Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection

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. Tak...

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Publicado: 2018
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008584_v207_n2_p117_Soprano
http://hdl.handle.net/20.500.12110/paper_03008584_v207_n2_p117_Soprano
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spelling paper:paper_03008584_v207_n2_p117_Soprano2023-06-08T15:27:33Z Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection Antigenicity Chagas’ disease Glycomics Serinecarboxypeptidase Sulfate groups Sulfotopes Trypanosoma cruzi concanavalin A cruzipain glycoprotein serine carboxipeptidase unclassified drug carboxypeptidase cysteine proteinase glycoprotein parasite antigen serine carboxypeptidase sulfate animal experiment antigen recognition Article Chagas disease controlled study cross reaction deglycosylation desulfurization enzyme activity epimastigote heart disease host parasite interaction human matrix assisted laser desorption ionization time of flight mass spectrometry molecular weight New Zealand White (rabbit) nonhuman polyacrylamide gel electrophoresis priority journal serum Trypanosoma cruzi trypomastigote ultraviolet spectroscopy animal Chagas disease chemistry enzymology immunology Leporidae mass spectrometry metabolism protein processing Trypanosoma cruzi Animals Antigens, Protozoan Carboxypeptidases Chagas Disease Cross Reactions Cysteine Endopeptidases Glycoproteins Humans Mass Spectrometry Protein Processing, Post-Translational Rabbits Sulfates Trypanosoma cruzi 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. © 2017, Springer-Verlag GmbH Germany, part of Springer Nature. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008584_v207_n2_p117_Soprano http://hdl.handle.net/20.500.12110/paper_03008584_v207_n2_p117_Soprano
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Antigenicity
Chagas’ disease
Glycomics
Serinecarboxypeptidase
Sulfate groups
Sulfotopes
Trypanosoma cruzi
concanavalin A
cruzipain
glycoprotein
serine carboxipeptidase
unclassified drug
carboxypeptidase
cysteine proteinase
glycoprotein
parasite antigen
serine carboxypeptidase
sulfate
animal experiment
antigen recognition
Article
Chagas disease
controlled study
cross reaction
deglycosylation
desulfurization
enzyme activity
epimastigote
heart disease
host parasite interaction
human
matrix assisted laser desorption ionization time of flight mass spectrometry
molecular weight
New Zealand White (rabbit)
nonhuman
polyacrylamide gel electrophoresis
priority journal
serum
Trypanosoma cruzi
trypomastigote
ultraviolet spectroscopy
animal
Chagas disease
chemistry
enzymology
immunology
Leporidae
mass spectrometry
metabolism
protein processing
Trypanosoma cruzi
Animals
Antigens, Protozoan
Carboxypeptidases
Chagas Disease
Cross Reactions
Cysteine Endopeptidases
Glycoproteins
Humans
Mass Spectrometry
Protein Processing, Post-Translational
Rabbits
Sulfates
Trypanosoma cruzi
spellingShingle Antigenicity
Chagas’ disease
Glycomics
Serinecarboxypeptidase
Sulfate groups
Sulfotopes
Trypanosoma cruzi
concanavalin A
cruzipain
glycoprotein
serine carboxipeptidase
unclassified drug
carboxypeptidase
cysteine proteinase
glycoprotein
parasite antigen
serine carboxypeptidase
sulfate
animal experiment
antigen recognition
Article
Chagas disease
controlled study
cross reaction
deglycosylation
desulfurization
enzyme activity
epimastigote
heart disease
host parasite interaction
human
matrix assisted laser desorption ionization time of flight mass spectrometry
molecular weight
New Zealand White (rabbit)
nonhuman
polyacrylamide gel electrophoresis
priority journal
serum
Trypanosoma cruzi
trypomastigote
ultraviolet spectroscopy
animal
Chagas disease
chemistry
enzymology
immunology
Leporidae
mass spectrometry
metabolism
protein processing
Trypanosoma cruzi
Animals
Antigens, Protozoan
Carboxypeptidases
Chagas Disease
Cross Reactions
Cysteine Endopeptidases
Glycoproteins
Humans
Mass Spectrometry
Protein Processing, Post-Translational
Rabbits
Sulfates
Trypanosoma cruzi
Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
topic_facet Antigenicity
Chagas’ disease
Glycomics
Serinecarboxypeptidase
Sulfate groups
Sulfotopes
Trypanosoma cruzi
concanavalin A
cruzipain
glycoprotein
serine carboxipeptidase
unclassified drug
carboxypeptidase
cysteine proteinase
glycoprotein
parasite antigen
serine carboxypeptidase
sulfate
animal experiment
antigen recognition
Article
Chagas disease
controlled study
cross reaction
deglycosylation
desulfurization
enzyme activity
epimastigote
heart disease
host parasite interaction
human
matrix assisted laser desorption ionization time of flight mass spectrometry
molecular weight
New Zealand White (rabbit)
nonhuman
polyacrylamide gel electrophoresis
priority journal
serum
Trypanosoma cruzi
trypomastigote
ultraviolet spectroscopy
animal
Chagas disease
chemistry
enzymology
immunology
Leporidae
mass spectrometry
metabolism
protein processing
Trypanosoma cruzi
Animals
Antigens, Protozoan
Carboxypeptidases
Chagas Disease
Cross Reactions
Cysteine Endopeptidases
Glycoproteins
Humans
Mass Spectrometry
Protein Processing, Post-Translational
Rabbits
Sulfates
Trypanosoma cruzi
description 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. © 2017, Springer-Verlag GmbH Germany, part of Springer Nature.
title Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
title_short Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
title_full Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
title_fullStr Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
title_full_unstemmed Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
title_sort trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human chagas disease infection
publishDate 2018
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008584_v207_n2_p117_Soprano
http://hdl.handle.net/20.500.12110/paper_03008584_v207_n2_p117_Soprano
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