Mutations in HIV-1 gag cleavage sites and their association with protease mutations

AIDS

Volumn 15, Issue 4, 2001, Pages 526-528

  Koch, Nathalie ^a,b   Yahi, Nouara ^a,b   Fantini, Jacques ^a,b   Tamalet, Catherine ^a,b  

^a TIMONE HOSPITAL   (France)

^b AIX MARSEILLE UNIVERSITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ABACAVIR; ADEFOVIR; AMPRENAVIR; DELAVIRDINE; DIDANOSINE; EFAVIRENZ; GAG PROTEIN; INDINAVIR; LAMIVUDINE; NELFINAVIR; NEVIRAPINE; PROTEINASE; PROTEINASE INHIBITOR; RITONAVIR; SAQUINAVIR; STAVUDINE; ZALCITABINE; ZIDOVUDINE;

ARTICLE; CONFORMATIONAL TRANSITION; GENE LOCUS; GENE MUTATION; GENE SEQUENCE; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION;

CLUSTER ANALYSIS; GENES, GAG; HIV PROTEASE; HIV-1; HUMANS; MUTATION; PHYLOGENY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, RNA;

EID: 0035831126     PISSN: 02699370     EISSN: None     Source Type: Journal    
DOI: 10.1097/00002030-200103090-00013     Document Type: Article

References (13)

1. HIV-1 evolution under pressure of protease inhibitors: Climbing the stairs of viral fitness
2. Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
3. Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites
4. In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor
5. Amprenavir resistant mutants show reduced viral fitness: Correlation of protease mutations, cleavage site mutations, enzyme kinetics, viral polyprotein processing and viral growth kinetics
6. Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo
7. Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: Phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients
8. Variations in the p7/p1 gag cleavage region and virological response to a HIV protease inhibitor
9. Polymorphism of HIV type 1 Gag p7/p1 and p1/p6 cleavage sites: Clinical significance and implications for resistance to protease inhibitors
10. Comparison of human immunodeficiency virus type 1 (HIV-1) protease mutations in HIV-1 genomes detected in plasma and in peripheral blood mononuclear cells from patients receiving combination drug therapy
11. Natural variation in HIV-1 protease, Gag p7 and p6, and protease cleavage sites within gag/pol polyproteins: Amino acid substitutions in the absence of protease inhibitors in mothers and children infected by human immunodeficiency virus type 1
12. 3′-Azido-3′-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes