HIV mutation literature information.


  Impact of residues in the nonnucleoside reverse transcriptase inhibitor binding pocket on HIV-1 reverse transcriptase heterodimer stability.
 PMID: 18336260       2008       Current HIV research
Abstract: We found that the mutations K101A, P225H, Y318F and Y318W decreased RT heterodimer stability whereas K103N, V108I, V108W, Y181C, Y188L, G190A, G190E, G190W and P225W increased RT heterodimer stability.


  Development of Novel Dihydrofuro[3,4-d]pyrimidine Derivatives as HIV-1 NNRTIs to Overcome the Highly Resistant Mutant Strains F227L/V106A and K103N/Y181C.
 PMID: 18338369       2008       ChemMedChem
Abstract: A three-layered ONIOM model was used to study the interactions between efavirenz and the binding sites of HIV-1 reverse transcriptase (RT): wild-type and double mutant K103N/Y181C enzyme forms.
Abstract: The calculated binding energy for the efavirenz-K103N/Y181C HIV-1 RT complex is less than that with the wild-type complex by approximately 8 kcal mol(-1).
Abstract: The interaction energies, calculated at the MP2/6-31G(d,p) level between efavirenz and individual residues surrounding the binding pocket of the K103N/Y181C enzyme, demonstrate that the attractive interactions between efavirenz and residue positions 101 and 103 were less than those for wild-type <


  Prevalence of resistance mutations in HIV-1-Infected Hondurans at the beginning of the National Antiretroviral Therapy Program.
 PMID: 18366313       2008       AIDS research and human retroviruses
Abstract: K103N mutations were present in 3.0% of study specimens.


  Development of Novel Dihydrofuro[3,4-d]pyrimidine Derivatives as HIV-1 NNRTIs to Overcome the Highly Resistant Mutant Strains F227L/V106A and K103N/Y181C.
 PMID: 18370589       2008       AIDS research and human retroviruses
Abstract: A cutoff of 0.5% K103N for detection of K103N was used for both assays.
Abstract: Forty-six samples (73.0%) were positive for K103N by both assays and 13 samples (20.6%) were negative by both assays.
Abstract: Results for the percentage K103N were similar for the two assays (R(2) = 0.92).


  Low rate of emergence of nevirapine and lamivudine resistance after post-partum interruption of a triple-drug regimen.
 PMID: 18389908       2008       Antiviral therapy
Abstract: Analysis of K103N by SPCR showed that 35% of the patients contained < or =0.1% of viruses carrying either the AAC or AAT mutations.
Abstract: Sequence-selective real-time PCR (SPCR), which quantifies minority viral populations containing K103N, Y181C and M184V mutations, and standard genotypic sequencing were assayed.


  Prevalence of HIV-1 drug resistance after failure of a first highly active antiretroviral therapy regimen in KwaZulu Natal, South Africa.
 PMID: 18419495       2008       Clinical infectious diseases
Abstract: The most common mutation was M184V/I (64.3% of patients); K103N was present in virus from 51.3%, and V106M was present in virus from 19.1%.


  Genotypic susceptibility scores and HIV type 1 RNA responses in treatment-experienced subjects with HIV type 1 infection.
 PMID: 18462083       2008       AIDS research and human retroviruses
Abstract: Certain NNRTI-associated mutations, such as K103N, were rapidly selected in the absence of NRTIs.


  Substrate-induced stable enzyme-inhibitor complex formation allows tight binding of novel 2-aminopyrimidin-4(3H)-ones to drug-resistant HIV-1 reverse transcriptase mutants.
 PMID: 18465760       2008       ChemMedChem
Abstract: Interestingly, one compound showed dissociation rates from the ternary complex with RT mutants K103N and Y181I 10-20-fold slower than from the corresponding complex with wild-type RT.
Abstract: These compounds are highly active against both wild-type HIV-1 and the K103N, Y181C, and Y188L mutant strains.


  Profile of drug resistance mutations among HIV-1-infected Tunisian subjects failing antiretroviral therapy.
 PMID: 18483694       2008       Archives of virology
Abstract: In the RT gene, resistance to nucleoside RT inhibitors (NRTIs) and non-nucleoside RT inhibitors (NNRTIs) were recognized in 66.25 and 37.5%, respectively, with M184V, T215Y and K103N being the codons most frequently involved.


  "Selective targeting of the HIV-1 reverse transcriptase catalytic complex through interaction with the ""primer grip"" region by pyrrolobenzoxazepinone non-nucleoside inhibitors correlates with increased activity towards drug-resistant mutants."
 PMID: 18541223       2008       Biochemical pharmacology
Abstract: Our kinetic analysis indicates that the ability of PBOs to selectively target the catalytic ternary complex of RT with its substrates directly correlates with greatly reduced sensitivity to NNRTIs-resistance mutations, particularly the K103N substitution.



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