Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus.
J Virol
; 67(1): 360-5, 1993 Jan.
Article
en En
| MEDLINE
| ID: mdl-8093220
ABSTRACT
Incorporation of human immunodeficiency virus type 1 (HIV-1) envelope proteins into vesicular stomatitis virus (VSV) particles was studied in a system that allows expressed envelope proteins to rescue phenotypically a temperature-sensitive mutant of VSV (tsO45). This mutant exhibits defective transport of its own envelope glycoprotein (G) and can be rescued by simultaneous expression of wild-type G protein from cDNA. We report here that a hybrid HIV-1-VSV protein containing the extracellular and transmembrane domains of the HIV-1 envelope protein fused to the cytoplasmic domain of VSV G protein was able to rescue the tsO45 mutant lacking the G protein, while the wild-type HIV-1 envelope protein was not. The VSV(HIV) pseudotypes obtained infected only CD4+ cells and were neutralized specifically by anti-HIV-1 sera. Our results indicate that the cytoplasmic tail of the VSV glycoprotein contains an independent signal capable of directing a foreign protein into VSV particles. The VSV(HIV) pseudotypes generated here were prepared in the absence of HIV-1 and should be useful for identifying molecules that block HIV-1 entry.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Glicoproteínas de Membrana
/
Productos del Gen env
/
Proteínas del Envoltorio Viral
/
Proteínas Virales de Fusión
/
VIH-1
/
Virus de la Estomatitis Vesicular Indiana
Idioma:
En
Revista:
J Virol
Año:
1993
Tipo del documento:
Article