Solid phase synthesis of the proteinase of bovine leukemia virus. Comparison of its specificity to that of HIV-2 proteinase.
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.
Bláha
I
I
Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research and Development Center, MD 21702.
Tözsér
J
J
Kim
Y
Y
Copeland
T D
TD
Oroszlan
S
S
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000138:chemical synthesis* / Q000378:metabolism; D016333:HIV Protease; D001909:Leukemia Virus, Bovine / Q000201:enzymology*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013379:Substrate Specificity
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2