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PMID: 3321060 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor.

Debouck C, Gorniak JG, Strickler JE, Meek TD, Metcalf BW, Rosenberg M

Abstract

The mature gag and pol proteins of human immunodeficiency virus (HIV) and all retroviruses derive from large gag and gag-pol polyprotein precursors by posttranslational cleavage. A highly specific, virally encoded protease is required for this essential proteolytic processing. In this study, the HIV protease gene product was expressed in Escherichia coli and shown to autocatalyze its maturation from a larger precursor. In addition, this bacterially produced HIV protease specifically processed an HIV p55 gag polyprotein precursor when coexpressed in E. coli. This system will allow detailed structure-function analysis of the HIV protease and provides a simple assay for the development of potential therapeutic agents directed against this critical viral enzyme.

MeSH Terms
Amino Acid Sequence Cloning, Molecular Endopeptidases/genetics Escherichia coli/metabolism Gene Products, gag Genes, Viral HIV/enzymology,genetics HIV Protease Molecular Weight Protein Processing, Post-Translational Recombinant Proteins Retroviridae Proteins/metabolism
Chemicals
Gene Products, gag Recombinant Proteins Retroviridae Proteins Endopeptidases HIV Protease
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Debouck C
Department of Molecular Genetics, Smith Kline and French Laboratories, King of Prussia, PA 19406.
Gorniak J G
Strickler J E
Meek T D
Metcalf B W
Rosenberg M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1987-12-00
Pages
8903-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC299659
Subset
IM
Grants
NIAID NIH HHS · AI24845 · United States
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