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M9650014.TXT
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1996-03-09
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Document 0014
DOCN M9650014
TI The Vpr protein of human immunodeficiency virus type 1 binds to
nucleocapsid protein p7 in vitro.
DT 9605
AU Li MS; Garcia-Asua G; Bhattacharyya U; Mascagni P; Austen BM; Roberts
MM; Department of Medical Microbiology, St. George's Hospital Medical;
School, University of London, U.K.
SO Biochem Biophys Res Commun. 1996 Jan 5;218(1):352-5. Unique Identifier :
AIDSLINE MED/96136326
AB The Vpr protein of human immunodeficiency virus type 1 (HIV-1) is
incorporated into the virion by the Gag polyprotein precursor Pr55gag.
The importance of the p6gag sequence at the C-terminal end of Pr55gag
has a crucial role in Vpr incorporation. To identify the Gag sequences
directly involved in Vpr binding, we compared the Vpr binding affinities
of the 71 amino acid nucleocapsid protein p7, the C-terminal peptide
(35-71) p7C and p6gag by affinity chromatography. p7 and p7C have the
strongest Vpr binding activities compared to p6gag. These results
suggest that the nucleocapsid protein and its C-terminal domain may be
important for the incorporation of Vpr into the mature HIV-1 virion and
the subsequent localisation of viral nucleic acid to the cell nucleus by
Vpr.
DE Blotting, Western Capsid/CHEMISTRY/ISOLATION & PURIF/*METABOLISM
Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Gene
Products, gag/ISOLATION & PURIF/METABOLISM Gene Products,
vpr/CHEMISTRY/ISOLATION & PURIF/*METABOLISM Human HIV-1/*METABOLISM
Peptide Fragments/CHEMICAL SYNTHESIS/METABOLISM Protein Binding
Support, Non-U.S. Gov't Viral Core Proteins/CHEMISTRY/ISOLATION &
PURIF/*METABOLISM Virion/METABOLISM JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).