Prevalence of the HIV protease mutation N88S causing hypersensitivity to amprenavir [7]

Clinical Infectious Diseases

Volumn 34, Issue 9, 2002, Pages 1288-1289

  Gallego, Oscar ^a   Corral, Angeélica ^a   De Mendoza, Carmen ^a   Soriano, Vincent ^a  

^a INSTITUTO DE SALUD CARLOS III   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMPRENAVIR; ANTIRETROVIRUS AGENT; INDINAVIR; NELFINAVIR; PROTEINASE; PROTEINASE INHIBITOR;

ANTIVIRAL ACTIVITY; GENE MUTATION; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; LETTER; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SUBSTITUTION; ANTI-HIV AGENTS; ASPARAGINE; CARBAMATES; DRUG HYPERSENSITIVITY; GENE FREQUENCY; HIV; HIV PROTEASE; HUMANS; MUTATION; SERINE; SULFONAMIDES;

EID: 0036569759     PISSN: 10584838     EISSN: None     Source Type: Journal    
DOI: 10.1086/339953     Document Type: Letter

References (7)

1. HIV-1 hypersusceptibility to amprenavir in vitro can be associated with virus load response to treatment in vivo
2. A mutation in HIV-1 protease, N88S, that causes in vitro hypersensitivity to amprenavir
3. In vitro resistance profile of the HIV-1 protease inhibitor BMS-232632
4. A mutation in HIV-1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A
5. Genotypic and phenotypic characterization of HIV-1 variants isolated from patients treated with the protease inhibitor nelfinavir
6. Drug resistance in patients experiencing early virologic failure under a triple combination including indinavir
7. Second Spanish consensus on the use of drug resistance testing in clinical practice