Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens 1

FEBS Letters

Coombs, G.H.²  Westrop, G.D.²  Mottram, J.C.¹  Scharfstein, J.³  Sanderson, S.J.² 

[1] Wellcome Centre for Molecular Parasitology, University of Glasgow, The Anderson College, Glasgow G11 6NU, UK;Division of Infection and Immunity, Institute of Biomedical and Life Sciences, University of Glasgow, Joseph Black Building, Glasgow G12 8QQ, UK;Instituto de Biofı́sica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, CCS–Cidade Univesritária, 21944-900 Rio de Janeiro, Brazil

关键词: Chagasin;    Cysteine peptidase inhibitor;    Peptidase;    Protease;    Leishmania;    Trypanosoma;    Pseudomonas;   

DOI  :  10.1016/S0014-5793(03)00327-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown