K20I, E34Q, I47V, I54M, K55R, T74P and I84V; and two mutations (E35D and V82A) with a positive impact.

Rapid and persistent selection of the K103N mutation as a majority quasispecies in a HIV1-patient exposed to efavirenz for three weeks: a case report and review of the literature.

PMID: 21092074 2009 Journal of medical case reports

Table: E35D

Genetic diversity and drug resistance of HIV type 1 circulating recombinant Form_BC among drug users in Guangdong Province.

PMID: 19698024 2009 AIDS research and human retroviruses

Abstract: Five high polymorphisms were found in CRF_07BC isolates; there were E35D (88%), R41K (100%), D60E (96%), L63P (99%), and I93L (91%).

Structural basis of drug resistance by genetic variants of HIV type 1 clade c protease from India.

PMID: 19400736 2009 AIDS research and human retroviruses

Abstract: The E35D mutation affects the flap structure in clade B strains and E35N and E35K mutation, seen in our modeled strains, have a more profound effect.

Antiretroviral drug susceptibility among drug-naive adults with recent HIV infection in Rakai, Uganda.

PMID: 19276794 2009 AIDS (London, England)

Table: E35D

Tipranavir-ritonavir genotypic resistance score in protease inhibitor-experienced patients.

PMID: 18625773 2008 Antimicrobial agents and chemotherapy

Abstract: Mutations at six residues were associated with a lower VR (E35D/G/K/N, M36I/L/V, Q58E, Q61D/E/G/H/N/R, H69I/K/N/Q/R/Y, and L89I/M/R/T/V), and one mutation was associated with a higher VR (F53L/W/Y).

Impact on replicative fitness of the G48E substitution in the protease of HIV-1: an in vitro and in silico evaluation.

PMID: 18545158 2008 Journal of acquired immune deficiency syndromes (1999)

Abstract: These simulations documented that the G48E mutant interacted with PI resistance mutations (M46I, I54V, Q58E, and L63P) and with natural polymorphisms specific to subtype A1 (E35D, M36I, and R57K) that were present in the patient's virus.

Virological response to darunavir/ritonavir-based regimens in antiretroviral-experienced patients (PREDIZISTA study).

PMID: 18505178 2008 Antiviral therapy

Abstract: We determined the genotypic score I13V+V32I+L33F/I/V+E35D+ M361/L/V+I47V+F53L+I62V.

Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D G S mutant in the South African HIV-1 subtype C protease.

PMID: 16794810 2007 Journal of molecular modeling

Abstract: In this paper, we report the first computational study of the clinically relevant E35D mutation of HIV-1 protease in its unbound conformation and complexed with the clinical inhibitor amprenavir and a sample substrate (Thr-Ile-Met-Met-Gln-Arg).

Abstract: One possible explanation for the emergence of this mutation, despite its unfavorable effect on substrate affinity, might be the role of E35D as an escape mutation, which favors escape from the immune system in addition to conferring drug resistance.

Abstract: Our data, collected from 10 ns molecular-dynamics simulations, show that the E35D mutation results in an increased flexibility of the flaps, thereby affecting the conformational equilibrium between the closed and semi-open conformations of the free protease.

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