Primary structure and partial characterization of a life-cycle-regulated cysteine protease from trypanosoma (Nannomonas) congolense

• Published in: Gene Vol. 161; no. 1; pp. 125 - 128
• Main Authors: Fish, Wallace R., Nkhungulu, Zeres M., Muriuki, Cecilia W., Ndegwa, David M., Lonsdale-Eccles, John D., Steyaert, Jan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 1995
• Subjects: African trypanosome; Amino Acid Sequence; Animals; antigen; Base Sequence; Blotting, Northern; cathepsin; Cloning, Molecular; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; DNA, Complementary; Gene Expression Regulation, Enzymologic; Molecular Sequence Data; mRNA; papain; parasite; pathogen; polypyrimidine; proteinase; Trypanosoma congolense; Trypanosoma congolense - enzymology; Trypanosoma congolense - genetics; Trypanosoma congolense - growth & development; Africa; African trypanosome; aa; polypyrimidine; T.b; mRNA; antigen; cathepsin; L; papain; bp; Tc; parasite; proteinase; T; kb; Cypr; pathogen; cDNA
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/0378-1119(95)00304-O

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.