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PMID: 7745738 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing.

Journal of virology ·Vol. 69 ·No. 6 ·1995-06-00 ·Pages 3878-84

Zybarth G, Carter C

Abstract

A critical step in the formation of infectious retroviral particles is the activation of the virally encoded protease (PR) and its release from the Gag-Pol precursor polyprotein. To identify factors that influence this step, the maturation of human immunodeficiency virus type 1 PR from various Gag-PR polyproteins was assayed in vitro by a using rabbit reticulocyte lysate as a coupled transcription-translation-autoprocessing system. Highly efficient autoprocessing was detected with polyproteins containing the viral nucleocapsid (NC) domain. In contrast, polyproteins consisting of only p6 and PR domains or containing a truncated NC domain exhibited no autoprocessing activity. Experiments designed to test the dimerization capability of short PR polyproteins revealed that precursors containing the NC domain exhibited very efficient homotypic protein-protein interactions while PR precursors consisting of only p6 and PR did not interact efficiently. The strong correlation between autoprocessing activity and PR polyprotein precursor dimerization suggests that NC and p6* domains play a role in PR activation by influencing the dimerization of the PR domain in the precursor.

MeSH Terms
Amino Acid Sequence Base Sequence Biopolymers DNA Primers Fusion Proteins, gag-pol/genetics,metabolism HIV Protease/genetics,metabolism HIV-1/enzymology,metabolism Molecular Sequence Data Protein Processing, Post-Translational
Chemicals
Biopolymers DNA Primers Fusion Proteins, gag-pol HIV Protease
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zybarth G
Department of Microbiology, State University of New York at Stony Brook 11794, USA.
Carter C
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.69.6.3878-3884.1995
Published
1995-06-00
Pages
3878-84
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC189109
Subset
IM
Grants
NIGMS NIH HHS · GM 48294 · United States
External Links
PubMed source DOI: 10.1128/JVI.69.6.3878-3884.1995 PMC Full Text View journal details
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