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
- Institución
- Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
- OAI Identificador
- oai:sgc.anlis.gob.ar:123456789/2269
Ver los metadatos del registro completo
id |
SGCANLIS_1aed1fc08bad1c237f092da37b9d309f |
---|---|
oai_identifier_str |
oai:sgc.anlis.gob.ar:123456789/2269 |
network_acronym_str |
SGCANLIS |
repository_id_str |
a |
network_name_str |
Sistema de Gestión del Conocimiento ANLIS MALBRÁN |
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 |
_version_ |
1844621859928145920 |
score |
12.559606 |