Abstract: Mutations used for genotypic surveillance of transmitted antiretroviral drug resistance were identified in six samples: three had nucleoside reverse transcriptase inhibitor (NRTI) surveillance mutations (two had M41L, one had K219R), and three had protease inhibitor surveillance mutations (I47V, F53L, N88D); none had nonnucleoside reverse transcriptase inhibitor (NNRTI) surveillance mutations.
Result: However, none of the 104 samples had a mutation pattern predictive of reduced protease inhibitor susceptibility, and only three samples had a mutation used for genotypic surveillance of transmi
Genotypic resistance profiles in antiretroviral-naive HIV-1 infections before and after initiation of first-line HAART: impact of polymorphism on resistance to therapy.
PMID: 18182278
2008
International journal of antimicrobial agents
Abstract: Moreover, major mutations (D30N and N88D) conferring resistance to PIs were found in patients infected with subtype B strain.
Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants.
Abstract: Crystal structures, molecular dynamics simulations, and calorimetric data for four mutants (D30N, D30N/A71V, D30N/N88D, and D30N/L90M) were used to augment our kinetic data.
Mutational patterns and correlated amino acid substitutions in the HIV-1 protease after virological failure to nelfinavir- and lopinavir/ritonavir-based treatments.
Abstract: D30N and N88D appeared mostly in patients without previous exposure to protease inhibitors, while K20T was identified as a secondary resistance mutation in those patients.
Primary resistance to enfuvirtide (T20) in recently HIV-1 infected, antiretroviral-naive patients from the ANRS Aquitaine Cohort.
Abstract: The first case had an N42D mutation in the HR1 region of the gp41, along with transmitted resistance mutations in the protease (D30N, M361, N88D) and in the RT (M41L, L210W, T215D).
HIV-1 subtype B protease and reverse transcriptase amino acid covariation.
Abstract: Different patterns of covariation were frequently observed for different mutations at the same position including the RT mutations T69D versus T69N, L74V versus L74I, V75I versus V75M, T215F versus T215Y, and K219Q/E versus K219N/R, and the protease mutations M46I versus M46L, I54V versus I54M/L, and N88D versus N88S.
Abstract: Patterns of
A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism.
Method: Primary protease resistance-associated mutations were defined as any change versus wild-type at positions 23, 24, 30, 32, 46, 47, 48, 50, 54, 82, 84, 88, and 90 in the viral protease, with the following exceptions: I54V and N88D (not reported to occur without other primary mutations) and V82I (known polymorphism in PI-naive patients).
HIV-1 protease catalytic efficiency effects caused by random single amino acid substitutions.
PMID: 17090696
2007
Molecular biology and evolution
Abstract: In particular, the mutation N88D, lethal for the wild-type protease, restored the wild-type catalytic efficiency when combined with the highly deleterious mutation D30N.
Within-host co-evolution of Gag P453L and protease D30N/N88D demonstrates virological advantage in a highly protease inhibitor-exposed HIV-1 case.
PMID: 17209774
2006
AIDS research and human retroviruses
Abstract: First, D30N was positively associated with N88D but negatively associated with N88S.
Abstract: In 16 patients having isolates with more than one combination of mutations at positions 30, 88, and 90, all exhibited one of the steps in the following progression: D30N-->D30N+N88D-->D30N+N88D+L90M-->D30N+N88D+L90M+(L33F+/-I84V or M46I/L+/-I54V).
Abstract: Second, D30N and L90M were negatively associated except in the presence of N88D<
Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate.
Abstract: Using the chi2 test, we show a positive correlation between the nelfinavir-resistant D30N/N88D protease mutations and mutations at the p1-p6 cleavage site as compared to the other cleavage sites.
HIV mutation literature information.
PMID: 
2009
AIDS (London, England)
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