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Human immunodeficiency virus type 1 viral background plays a major role in development of resistance to protease inhibitors.
Rose, R E; Gong, Y F; Greytok, J A; Bechtold, C M; Terry, B J; Robinson, B S; Alam, M; Colonno, R J; Lin, P F.
Afiliación
  • Rose RE; Department of Virology, Bristol-Myers Squibb Company, Wallingford, CT 06492, USA.
Proc Natl Acad Sci U S A ; 93(4): 1648-53, 1996 Feb 20.
Article en En | MEDLINE | ID: mdl-8643685
The observed in vitro and in vivo benefit of combination treatment with anti-human immunodeficiency virus (HIV) agents prompted us to examine the potential of resistance development when two protease inhibitors are used concurrently. Recombinant HIV-1 (NL4-3) proteases containing combined resistance mutations associated with BMS-186318 and A-77003 (or saquinavir) were either inactive or had impaired enzyme activity. Subsequent construction of HIV-1 (NL4-3) proviral clones containing the same mutations yielded viruses that were severely impaired in growth or nonviable, confirming that combination therapy may be advantageous. However, passage of BMS-186318-resistant HIV-1 (RF) in the presence of either saquinavir or SC52151, which represented sequential drug treatment, produced viable viruses resistant to both BMS-186318 and the second compound. The predominant breakthrough virus contained the G48V/A71T/V82A protease mutations. The clone-purified RF (G48V/A71T/V82A) virus, unlike the corresponding defective NL4-3 triple mutant, grew well and displayed cross-resistance to four distinct protease inhibitors. Chimeric virus and in vitro mutagenesis studies indicated that the RF-specific protease sequence, specifically the Ile at residue 10, enabled the NL4-3 strain with the triple mutant to grow. Our results clearly indicate that viral genetic background will play a key role in determining whether cross-resistance variants will arise.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteasa del VIH / VIH-1 / Inhibidores de la Proteasa del VIH Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1996 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteasa del VIH / VIH-1 / Inhibidores de la Proteasa del VIH Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1996 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos