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 HIV mutation literature information.


  Virologic responses to a ritonavir--saquinavir-containing regimen in patients who had previously failed nelfinavir.
 PMID: 10202820       1999       AIDS (London, England)
Abstract: The most frequent baseline mutations in the protease gene prior to switching were D30N (13 out of 18), N88D (eight out of 18) and M36I (eight out of 18).


  Clinical resistance patterns and responses to two sequential protease inhibitor regimens in saquinavir and reverse transcriptase inhibitor-experienced persons.
 PMID: 10228055       1999       The Journal of infectious diseases
Abstract: Rapid failure was surprisingly associated with baseline presence of protease gene mutation L90M (P=.04) in the absence of D30N and with RT mutations D67N (P<.01), K70R/S (P=.02), and K219Q/W/R/E (P<.01).


  Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.
 PMID: 10429209       1999       European journal of biochemistry
Abstract: In contrast, D30N is variable in its activity on different substrates (10-110% of wild-type), with the PR-RT site being the most affected.
Abstract: The mutants D30N and V82S were similar to wild-type protease in their stability toward urea denaturation, while R8Q, G48V, and L90M showed 1.5 to 2.7-fold decreased stability, and N88D and K45I showed 1.6 to 1.7-fold increased stability.


  Genetic variation and susceptibilities to protease inhibitors among subtype B and F isolates in Brazil.
 PMID: 9925514       1999       Antimicrobial agents and chemotherapy
Abstract: The frequency of critical PI resistance substitutions (amino acid changes D30N, V82A/F/T, I84V, N88D, and L90M) among Brazilian isolates is very low (mean, 2.5%), and the associated secondary substitutions (amino acid positions 10L, 20K, 36M, 46M, 48G, 54I, 63P, 71A, and 77A) are infrequent.


  Human immunodeficiency virus type 1 protease genotypes and in vitro protease inhibitor susceptibilities of isolates from individuals who were switched to other protease inhibitors after long-term saquinavir treatment.
 PMID: 9573309       1998       Journal of virology
Abstract: Reduced susceptibility to nelfinavir was found in 14 isolates, but only 1 possessed the D30N mutation.


  A preliminary evaluation of nelfinavir mesylate, an inhibitor of human immunodeficiency virus (HIV)-1 protease, to treat HIV infection.
 PMID: 9607830       1998       The Journal of infectious diseases
Abstract: Studies of viral genotype and phenotype after virus rebound revealed that the initial active site mutation allowing for nelfinavir resistance is mediated by a unique amino acid substitution in the HIV-1 protease D30N, which does not confer in vitro phenotypic cross-resistance to the currently available protease inhibitors.


  Nelfinavir. A review of its therapeutic efficacy in HIV infection.
 PMID: 9664204       1998       Drugs
Abstract: A unique mutation at codon 30 (D30N) of the protease gene confers resistance to nelfinavir, but HIV with D30N mutation remains fully susceptible to indinavir, ritonavir and saquinavir in vitro.


  Genotypic and phenotypic characterization of human immunodeficiency virus type 1 variants isolated from patients treated with the protease inhibitor nelfinavir.
 PMID: 9756769       1998       Antimicrobial agents and chemotherapy
Abstract: Although the appearance of D30N was occasionally associated with concurrent or sequential emergence of other changes (e.g., at residues 35, 36, 46, 71, 77, and 88), genotypic changes associated with phenotypic resistance to other protease inhibitors were not observed (e.g., at residues 48, 50, 82, and 84) or were only rarely observed (e.g., at residue 90).
Abstract: Nucleotide sequence analysis of protease genes from plasma HIV type 1 (HIV-1) RNA revealed a unique aspartic acid (D)-to-asparagine (N) substitution at residue 30 (D30N) in 25 of 55 patients treated with nelfinavir for a median of 13 weeks.
Abstract: Similar results were observed in phenotypic assays utilizing HIV-1 NL4-3, which contained the D30N substitution alone or in combination with substitutions at other residues (e.g., residues 46, 7



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