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

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.

authors

• Meek, Thomas

published proceedings

• Proc Natl Acad Sci U S A

altmetric score

• 6

author list (cited authors)

• Debouck, C., Gorniak, J. G., Strickler, J. E., Meek, T. D., Metcalf, B. W., & Rosenberg, M.

citation count

• 271

complete list of authors

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

publication date

• December 1987

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Amino Acid Sequence
• Cloning, Molecular
• Endopeptidases
• Escherichia Coli
• Gene Products, Gag
• Genes, Viral
• HIV
• Hiv Protease
• Molecular Weight
• Protein Processing, Post-Translational
• Recombinant Proteins
• Retroviridae Proteins

PubMed Central ID

• 3321060

Digital Object Identifier (DOI)

• 10.1073/pnas.84.24.8903

start page

• 8903

end page

• 8906

volume

• 84

issue

• 24

URL

• http://dx.doi.org/10.1073/pnas.84.24.8903