Procongopain from Trypanosoma congolense is processed at basic pH : An unusual feature among cathepsin L-like cysteine proteases

Serveau Carole, Boulangé Alain, Lecaille Fabien, Gauthier Francis, Authié Edith, Lalmanach Gilles. 2003. Procongopain from Trypanosoma congolense is processed at basic pH : An unusual feature among cathepsin L-like cysteine proteases. Biological Chemistry, 384 : 921-927.

Résumé : Congopain, the major cysteine protease from Trypanosoma congolense, is synthesized as an inactive zymogen, and further converted into its active form after removal of the proregion, most probably via an autocatalytic mechanism. Processing of recombinant procongopain occurs via an apparent one-step or a multistep mechanism depending on the ionic strength. The auto-activation is pH-dependent, with an optimum at pH 4.0, and no activation observed at pH 6.0. After addition of dextran sulfate (10 [mu]g/ml), an approx. 20-fold increase of processing (expressed as enzymatic activity) is observed. Furthermore, in the presence of dextran sulfate, procongopain can be processed at pH 8.0, an unusual feature among papain-like enzymes. Detection of procongopain and trypanosomal enzymatic activity in the plasma of T. congolense-infected cattle, together with the capacity of procongopain to be activated at weakly basic pH, suggest that procongopain may be extracellularly processed in the presence of blood vessel glycosaminoglycans, supporting the hypothesis that congopain acts as a pathogenic factor in host-parasite relationships.

Classification Agris : L72 - Organismes nuisibles des animaux

Auteurs et affiliations

• Serveau Carole, Université François Rabelais (FRA)
• Boulangé Alain, CIRAD-EMVT-SANTE ANIMALE (KEN) ORCID: 0000-0002-8505-7465
• Lecaille Fabien, Université François Rabelais (FRA)
• Gauthier Francis, Université François Rabelais (FRA)
• Authié Edith, CIRAD-EMVT-SANTE ANIMALE (KEN)
• Lalmanach Gilles, Université François Rabelais (FRA)

Source : Cirad - Agritrop (https://agritrop.cirad.fr/517447/)

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