Cargando…
G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to Raltegravir whereas Y143C does not
BACKGROUND: HIV-2 is endemic in West Africa and has spread throughout Europe. However, the alternatives for HIV-2-infected patients are more limited than for HIV-1. Raltegravir, an integrase inhibitor, is active against wild-type HIV-2, with a susceptibility to this drug similar to that of HIV-1, an...
Autores principales: | Ni, Xiao-Ju, Delelis, Olivier, Charpentier, Charlotte, Storto, Alexandre, Collin, Gilles, Damond, Florence, Descamps, Diane, Mouscadet, Jean-François |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3170264/ https://www.ncbi.nlm.nih.gov/pubmed/21854605 http://dx.doi.org/10.1186/1742-4690-8-68 |
Ejemplares similares
-
The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation
por: Delelis, Olivier, et al.
Publicado: (2009) -
Mutations Located outside the Integrase Gene Can Confer Resistance to HIV-1 Integrase Strand Transfer Inhibitors
por: Malet, Isabelle, et al.
Publicado: (2017) -
Integrase and integration: biochemical activities of HIV-1 integrase
por: Delelis, Olivier, et al.
Publicado: (2008) -
G140S mutation rescues HIV-1 IN integration defect due to Q148H in vitro and in vivo
por: Delelis, Olivier, et al.
Publicado: (2009) -
A novel function for spumaretrovirus integrase: an early requirement for integrase-mediated cleavage of 2 LTR circles
por: Delelis, Olivier, et al.
Publicado: (2005)