Collect. Czech. Chem. Commun.
2000, 65, 1191-1197
https://doi.org/10.1135/cccc20001191
Proteases of HIV-1 and MAV Hydrolyze Specifically Human Apo-Hemopexin
Ivan Kluha,*, Věra Černáb, Iva Pichováa and Zdeněk Voburkaa
a Department of Protein Chemistry, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 166 10 Prague 6, Czech Republic
b Polypeptide Laboratories, Radiová 14, 102 27 Prague 10, Czech Republic
Abstract
The specificities of HIV-1 (Human Immunodeficiency Virus Type 1) and MAV (Myeloblastosis Associated Virus) proteases have been evaluated for their ability to split two-domain protein human apo-hemopexin. Both proteases hydrolyze only one peptidic bond Leu240-Ser241 located in the connecting region between two domains. The ability of viral proteases to cleave Leu-Ser bond was confirmed by cleavage of synthetic octapeptide His-Leu-Val-Leu-Ser-Ala-Leu-Thr-NH2 covering the susceptible area of human apo-hemopexin. The results demonstrate that the cleavage of Leu-Ser bond is not due to its location in the interdomain region of apo-hemopexin. The cleavable bond Leu-Ser has never been found either in viral or in non-viral proteins. According to the vector projection method this octapeptide was considered as non-hydrolyzable.
Keywords: HIV-1 protease; MAV protease; Proteolytic cleavage; Proteases; Hemopexin; Enzyme catalysis; Viral Proteins; Viruses.
References: 10 live references.
