Substrates and inhibitors of human T-cell leukemia virus type 1 (HTLV-1) proteinase

• Published in: Leukemia Vol. 11; pp. 45 - 46
• Main Authors: HRUSKOVA-HEIDINGSFELDOVA, O, BLAHA, I, URBAN, J, STROP, P, PICHOVA, I
• Format: Conference Proceeding Journal Article
• Language: English
• Published: London Nature Publishing 01.04.1997
• Subjects: Action of physical and chemical agents; AIDS/HIV; Amino Acid Sequence; Aspartic Acid Endopeptidases - chemistry; Aspartic Acid Endopeptidases - isolation & purification; Aspartic Acid Endopeptidases - metabolism; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Human T-lymphotropic virus 1; Human T-lymphotropic virus 1 - enzymology; Humans; Microbiology; Molecular Sequence Data; Oligopeptides - chemical synthesis; Oligopeptides - metabolism; Oligopeptides - pharmacology; Protease Inhibitors - chemical synthesis; Protease Inhibitors - pharmacology; Protein Folding; Substrate Specificity; Virology
• ISSN: 0887-6924; 1476-5551

Human T-cell leukemia virus type 1 (HTLV-1) proteinase, a 125 residue polypeptide, was chemically synthesized using the solid phase method. The crude product was purified, renaturated and proteolytic activity was tested using oligopeptide substrates derived from processing sites of various retroviral polyproteins. Cleavage of the oligopeptide substrates together with an initial study using a series of HIV-1 and MAV (myeloblastosis associated virus) proteinase inhibitors suggest that the substrate specificity of HTLV-1 proteinase is very close to that of BLV (bovine leukemia virus) proteinase and distinct from that of both HIV-1 and MAV proteinases.