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Abstract:

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.

Registro:

Documento: Artículo
Título:Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
Autor:Soprano, L.L.; Parente, J.E.; Landoni, M.; Couto, A.S.; Duschak, V.G.
Filiación:Area de Bioquímica de Proteínas y Glicobiología de Parásitos, Consejo Nacional de Investigaciones Científicas y Tecnicas (CONICET), Departamento de Investigación, Instituto Nacional de Parasitología “Dr. Mario Fatala Chaben”, ANLIS-Malbrán, Ministerio de Salud de la Nación, CONICET, Av. Paseo Colon 568 (1063), Buenos Aires, Argentina
Centro de Investigación en Hidratos de Carbono (CIHIDECAR), Departamento de Química Orgánica-Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Intendente Güiraldes 2160, Buenos Aires, C1428GA, Argentina
Palabras clave: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
Año:2018
Volumen:207
Número:2
Página de inicio:117
Página de fin:128
DOI: http://dx.doi.org/10.1007/s00430-017-0529-7
Título revista:Medical Microbiology and Immunology
Título revista abreviado:Med. Microbiol. Immunol.
ISSN:03008584
CODEN:MMIYA
CAS:concanavalin A, 11028-71-0; cruzipain; carboxypeptidase, 9031-98-5; cysteine proteinase, 37353-41-6; mucosa associated lymphoid tissue lymphoma translocation protein 1; serine carboxypeptidase, 11104-54-4; sulfate, 14808-79-8; Antigens, Protozoan; Carboxypeptidases; cruzipain; Cysteine Endopeptidases; Glycoproteins; serine carboxypeptidase; Sulfates
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008584_v207_n2_p117_Soprano

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Citas:

---------- APA ----------
Soprano, L.L., Parente, J.E., Landoni, M., Couto, A.S. & Duschak, V.G. (2018) . Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection. Medical Microbiology and Immunology, 207(2), 117-128.
http://dx.doi.org/10.1007/s00430-017-0529-7
---------- CHICAGO ----------
Soprano, L.L., Parente, J.E., Landoni, M., Couto, A.S., Duschak, V.G. "Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection" . Medical Microbiology and Immunology 207, no. 2 (2018) : 117-128.
http://dx.doi.org/10.1007/s00430-017-0529-7
---------- MLA ----------
Soprano, L.L., Parente, J.E., Landoni, M., Couto, A.S., Duschak, V.G. "Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection" . Medical Microbiology and Immunology, vol. 207, no. 2, 2018, pp. 117-128.
http://dx.doi.org/10.1007/s00430-017-0529-7
---------- VANCOUVER ----------
Soprano, L.L., Parente, J.E., Landoni, M., Couto, A.S., Duschak, V.G. Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection. Med. Microbiol. Immunol. 2018;207(2):117-128.
http://dx.doi.org/10.1007/s00430-017-0529-7