Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense
The catalytic domains of two closely related cysteine proteinases (CP1 and CP2) from Trypanosoma congolense, referred to as C1 and C2, were expressed as proforms in Escherichia coli (C1) and in the baculovirus system (C1 and C2). While the bacterial expression system did not allow recovery of active C1, the baculovirus system led to secretion of inactive zymogens which could be processed at acidic pH into mature enzymes. Active C1 and C2 were purified from serum-free culture supernatants by anion-exchange chromatography and characterised. Their kinetic parameters and pH activity profiles confirmed the relatedness between C2 and native CP2 (congopain). These properties also underline major functional differences between C1 and C2, that appear to relate to discrete but essential sequence differences. It is likely that these two enzymes perform distinct roles in vivo, in the parasite and/or in the host-parasite relationships.
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dig-cirad-fr-4833222023-06-28T14:37:50Z http://agritrop.cirad.fr/483322/ http://agritrop.cirad.fr/483322/ Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense. Boulangé Alain, Serveau Carole, Brillard M., Minet Cécile, Gauthier Francis, Diallo Adama, Lalmanach Gilles, Authié Edith. 2001. International Journal for Parasitology, 31 : 1435-1440.https://doi.org/10.1016/S0020-7519(01)00267-3 <https://doi.org/10.1016/S0020-7519(01)00267-3> Researchers Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense Boulangé, Alain Serveau, Carole Brillard, M. Minet, Cécile Gauthier, Francis Diallo, Adama Lalmanach, Gilles Authié, Edith eng 2001 International Journal for Parasitology L72 - Organismes nuisibles des animaux The catalytic domains of two closely related cysteine proteinases (CP1 and CP2) from Trypanosoma congolense, referred to as C1 and C2, were expressed as proforms in Escherichia coli (C1) and in the baculovirus system (C1 and C2). While the bacterial expression system did not allow recovery of active C1, the baculovirus system led to secretion of inactive zymogens which could be processed at acidic pH into mature enzymes. Active C1 and C2 were purified from serum-free culture supernatants by anion-exchange chromatography and characterised. Their kinetic parameters and pH activity profiles confirmed the relatedness between C2 and native CP2 (congopain). These properties also underline major functional differences between C1 and C2, that appear to relate to discrete but essential sequence differences. It is likely that these two enzymes perform distinct roles in vivo, in the parasite and/or in the host-parasite relationships. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/483322/1/483322.pdf text Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1016/S0020-7519(01)00267-3 10.1016/S0020-7519(01)00267-3 http://catalogue-bibliotheques.cirad.fr/cgi-bin/koha/opac-detail.pl?biblionumber=167745 info:eu-repo/semantics/altIdentifier/doi/10.1016/S0020-7519(01)00267-3 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1016/S0020-7519(01)00267-3 |
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L72 - Organismes nuisibles des animaux L72 - Organismes nuisibles des animaux Boulangé, Alain Serveau, Carole Brillard, M. Minet, Cécile Gauthier, Francis Diallo, Adama Lalmanach, Gilles Authié, Edith Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
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The catalytic domains of two closely related cysteine proteinases (CP1 and CP2) from Trypanosoma congolense, referred to as C1 and C2, were expressed as proforms in Escherichia coli (C1) and in the baculovirus system (C1 and C2). While the bacterial expression system did not allow recovery of active C1, the baculovirus system led to secretion of inactive zymogens which could be processed at acidic pH into mature enzymes. Active C1 and C2 were purified from serum-free culture supernatants by anion-exchange chromatography and characterised. Their kinetic parameters and pH activity profiles confirmed the relatedness between C2 and native CP2 (congopain). These properties also underline major functional differences between C1 and C2, that appear to relate to discrete but essential sequence differences. It is likely that these two enzymes perform distinct roles in vivo, in the parasite and/or in the host-parasite relationships. |
format |
article |
topic_facet |
L72 - Organismes nuisibles des animaux |
author |
Boulangé, Alain Serveau, Carole Brillard, M. Minet, Cécile Gauthier, Francis Diallo, Adama Lalmanach, Gilles Authié, Edith |
author_facet |
Boulangé, Alain Serveau, Carole Brillard, M. Minet, Cécile Gauthier, Francis Diallo, Adama Lalmanach, Gilles Authié, Edith |
author_sort |
Boulangé, Alain |
title |
Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
title_short |
Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
title_full |
Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
title_fullStr |
Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
title_full_unstemmed |
Functional expression of the catalytic domains of two cysteine proteinases from Trypanosoma congolense |
title_sort |
functional expression of the catalytic domains of two cysteine proteinases from trypanosoma congolense |
url |
http://agritrop.cirad.fr/483322/ http://agritrop.cirad.fr/483322/1/483322.pdf |
work_keys_str_mv |
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