Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

Interactions in vivo between the Vif protein of HIV-1 and the precursor (Pr55(GAG)) of the virion nucleocapsid proteins

Tools
- Tools
+ Tools

Syed, Farhatullah and McCrae, Malcolm A.. (2009) Interactions in vivo between the Vif protein of HIV-1 and the precursor (Pr55(GAG)) of the virion nucleocapsid proteins. Archives of Virology, Vol.154 (No.11). pp. 1797-1805. ISSN 0304-8608

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1007/s00705-009-0520-8

Abstract

The abnormality of viral core structure seen in vif-defective HIV-1 grown in PBMCs has suggested a role for Vif in viral morphogenesis. Using an in vivo mammalian two-hybrid assay, the interaction between Vif and the precursor (Pr55(GAG)) of the virion nucleocapsid proteins has been analysed. This revealed the amino-terminal (aa 1-22) and central (aa 70-100) regions of Vif to be essential for its interaction with Pr55(GAG), but deletion of the carboxy-terminal (aa 158-192) region of the protein had only a minor effect on its interaction. Initial deletion studies carried out on Pr55(GAG) showed that a 35-amino-acid region of the protein bridging the MA(p17)-CA(p24) junction was essential for its ability to interact with Vif. Site-directed mutagenesis of a conserved tryptophan (Trp(21)) near the amino terminus of Vif showed it to be important for the interaction with Pr55(GAG). By contrast, mutagenesis of the highly conserved YLAL residues forming part of the BC-box motif, shown to be important in Vif promoting degradation of APOBEC3G/3F, had little or no effect on the Vif-Pr55(GAG) interaction.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology > QR355 Virology
Divisions: Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Journal or Publication Title: Archives of Virology
Publisher: Springer Wien
ISSN: 0304-8608
Date: November 2009
Volume: Vol.154
Number: No.11
Number of Pages: 9
Page Range: pp. 1797-1805
Identification Number: 10.1007/s00705-009-0520-8
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
URI: http://wrap.warwick.ac.uk/id/eprint/17105

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us