Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus.

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Owens RJ,Rose JK

doi

10.1128/JVI.67.1.360-365.1993

subject

Has Abstract

pub_date

1993-01-01 00:00:00

pages

360-5

issue

1

eissn

0022-538X

issn

1098-5514

journal_volume

67

pub_type

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