HIV mutation literature information.


  Evolution of raltegravir resistance during therapy.
 PMID: 19447792       2009       The Journal of antimicrobial chemotherapy
Abstract: The secondary mutations L74M, T97A, V151I and G163R were observed with a frequency of <4%.


  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: In three other patients, viruses with N155H emerged at viral rebound either alone (2 months), followed by V151I (8 months) or alone (10 months), or together with V151I/G163RG (7 months).
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were detected in the virus from one patient, and these reverted to wild type when treatment was withdrawn, although clonal analysis identified maintenance of RAL resistance minority species at this time point.
Abstract: RAL treatment was restarted after 6 months, and 2 weeks later,  PMID: 18702518       2008       Biochemistry
Introduction: Additional mutations have been reported (L74M, E92Q, E138K, G140S/A and G163R).


  Natural variation of HIV-1 group M integrase: implications for a new class of antiretroviral inhibitors.
 PMID: 18687142       2008       Retrovirology
Abstract: Several accessory INI-resistance mutations including L74M, T97A, V151I, G163R, and S230N were also polymorphic with polymorphism rates ranging between 0.5% to 2.0%.
Result: Among mutations selected by raltegravir or elvitegravir that have not been shown to directly reduce susceptibility, L74R, Q95K, E138A/K, and H183P were conserved, whereas V54I, L68V, L74M, T97A, V151I, G163R, and I203M


  Natural polymorphism of the HIV-1 integrase gene and mutations associated with integrase inhibitor resistance.
 PMID: 17668566       2007       Antiviral therapy
Abstract: Of the 42 aa substitutions currently associated with INI resistance, 21 occurred as natural polymorphisms: V72I, L74I, T97A, T112I, A128T, E138K, Q148H, V151I, S153Y/A, M154I, N155H, K156N, E157Q, G163R, V165I, V201I, I203M, T206S, S230N and R263K.


  Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1.
 PMID: 10888639       2000       Journal of virology
Abstract: To address these issues, we studied the effects of CCR5 concentrations on HIV-1 infections using wild-type CCR5 and two attenuated mutant CCR5s, one with the mutation Y14N at a critical tyrosine sulfation site in the amino terminus and one with the mutation G163R in extracellular loop 2.



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