Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/32482 http://dx.doi.org/10.1074/jbc.M109.096305 |
Resumo: | Upon activation, cytotoxic CD8(+) T lymphocytes are desialylated exposing beta-galactose residues in a physiological change that enhances their effector activity and that can be monitored on the basis of increased binding of the lectin peanut agglutinin. Herein, we investigated the impact of sialylation mediated by trans-sialidase, a specific and unique Trypanosoma transglycosylase for sialic acid, on CD8(+) T cell response of mice infected with T. cruzi. Our data demonstrate that T. cruzi uses its trans-sialidase enzyme to resialylate the CD8(+) T cell surface, thereby dampening antigen-specific CD8(+) T cell response that might favor its own persistence in the mammalian host. Binding of the monoclonal antibody S7, which recognizes sialic acid-containing epitopes on the 115-kDa isoform of CD43, was augmented on CD8(+) T cells from ST3Gal-I-deficient infected mice, indicating that CD43 is one sialic acid acceptor for trans-sialidase activity on the CD8(+) T cell surface. the cytotoxic activity of antigen-experienced CD8(+) T cells against the immunodominant trans-sialidase synthetic peptide IYNVGQVSI was decreased following active trans-sialidase-mediated resialylation in vitro and in vivo. Inhibition of the parasite's native trans-sialidase activity during infection strongly decreased CD8(+) T cell sialylation, reverting it to the glycosylation status expected in the absence of parasite manipulation increasing mouse survival. Taken together, these results demonstrate, for the first time, that T. cruzi subverts sialylation to attenuate CD8(+) T cell interactions with peptide-major histocompatibility complex class I complexes. CD8(+) T cell resialylation may represent a sophisticated strategy to ensure lifetime host parasitism. |
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Freire-de-Lima, LeonardoAlisson-Silva, FredericoCarvalho, Sebastiao T.Takiya, Christina M.Rodrigues, Mauricio Martins [UNIFESP]DosReis, George A.Mendonca-Previato, LuciaPreviato, Jose O.Todeschini, Adriane R.Universidade Federal do Rio de Janeiro (UFRJ)Universidade Federal de São Paulo (UNIFESP)2016-01-24T13:59:36Z2016-01-24T13:59:36Z2010-04-30Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 285, n. 18, p. 13388-13396, 2010.0021-9258http://repositorio.unifesp.br/handle/11600/32482http://dx.doi.org/10.1074/jbc.M109.09630510.1074/jbc.M109.096305WOS:000276987700010Upon activation, cytotoxic CD8(+) T lymphocytes are desialylated exposing beta-galactose residues in a physiological change that enhances their effector activity and that can be monitored on the basis of increased binding of the lectin peanut agglutinin. Herein, we investigated the impact of sialylation mediated by trans-sialidase, a specific and unique Trypanosoma transglycosylase for sialic acid, on CD8(+) T cell response of mice infected with T. cruzi. Our data demonstrate that T. cruzi uses its trans-sialidase enzyme to resialylate the CD8(+) T cell surface, thereby dampening antigen-specific CD8(+) T cell response that might favor its own persistence in the mammalian host. Binding of the monoclonal antibody S7, which recognizes sialic acid-containing epitopes on the 115-kDa isoform of CD43, was augmented on CD8(+) T cells from ST3Gal-I-deficient infected mice, indicating that CD43 is one sialic acid acceptor for trans-sialidase activity on the CD8(+) T cell surface. the cytotoxic activity of antigen-experienced CD8(+) T cells against the immunodominant trans-sialidase synthetic peptide IYNVGQVSI was decreased following active trans-sialidase-mediated resialylation in vitro and in vivo. Inhibition of the parasite's native trans-sialidase activity during infection strongly decreased CD8(+) T cell sialylation, reverting it to the glycosylation status expected in the absence of parasite manipulation increasing mouse survival. Taken together, these results demonstrate, for the first time, that T. cruzi subverts sialylation to attenuate CD8(+) T cell interactions with peptide-major histocompatibility complex class I complexes. CD8(+) T cell resialylation may represent a sophisticated strategy to ensure lifetime host parasitism.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)National Institute for Science and Technology in VaccinesUniv Fed Rio de Janeiro, Inst Biofis Carlos Chagas Filho, Ilha Fundao, BR-21949900 Rio de Janeiro, BrazilUniv Fed Rio de Janeiro, Inst Ciencias Biomed, Ctr Ciencias Saude, Ilha Fundao, BR-21949900 Rio de Janeiro, BrazilUniversidade Federal de São Paulo, Ctr Interdisciplinar Terapia Gen, BR-04044010 São Paulo, BrazilUniversidade Federal de São Paulo, Ctr Interdisciplinar Terapia Gen, BR-04044010 São Paulo, BrazilWeb of Science13388-13396engAmer Soc Biochemistry Molecular Biology IncJournal of Biological ChemistryTrypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responsesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/324822022-07-08 10:45:09.733metadata only accessoai:repositorio.unifesp.br:11600/32482Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:19:48.883765Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
title |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
spellingShingle |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses Freire-de-Lima, Leonardo |
title_short |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
title_full |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
title_fullStr |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
title_full_unstemmed |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
title_sort |
Trypanosoma cruzi Subverts Host Cell Sialylation and May Compromise Antigen-specific CD8(+) T Cell Responses |
author |
Freire-de-Lima, Leonardo |
author_facet |
Freire-de-Lima, Leonardo Alisson-Silva, Frederico Carvalho, Sebastiao T. Takiya, Christina M. Rodrigues, Mauricio Martins [UNIFESP] DosReis, George A. Mendonca-Previato, Lucia Previato, Jose O. Todeschini, Adriane R. |
author_role |
author |
author2 |
Alisson-Silva, Frederico Carvalho, Sebastiao T. Takiya, Christina M. Rodrigues, Mauricio Martins [UNIFESP] DosReis, George A. Mendonca-Previato, Lucia Previato, Jose O. Todeschini, Adriane R. |
author2_role |
author author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal do Rio de Janeiro (UFRJ) Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Freire-de-Lima, Leonardo Alisson-Silva, Frederico Carvalho, Sebastiao T. Takiya, Christina M. Rodrigues, Mauricio Martins [UNIFESP] DosReis, George A. Mendonca-Previato, Lucia Previato, Jose O. Todeschini, Adriane R. |
description |
Upon activation, cytotoxic CD8(+) T lymphocytes are desialylated exposing beta-galactose residues in a physiological change that enhances their effector activity and that can be monitored on the basis of increased binding of the lectin peanut agglutinin. Herein, we investigated the impact of sialylation mediated by trans-sialidase, a specific and unique Trypanosoma transglycosylase for sialic acid, on CD8(+) T cell response of mice infected with T. cruzi. Our data demonstrate that T. cruzi uses its trans-sialidase enzyme to resialylate the CD8(+) T cell surface, thereby dampening antigen-specific CD8(+) T cell response that might favor its own persistence in the mammalian host. Binding of the monoclonal antibody S7, which recognizes sialic acid-containing epitopes on the 115-kDa isoform of CD43, was augmented on CD8(+) T cells from ST3Gal-I-deficient infected mice, indicating that CD43 is one sialic acid acceptor for trans-sialidase activity on the CD8(+) T cell surface. the cytotoxic activity of antigen-experienced CD8(+) T cells against the immunodominant trans-sialidase synthetic peptide IYNVGQVSI was decreased following active trans-sialidase-mediated resialylation in vitro and in vivo. Inhibition of the parasite's native trans-sialidase activity during infection strongly decreased CD8(+) T cell sialylation, reverting it to the glycosylation status expected in the absence of parasite manipulation increasing mouse survival. Taken together, these results demonstrate, for the first time, that T. cruzi subverts sialylation to attenuate CD8(+) T cell interactions with peptide-major histocompatibility complex class I complexes. CD8(+) T cell resialylation may represent a sophisticated strategy to ensure lifetime host parasitism. |
publishDate |
2010 |
dc.date.issued.fl_str_mv |
2010-04-30 |
dc.date.accessioned.fl_str_mv |
2016-01-24T13:59:36Z |
dc.date.available.fl_str_mv |
2016-01-24T13:59:36Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 285, n. 18, p. 13388-13396, 2010. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/32482 http://dx.doi.org/10.1074/jbc.M109.096305 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.M109.096305 |
dc.identifier.wos.none.fl_str_mv |
WOS:000276987700010 |
identifier_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 285, n. 18, p. 13388-13396, 2010. 0021-9258 10.1074/jbc.M109.096305 WOS:000276987700010 |
url |
http://repositorio.unifesp.br/handle/11600/32482 http://dx.doi.org/10.1074/jbc.M109.096305 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Journal of Biological Chemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
13388-13396 |
dc.publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
publisher.none.fl_str_mv |
Amer Soc Biochemistry Molecular Biology Inc |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1783460277269823488 |