Journal
VIRUS RESEARCH
Volume 105, Issue 1, Pages 97-100Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.virusres.2004.04.010
Keywords
HIV-1 protease; limited proteolysis; complement proteins; protease cleavage site; HIV-1 pathogenesis
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We have investigated the ability of HIV-1 protease to cleave human complement proteins of the classical complement pathway: C1q, C2 and C4 as well as the regulatory protein, C1-inhibitor. Purified complement proteins were incubated with recombinant HIV-1 protease in vitro and analyzed by SDS-PAGE and immunoblotting assay. The only cleavage site was found in N-terminal region of C1-inhibitor, and it was located between residues Leu-32 and Phe-33 as determined by amino acid sequence analysis of the 85 kDa proteolyfic fragment after 12 Edman degradation cycles. The HIV-1 protease cleavage sites were not found in C1q, C2 and C4 protein. HIV-1 protease-susceptible site in N-terminal region of C1-inhibitor is very close to the cleavage sites of some other proteases that are able to induce N-terminal proteolysis of the protein. (C) 2004 Elsevier B.V. All rights reserved.
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