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Solid phase synthesis of the proteinase of bovine leukemia virus Comparison of its specificity to that of HIV‐2 proteinase
Author(s) -
Bláha Ivo,
Tözsér József,
Kim Young,
Copeland Terry D.,
Oroszlan Stephen
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80813-v
Subject(s) - bovine leukemia virus , oligopeptide , virology , peptide , leukemia , enzyme , virus , biology , murine leukemia virus , chemistry , microbiology and biotechnology , biochemistry , immunology
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.