literature

HIV mutation literature information.

Drug Susceptibility and Viral Fitness of HIV-1 with Integrase Strand Transfer Inhibitor Resistance Substitution Q148R or N155H in Combination with Nucleoside/Nucleotide Reverse Transcriptase Inhibitor Resistance Substitutions.

PMID: 26574015 2016 Antimicrobial agents and chemotherapy

Abstract: As a follow-up, the in vitro characteristics of mutant HIV-1 containing RT-K65R and/or RT-M184V with IN-Q148R or IN-N155H were also evaluated, alone and in combination, for potential interactions.

Abstract: In clinical trials of coformulated elvitegravir (EVG), cobicistat (COBI), emtricitabine (FTC), and tenofovir disoproxil fumarate (TDF), emergent drug resistance predominantly involved the FTC resistance substitution M184V/I in reverse transcriptase (RT), with or without the tenofovir (TFV) resistance substitution K65R, accompanied by a primary EVG resista

Transmitted drug resistance of HIV-1 strains among individuals attending voluntary counselling and testing in Taiwan.

PMID: 26404079 2016 The Journal of antimicrobial chemotherapy

Abstract: Among the seven major integrase mutations (T66I, E92Q, G140S, Y143C/H/R, S147G, Q148H/K/R and N155H), only one strain harbouring the Q148R mutation was detected.

[Resistance profile and genetic barrier of dolutegravir].

PMID: 25858608 2015 Enfermedades infecciosas y microbiologia clinica

Abstract: Dolutegravir displays in vitro activity against mutant HIV-1 harboring any isolated resistance mutations selected during failures to raltegravir or elvitegravir (Y143C/H/, N155H, Q148H/K/R, E92G/Q, T66A/I/K, T97A, E138A/K, G140A/S).

Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study.

PMID: 25927004 2015 Acta naturae

Introduction: However, investigation of the DTG effect on HIV-1 isolates from patients insensitive to RAL and EVG showed that Q148H/K/R substitutions in the integrase structure lead to some resistance to DTG.

Introduction: Mutations Q148H/R/K lead to RAL- and EVG-resistance in different HIV-1 subtypes.

Natural polymorphism S119R of HIV-1 integrase enhances primary INSTI resistance.

PMID: 25956162 2015 Antiviral research

Abstract: The frequency of the S119X polymorphism together with Q148H/R (n=8, 63%) or N155H (n=12, 83%) was relatively high compared with that of naive group.

HIV-1 Group O Resistance Against Integrase Inhibitors.

PMID: 26017662 2015 Journal of acquired immune deficiency syndromes (1999)

Abstract: CONCLUSIONS: HIV-O harboring Q148R and N155H shows higher resistance to DTG compared with HIV-M subtype B.

Abstract: Site-directed mutagenesis was performed on the pCOM2.5 HIV group 0 infectious clone to ascertain the impact of INSTI resistance substitutions at positions Q148R, N155H, and R263K within integrase on susceptibility to INSTIs and infectiousness.

Abstract: The pCMO2.5/Q148R and pCMO2.5/N155H variants displayed far higher levels of resistance to DTG (>1000 FC) than was seen for group M viruses.

Characterization of the Drug Resistance Profiles of Integrase Strand Transfer Inhibitors in Simian Immunodeficiency Virus SIVmac239.

PMID: 26378179 2015 Journal of virology

Abstract: RAL and EVG showed reduced activity against both viruses and against enzymes containing Q148R, E92Q Y143R, and G140S Q148R.

Abstract: The results show that the G118R and G140S Q148R substitutions decreased Km' and Vmax'/Km' for strand transfer compared to those of the WT.

Abstract: To study this at a biochemical level, purified recombinant SIVmac239 wild-type (WT) and E92Q, T97A, G118R, Y143R, Q148R, N155H, R263K,

In vitro activity of dolutegravir against wild-type and integrase inhibitor-resistant HIV-2.

PMID: 25808007 2015 Retrovirology

Abstract: Integrase substitutions E92Q, Y143C, E92Q + Y143C, and Q148R conferred relatively low levels of resistance to dolutegravir in HIV-2ROD9 (2- to 6-fold), but Q148K, E92Q + N155H, T97A + N155H and

Abstract: In contrast, HIV-1NL4-3 mutants E92Q + N155H, G140S + Q148R, and T97A + Y143C showed 2-fold, 4-fold, and no increase in EC50, respectively, relative to the parental strain.

Lack of integrase inhibitors associated resistance mutations among HIV-1C isolates.

PMID: 26626277 2015 Journal of translational medicine

Abstract: Neither major resistance-associated IN mutations (T66I/A/K, E92Q/G, T97A, Y143HCR, S147G, Q148H/R/K, and N155H) nor silent mutations known to change the genetic barrier were observed.

Conclusion: None of the previously reported major mutations (T66AIK, E92Q, Y143RCH, S147G, Q148HRK and N155H) associated with resistance to INIs were observed in HIV-1C Ethiopian isolates, indicating that

Resistance against Integrase Strand Transfer Inhibitors and Relevance to HIV Persistence.

PMID: 26198244 2015 Viruses

Introduction: Under such circumstances, extensive genotypic characterisation of resistant strains from two large clinical studies, i.e., Studies 102 and 103, revealed the emergence of the T66I, E92Q, T97A, Q148R and N155H resistance mutations in integrase, mostly in combination with the M184I/V substitutions in RT.

Table: Q148R

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