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Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens 1
Author(s) -
Sanderson S.J.,
Westrop G.D.,
Scharfstein J.,
Mottram J.C.,
Coombs G.H.
Publication year - 2003
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/s0014-5793(03)00327-2
Subject(s) - cysteine , biology , biochemistry , serine , cysteine proteinase inhibitors , recombinant dna , serine proteinase inhibitors , peptide sequence , enzyme , microbiology and biotechnology , gene , serine protease , protease , apoptosis , programmed cell death , caspase
Cysteine peptidase inhibitor genes ( ICP ) of the chagasin family have been identified in protozoan ( Leishmania mexicana and Trypanosoma brucei ) and bacterial ( Pseudomonas aeruginosa ) pathogens. The encoded proteins have low sequence identities with each other and no significant identity with cystatins or other known cysteine peptidase inhibitors. Recombinant forms of each ICP inhibit protozoan and mammalian clan CA, family C1 cysteine peptidases but do not inhibit the clan CD cysteine peptidase caspase 3, the serine peptidase trypsin or the aspartic peptidases pepsin and thrombin. The functional homology between ICPs implies a common evolutionary origin for these bacterial and protozoal proteins.