| Literature DB >> 12108538 |
Gilles Lalmanach1, Alain Boulangé, Carole Serveau, Fabien Lecaille, Julio Scharfstein, Francis Gauthier, Edith Authié.
Abstract
Trypanosomes are the etiological agents of human sleeping sickness and livestock trypanosomosis (nagana), which are major diseases in Africa. Their cysteine proteases (CPs), which are members of the papain family, are expressed during the infective stages of the parasites' life cycle. They are suspected to act as pathogenic factors in the mammalian host, where they also trigger prominent immune responses. Trypanosoma congolense, a major pathogenic species in livestock, possesses at least two families of closely related CPs, named CP1 and CP2. Congopain, a CP2-type of enzyme, shares structural and functional resemblances with cruzipain from T. cruzi and with mammalian cathepsin L. Like CPs from other Trypanosomatids, congopain might be an attractive target for trypanocidal drugs. Here we summarise the current knowledge in the two main areas of research on congopain: first, the biochemical properties of congopain were characterised and its substrate specificity was determined, as a first step towards drug design; second, the possibility was being explored that inhibition of congopain by host-specific antibodies may mitigate the pathology associated with trypanosome infection.Entities:
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Year: 2002 PMID: 12108538 DOI: 10.1515/BC.2002.077
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915