Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis

Autores
Duschak, Vilma G; Barboza, M; Garcia, G. A.; Lammel, Estela M.; Couto, Alicia S; Isola, E L D
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Barboza, M. Universidad Nacional de General San Martín. Instituto de Investigaciones Biotecnológicas–INTECH; Argentina.
Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Lammel, Estela M. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.
Fil: Couto, Alicia S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. CIHIDECAR; Argentina.
Fil: Isola, E. L. D. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.
With the aim to study proteinases released to the culture medium during Trypanosoma cruzi metacyclogenesis, the presence of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the important role of these enzymes in metacyclogenesis.
Fuente
Parasitology 2006;132(Pt 3):345-355
Materia
Trypanosoma cruzi
Proteasas de Cisteína
Enfermedad de Chagas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
none
Repositorio
Sistema de Gestión del Conocimiento ANLIS MALBRÁN
Institución
Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
OAI Identificador
oai:sgc.anlis.gob.ar:123456789/2269

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spelling Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesisDuschak, Vilma GBarboza, MGarcia, G. A.Lammel, Estela M.Couto, Alicia SIsola, E L DTrypanosoma cruziProteasas de CisteínaEnfermedad de ChagasFil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Barboza, M. Universidad Nacional de General San Martín. Instituto de Investigaciones Biotecnológicas–INTECH; Argentina.Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Lammel, Estela M. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.Fil: Couto, Alicia S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. CIHIDECAR; Argentina.Fil: Isola, E. L. D. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.With the aim to study proteinases released to the culture medium during Trypanosoma cruzi metacyclogenesis, the presence of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the important role of these enzymes in metacyclogenesis.2006-03info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdf1469-8161http://sgc.anlis.gob.ar/handle/123456789/226910.1017/S0031182005009030Parasitology 2006;132(Pt 3):345-355reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLISParasitologynoneinfo:eu-repo/semantics/openAccesseng2025-09-29T14:30:45Zoai:sgc.anlis.gob.ar:123456789/2269Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-29 14:30:45.39Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"false
dc.title.none.fl_str_mv Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
title Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
spellingShingle Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
Duschak, Vilma G
Trypanosoma cruzi
Proteasas de Cisteína
Enfermedad de Chagas
title_short Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
title_full Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
title_fullStr Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
title_full_unstemmed Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
title_sort Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
dc.creator.none.fl_str_mv Duschak, Vilma G
Barboza, M
Garcia, G. A.
Lammel, Estela M.
Couto, Alicia S
Isola, E L D
author Duschak, Vilma G
author_facet Duschak, Vilma G
Barboza, M
Garcia, G. A.
Lammel, Estela M.
Couto, Alicia S
Isola, E L D
author_role author
author2 Barboza, M
Garcia, G. A.
Lammel, Estela M.
Couto, Alicia S
Isola, E L D
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Trypanosoma cruzi
Proteasas de Cisteína
Enfermedad de Chagas
topic Trypanosoma cruzi
Proteasas de Cisteína
Enfermedad de Chagas
dc.description.none.fl_txt_mv Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Barboza, M. Universidad Nacional de General San Martín. Instituto de Investigaciones Biotecnológicas–INTECH; Argentina.
Fil: Garcia, G. A. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Lammel, Estela M. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.
Fil: Couto, Alicia S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. CIHIDECAR; Argentina.
Fil: Isola, E. L. D. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Microbiología, Parasitología e Inmunología; Argentina.
With the aim to study proteinases released to the culture medium during Trypanosoma cruzi metacyclogenesis, the presence of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the important role of these enzymes in metacyclogenesis.
description Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
publishDate 2006
dc.date.none.fl_str_mv 2006-03
dc.type.none.fl_str_mv info:ar-repo/semantics/articulo
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 1469-8161
http://sgc.anlis.gob.ar/handle/123456789/2269
10.1017/S0031182005009030
identifier_str_mv 1469-8161
10.1017/S0031182005009030
url http://sgc.anlis.gob.ar/handle/123456789/2269
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Parasitology
dc.rights.none.fl_str_mv none
info:eu-repo/semantics/openAccess
rights_invalid_str_mv none
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Parasitology 2006;132(Pt 3):345-355
reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron:ANLIS
reponame_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
collection Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname_str Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron_str ANLIS
institution ANLIS
repository.name.fl_str_mv Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
repository.mail.fl_str_mv biblioteca@anlis.gov.ar
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