|Title||Primary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense.|
|Publication Type||Journal Article|
|Year of Publication||1995|
|Authors||Fish, W. R., Z. M. Nkhungulu, C. W. Muriuki, D. M. Ndegwa, J. D. Lonsdale-Eccles, and J. Steyaert|
|Date Published||1995 Aug 8|
|Keywords||Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cloning, Molecular, Cysteine Endopeptidases, DNA, Complementary, Gene Expression Regulation, Enzymologic, Molecular Sequence Data, Trypanosoma congolense|
Trypanosoma (Nannomonas) congolense is an important pathogenic parasite of domestic livestock in Africa. We have cloned a cDNA encoding a prepro-cysteine protease of this protozoan, the sequence of which indicates it is an early mRNA processing intermediate. Northern analysis demonstrates a life-cycle-stage specificity similar to previously described enzymatic data. The deduced amino-acid sequence shows extensive similarity to cysteine proteases of other parasitic protozoa, as well as papain and cathepsin L. As with other African trypanosomes, a poly-proline tract connects the catalytic domain with an unusual C-terminal extension.