Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection

Autores
Soprano, Luciana L.; Parente, Juliana Elena; Landoni, Malena; Couto, Alicia S.; Duschak, Vilma G.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión enviada
Descripción
In this work, the presence of sulfated N-glycans was studied in a high-mannose-type glycoprotein of Trypanosoma cruzi with serinecarboxipeptidase (TcSCP) activity. The immune cross-reactivity between purified SCP and Cruzipain (Cz) was evidenced using rabbit sera specific for both glycoproteins. Taking advantage that SCP co-purifies with Cz from Concanavalin-A affinity columns, the Cz–SCP mixture was desulfated, ascribing the cross-reactivity to the presence of sulfate groups in both molecules. Therefore, knowing that Cz is a sulfated glycoprotein, with antigenic sulfated epitopes (sulfotopes), SCP was excised from SDS-PAGE and the N-glycosydic chains were analyzed by UV–MALDI–TOF-MS, confirming the presence of short-sulfated high-mannose-type oligosaccharidic chains. Besides, the presence of sulfotopes was analyzed in lysates of the different parasite stages demonstrating that a band with apparent molecular weight similar to SCP was highly recognized in trypomastigotes. In addition, SCP was confronted with sera of infected people with different degrees of cardiac dysfunction. Although most sera recognized it in different groups, no statistical association was found between sera antibodies specific for SCP and the severity of the disease. In summary, our findings demonstrate (1) the presence of sulfate groups in the N-glycosidic short chains of native TcSCP, (2) the existence of immune cross-reactivity between Cz and SCP, purified from epimastigotes, (3) the presence of common sulfotopes between both parasite glycoproteins, and (4) the enhanced presence of sulfotopes in trypomastigotes, probably involved in parasite–host relationship and/or infection. Interestingly, we show for the first time that SCP is a minor antigen recognized by most of chronic Chagas disease patient’s sera.
Materia
Ciencias Médicas y de la Salud
Trypanosoma cruzi
serinecarboxipeptidase
immune cross-reactivity
glycoprotein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
CIC Digital (CICBA)
Institución
Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
OAI Identificador
oai:digital.cic.gba.gob.ar:11746/8275

id CICBA_1162f76a8c42b99ee2195897e06b8aab
oai_identifier_str oai:digital.cic.gba.gob.ar:11746/8275
network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infectionSoprano, Luciana L.Parente, Juliana ElenaLandoni, MalenaCouto, Alicia S.Duschak, Vilma G.Ciencias Médicas y de la SaludTrypanosoma cruziserinecarboxipeptidaseimmune cross-reactivityglycoproteinIn this work, the presence of sulfated N-glycans was studied in a high-mannose-type glycoprotein of <em>Trypanosoma cruzi</em> with serinecarboxipeptidase (T<em>c</em>SCP) activity. The immune cross-reactivity between purified SCP and Cruzipain (Cz) was evidenced using rabbit sera specific for both glycoproteins. Taking advantage that SCP co-purifies with Cz from Concanavalin-A affinity columns, the Cz–SCP mixture was desulfated, ascribing the cross-reactivity to the presence of sulfate groups in both molecules. Therefore, knowing that Cz is a sulfated glycoprotein, with antigenic sulfated epitopes (sulfotopes), SCP was excised from SDS-PAGE and the N-glycosydic chains were analyzed by UV–MALDI–TOF-MS, confirming the presence of short-sulfated high-mannose-type oligosaccharidic chains. Besides, the presence of sulfotopes was analyzed in lysates of the different parasite stages demonstrating that a band with apparent molecular weight similar to SCP was highly recognized in trypomastigotes. In addition, SCP was confronted with sera of infected people with different degrees of cardiac dysfunction. Although most sera recognized it in different groups, no statistical association was found between sera antibodies specific for SCP and the severity of the disease. In summary, our findings demonstrate (1) the presence of sulfate groups in the N-glycosidic short chains of native T<em>c</em>SCP, (2) the existence of immune cross-reactivity between Cz and SCP, purified from epimastigotes, (3) the presence of common sulfotopes between both parasite glycoproteins, and (4) the enhanced presence of sulfotopes in trypomastigotes, probably involved in parasite–host relationship and/or infection. Interestingly, we show for the first time that SCP is a minor antigen recognized by most of chronic Chagas disease patient’s sera.2017-12-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/8275enginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00430-017-0529-7info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-09-29T13:40:02Zoai:digital.cic.gba.gob.ar:11746/8275Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-09-29 13:40:03.238CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
title Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
spellingShingle Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
Soprano, Luciana L.
Ciencias Médicas y de la Salud
Trypanosoma cruzi
serinecarboxipeptidase
immune cross-reactivity
glycoprotein
title_short Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
title_full Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
title_fullStr Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
title_full_unstemmed Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
title_sort Trypanosoma cruzi serinecarboxipeptidaseis a sufated glycoprotein and a minor antigen in human Chagas disease infection
dc.creator.none.fl_str_mv Soprano, Luciana L.
Parente, Juliana Elena
Landoni, Malena
Couto, Alicia S.
Duschak, Vilma G.
author Soprano, Luciana L.
author_facet Soprano, Luciana L.
Parente, Juliana Elena
Landoni, Malena
Couto, Alicia S.
Duschak, Vilma G.
author_role author
author2 Parente, Juliana Elena
Landoni, Malena
Couto, Alicia S.
Duschak, Vilma G.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Médicas y de la Salud
Trypanosoma cruzi
serinecarboxipeptidase
immune cross-reactivity
glycoprotein
topic Ciencias Médicas y de la Salud
Trypanosoma cruzi
serinecarboxipeptidase
immune cross-reactivity
glycoprotein
dc.description.none.fl_txt_mv In this work, the presence of sulfated N-glycans was studied in a high-mannose-type glycoprotein of <em>Trypanosoma cruzi</em> with serinecarboxipeptidase (T<em>c</em>SCP) activity. The immune cross-reactivity between purified SCP and Cruzipain (Cz) was evidenced using rabbit sera specific for both glycoproteins. Taking advantage that SCP co-purifies with Cz from Concanavalin-A affinity columns, the Cz–SCP mixture was desulfated, ascribing the cross-reactivity to the presence of sulfate groups in both molecules. Therefore, knowing that Cz is a sulfated glycoprotein, with antigenic sulfated epitopes (sulfotopes), SCP was excised from SDS-PAGE and the N-glycosydic chains were analyzed by UV–MALDI–TOF-MS, confirming the presence of short-sulfated high-mannose-type oligosaccharidic chains. Besides, the presence of sulfotopes was analyzed in lysates of the different parasite stages demonstrating that a band with apparent molecular weight similar to SCP was highly recognized in trypomastigotes. In addition, SCP was confronted with sera of infected people with different degrees of cardiac dysfunction. Although most sera recognized it in different groups, no statistical association was found between sera antibodies specific for SCP and the severity of the disease. In summary, our findings demonstrate (1) the presence of sulfate groups in the N-glycosidic short chains of native T<em>c</em>SCP, (2) the existence of immune cross-reactivity between Cz and SCP, purified from epimastigotes, (3) the presence of common sulfotopes between both parasite glycoproteins, and (4) the enhanced presence of sulfotopes in trypomastigotes, probably involved in parasite–host relationship and/or infection. Interestingly, we show for the first time that SCP is a minor antigen recognized by most of chronic Chagas disease patient’s sera.
description In this work, the presence of sulfated N-glycans was studied in a high-mannose-type glycoprotein of <em>Trypanosoma cruzi</em> with serinecarboxipeptidase (T<em>c</em>SCP) activity. The immune cross-reactivity between purified SCP and Cruzipain (Cz) was evidenced using rabbit sera specific for both glycoproteins. Taking advantage that SCP co-purifies with Cz from Concanavalin-A affinity columns, the Cz–SCP mixture was desulfated, ascribing the cross-reactivity to the presence of sulfate groups in both molecules. Therefore, knowing that Cz is a sulfated glycoprotein, with antigenic sulfated epitopes (sulfotopes), SCP was excised from SDS-PAGE and the N-glycosydic chains were analyzed by UV–MALDI–TOF-MS, confirming the presence of short-sulfated high-mannose-type oligosaccharidic chains. Besides, the presence of sulfotopes was analyzed in lysates of the different parasite stages demonstrating that a band with apparent molecular weight similar to SCP was highly recognized in trypomastigotes. In addition, SCP was confronted with sera of infected people with different degrees of cardiac dysfunction. Although most sera recognized it in different groups, no statistical association was found between sera antibodies specific for SCP and the severity of the disease. In summary, our findings demonstrate (1) the presence of sulfate groups in the N-glycosidic short chains of native T<em>c</em>SCP, (2) the existence of immune cross-reactivity between Cz and SCP, purified from epimastigotes, (3) the presence of common sulfotopes between both parasite glycoproteins, and (4) the enhanced presence of sulfotopes in trypomastigotes, probably involved in parasite–host relationship and/or infection. Interestingly, we show for the first time that SCP is a minor antigen recognized by most of chronic Chagas disease patient’s sera.
publishDate 2017
dc.date.none.fl_str_mv 2017-12-22
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/8275
url https://digital.cic.gba.gob.ar/handle/11746/8275
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s00430-017-0529-7
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:CIC Digital (CICBA)
instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron:CICBA
reponame_str CIC Digital (CICBA)
collection CIC Digital (CICBA)
instname_str Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron_str CICBA
institution CICBA
repository.name.fl_str_mv CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
repository.mail.fl_str_mv marisa.degiusti@sedici.unlp.edu.ar
_version_ 1844618596115808256
score 13.070432