Introduction: We tested the effects of three IN mutations, Y143R, N155H, and the double mutation G140S/Q148H, all of which reduce the susceptibility of HIV-1 to RAL, on viral DNA integration.
Result: Although the data suggest that a suboptimal concentration of RAL appears to increase the propensity of the Y143R mutant to make aberrant integrations, the differences in the fraction of integration sites that were aberrant for the Y143R mutant, comparing the presence and absence of RAL, were not statistically significant.
Result: In the absence of any added RAL, we found aberrant integrations in infections that were done using the Y143R mutant; howeve
Table: Y143R
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.
Integrase Strand Transfer Inhibitors (INSTIs) Resistance Mutations in HIV-1 Infected Turkish Patients.
Abstract: However, ARV-experienced patients had major resistance mutations associated with raltegravir and elvitegravir; the following results were generated:F121Y, Y143R, Q148R and E157Q (6/91 - 6.6%).
Effect on HIV-1 viral replication capacity of DTG-resistance mutations in NRTI/NNRTI resistant viruses.
Introduction: The absence of compensatory secondary mutations for R263K is also consistent with the observation that many major RAL- and EVG-resistance substitutions such as G140S, Q148R, E92Q, N155H and Y143R are incompatible with the simultaneous presence of R263K in terms of both integrase strand-transfer activity and viral replication capacity.
Selectivity for strand-transfer over 3'-processing and susceptibility to clinical resistance of HIV-1 integrase inhibitors are driven by key enzyme-DNA interactions in the active site.
Introduction: In a previous study, we compared EVG to RAL and showed that EVG retains potency against the RAL-specific mutant Y143R.
Introduction: Using recombinant enzymes and oligonucleotides mimicking the ends of the retroviral DNA, IN mutants have been extensively characterized and RAL resistance can be recapitulated with three primary mutants: Y143R, N155H and G140S-Q148H (SH).
Introduction: While DTG effectively inhibits the Y143R and N155H mutants, the SH double mutant still reduces DTG potency by about 5- to 6-fold.
Result: No correlation was found for the Y143R mutant (Supplementary Figure S4).
Result: The lack of correlation for the
Development of a phenotypic susceptibility assay for HIV-1 integrase inhibitors.
PMID: 27737783
2016
Journal of virological methods
Abstract: While raltegravir resistance profiles presented a high cross-resistance to elvitegravir, dolutegravir maintained in-vitro activity in spite of the Y143R and N155H mutations, confirming the strong activity of dolutegravir against raltegravir-resistant viruses.
Prevalence of Integrase Strand Transfer Inhibitors (INSTI) Resistance Mutations in Taiwan.
Abstract: Of these 12 sequences, 11 harboured Q148H/K/R, one Y143R, and none N155H.
Introduction: With one or two major mutations, such as Q148HKR +- G140SA, N155H +- E92Q or Y143CR +- T97A, a marked reduction of viral susceptibility to raltegravir and elvitegravir has been observed.
Method: The major INSTI mutations, which have been determined having a marked reduction of viral susceptibility to raltegravir and elvitegravir, include Y143C/H/R, Q148H/K/R, and N155H.|m
Antiviral Activity of Bictegravir (GS-9883), a Novel Potent HIV-1 Integrase Strand Transfer Inhibitor with an Improved Resistance Profile.
PMID: 27645238
2016
Antimicrobial agents and chemotherapy
Result: The set of tested mutations included E92Q, Y143R, Q148R, N155H, R263K, E138K/Q148K, G140S/Q148R, E92Q/N155H, and Q148R/N155H.
Discussion: The Y143R single mutant in our panel has no effect on susceptibility to BIC or DTG and is mildly resistant to EVG but has a higher resistance to RAL.
Discussion: While Y143R, Q148R, and N155H are primary RAL-associated mutations,
Therapy-Emergent Drug Resistance to Integrase Strand Transfer Inhibitors in HIV-1 Patients: A Subgroup Meta-Analysis of Clinical Trials.
Introduction: Resistance mutations that were found in viral isolates from treatment-naive participants who experienced treatment failure during the initial dose-ranging Protocol 004 clinical trial were: L74L/M, V151I, N155H, Y143R and S230R in integrase (IN) and M184M/I/V and K65K/R in RT (Table 1).
HIV mutation literature information.
PMID: 
2016
Retrovirology
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