Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens

• Published in: FEBS letters Vol. 542; no. 1; pp. 12 - 16
• Main Authors: Sanderson, S.J., Westrop, G.D., Scharfstein, J., Mottram, J.C., Coombs, G.H.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 08.05.2003
• Subjects: Amino Acid Sequence; Animals; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - pharmacology; Chagasin; Cysteine peptidase inhibitor; Cysteine Proteinase Inhibitors - genetics; Cysteine Proteinase Inhibitors - metabolism; Cysteine Proteinase Inhibitors - pharmacology; Eukaryota - enzymology; Evolution, Molecular; Leishmania; Leishmania major - genetics; Leishmania mexicana - genetics; Mammals; Molecular Sequence Data; Peptidase; Protease; Protozoan Proteins - genetics; Protozoan Proteins - metabolism; Protozoan Proteins - pharmacology; Pseudomonas; Pseudomonas aeruginosa - genetics; Recombinant Proteins - pharmacology; Sequence Alignment; Sequence Homology, Amino Acid; Trypanosoma; Peptidase; Trypanosoma; Chagasin; Protease; Leishmania; Pseudomonas; Cysteine peptidase inhibitor
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(03)00327-2

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.