Conserved functional organization of the human immunodeficiency virus type 1 and visna virus Rev proteins.

Journal Article

Visna virus encodes a posttranscriptional regulatory protein that is functionally analogous to the Rev trans activator of human immunodeficiency virus type 1. Here, we demonstrate that the known functional organization of the human immunodeficiency virus type 1 Rev trans activator is shared by the distantly related visna virus Rev protein. In particular, both Rev proteins contain an N-terminal domain marked by a highly basic core motif that determines RNA sequence specificity, as well as a second C-terminal domain containing an essential leucine-rich motif that functions as an activation domain. Chimeric proteins consisting of the binding domain of one Rev protein fused to the activation domain of the other were fully functional in the viral sequence context cognate for the binding domain. We also describe derivatives of visna virus Rev bearing a defective activation domain that displayed a trans-dominant negative phenotype in transfected cells. These visna virus Rev mutants may prove useful in the derivation of transgenic animals resistant to this agriculturally important retroviral pathogen.

Full Text

Duke Authors

Cited Authors

  • Tiley, LS; Malim, MH; Cullen, BR

Published Date

  • July 1991

Published In

Volume / Issue

  • 65 / 7

Start / End Page

  • 3877 - 3881

PubMed ID

  • 1645796

International Standard Serial Number (ISSN)

  • 0022-538X

Language

  • eng

Conference Location

  • United States