Solid phase synthesis of the proteinase of bovine leukemia virus Comparison of its specificity to that of HIV-2 proteinase

Ivo Bláha, József Tözsér, Young Kim, Terry D. Copeland, Stephen Oroszlan

Research output: Contribution to journalArticle

19 Citations (Scopus)


The 126-residue proteinase (PR) of bovine leukemia virus (BLV) was synthesized by solid-phase peptide synthesis and its activity was shown using various oligopeptide substrates representing cleavage sites in BLV, human T-cell leukemia virus type 1 (HTLV-1), murine leukemia virus (MuLV) and human immunodeficiency virus type 1 (HIV-1). The specificity of the BLV PR was also compared to that of chemically synthesized human immunodeficiency virus type 2 (HIV-2) PR. Many of the peptides were cleaved at the expected site, however, 6 out of 15 were hydrolyzed only by one of the PRs. Furthermore, one BLV peptide was processed differently by the two enzymes. These results, together with the relative activities and the lack of inhibition of BLV PR by two HIV-1 PR inhibitors, suggest that the BLV PR specificity is substantially different from that of HIV PRs.

Original languageEnglish
Pages (from-to)389-393
Number of pages5
JournalFEBS letters
Issue number3
Publication statusPublished - Sep 14 1992



  • BLV proteinase
  • Solid phase peptide synthesis
  • Substrate specificity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this