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Cloning of the bovine leukemia virus proteinase in Escherichia coli and comparison of its specificity to that of human T-cell leukemia virus proteinase

  1. Author:
    Zahuczky, G.
    Boross, P.
    Bagossi, P.
    Emri, G.
    Copeland, T. D.
    Oroszlan, S.
    Louis, J. M.
    Tozser, J.

  2. Author Address

    Tozser J Debrecen Univ Med, Sch Med, Dept Biochem & Mol Biol POB 6 H-4012 Debrecen Hungary Debrecen Univ Med, Sch Med, Dept Biochem & Mol Biol H-4012 Debrecen Hungary NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Special Program Prot Chem Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Mol Virol & Carcinogenesis Lab Frederick, MD 21702 USA NIDDKD, Chem Phys Lab, NIH Bethesda, MD 20892 USA
    1. Year: 2000
  2. Journal: Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology
    1. 1478
    2. 1
    3. Pages: 1-8
  4. Type of Article: Article
  1. Abstract:

    The protinase of bovine leukemia virus (BLV) was cloned into pMal-c2 vector with N-terminal or with N- as well as C-terminal flanking sequences, and expressed in fusion with maltose binding protein. The proteinase self-processed itself from the fusion protein during expression and formed inclusion bodies. The enzyme was purified from inclusion bodies by cation-exchange chromatography followed by gel filtration. Specificity of the enzyme was compared to that of human T-cell leukemia proteinase type I. Although the two viruses belong to the same subfamily of retroviruses, the differences in their proteinase specificity, based on kinetics with oligopeptide substrates representing naturally occurring cleavage sites as well as on inhibition pattern, appear to be pronounced. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 37]

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