Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/26560 http://dx.doi.org/10.1074/jbc.M011474200 |
Resumo: | The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/transsialidase supergene family. A member of this family, Tc85-11, with adhesive properties to laminin and cell surfaces was recently cloned. in this report, the Tc85-11 domain for cell binding and its corresponding receptor on epithelial cell LLC-MK2 are described. Using synthetic peptides corresponding to the Tc85-11 carboxyl-terminal segment, we show that the mammalian cell-binding domain colocalizes to the most conserved motif of the trypanosome gp85/trans-sialidase supergene family (VTVXNVFLYNR), Even though Tc85-11 binds to laminin, the 19-residue cell-binding peptide (peptide J) does not contain the laminin-binding site, because it does not bind to laminin or inhibit cell binding to this glycoprotein, the host cell receptor for the peptide was characterized as cytokeratin 18, Addition of anti-cytokeratin antibodies to the culture medium significantly inhibited the infection of epithelial cells by T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one for cytokeratin 18, that allow the parasite to overcome the barriers imposed by cell membranes, extracellular matrices, and basal laminae to reach the definitive host cell. This is the first description of a direct interaction between cytokeratin and a protozoan parasite. |
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Magdesian, M. H.Giordano, R.Ulrich, Alexander Henning [UNIFESP]Juliano, Maria Aparecida [UNIFESP]Juliano, Luiz [UNIFESP]Schumacher, R. I.Colli, W.Alves, MJMUniversidade de São Paulo (USP)Universidade Federal de São Paulo (UNIFESP)2016-01-24T12:31:24Z2016-01-24T12:31:24Z2001-06-01Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 276, n. 22, p. 19382-19389, 2001.0021-9258http://repositorio.unifesp.br/handle/11600/26560http://dx.doi.org/10.1074/jbc.M01147420010.1074/jbc.M011474200WOS:000169091000099The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/transsialidase supergene family. A member of this family, Tc85-11, with adhesive properties to laminin and cell surfaces was recently cloned. in this report, the Tc85-11 domain for cell binding and its corresponding receptor on epithelial cell LLC-MK2 are described. Using synthetic peptides corresponding to the Tc85-11 carboxyl-terminal segment, we show that the mammalian cell-binding domain colocalizes to the most conserved motif of the trypanosome gp85/trans-sialidase supergene family (VTVXNVFLYNR), Even though Tc85-11 binds to laminin, the 19-residue cell-binding peptide (peptide J) does not contain the laminin-binding site, because it does not bind to laminin or inhibit cell binding to this glycoprotein, the host cell receptor for the peptide was characterized as cytokeratin 18, Addition of anti-cytokeratin antibodies to the culture medium significantly inhibited the infection of epithelial cells by T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one for cytokeratin 18, that allow the parasite to overcome the barriers imposed by cell membranes, extracellular matrices, and basal laminae to reach the definitive host cell. This is the first description of a direct interaction between cytokeratin and a protozoan parasite.Univ São Paulo, Inst Quim, Dept Bioquim, BR-05513970 São Paulo, BrazilUniversidade Federal de São Paulo, BR-04023900 São Paulo, BrazilUniversidade Federal de São Paulo, EPM, BR-04023900 São Paulo, BrazilWeb of Science19382-19389engAmer Soc Biochemistry Molecular Biology IncJournal of Biological ChemistryInfection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptorinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/265602022-07-08 10:40:20.491metadata only accessoai:repositorio.unifesp.br:11600/26560Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:19:20.834866Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
title |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
spellingShingle |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor Magdesian, M. H. |
title_short |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
title_full |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
title_fullStr |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
title_full_unstemmed |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
title_sort |
Infection by Trypanosoma cruzi - Identification of a parasite ligand and its host cell receptor |
author |
Magdesian, M. H. |
author_facet |
Magdesian, M. H. Giordano, R. Ulrich, Alexander Henning [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Juliano, Luiz [UNIFESP] Schumacher, R. I. Colli, W. Alves, MJM |
author_role |
author |
author2 |
Giordano, R. Ulrich, Alexander Henning [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Juliano, Luiz [UNIFESP] Schumacher, R. I. Colli, W. Alves, MJM |
author2_role |
author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Magdesian, M. H. Giordano, R. Ulrich, Alexander Henning [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Juliano, Luiz [UNIFESP] Schumacher, R. I. Colli, W. Alves, MJM |
description |
The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/transsialidase supergene family. A member of this family, Tc85-11, with adhesive properties to laminin and cell surfaces was recently cloned. in this report, the Tc85-11 domain for cell binding and its corresponding receptor on epithelial cell LLC-MK2 are described. Using synthetic peptides corresponding to the Tc85-11 carboxyl-terminal segment, we show that the mammalian cell-binding domain colocalizes to the most conserved motif of the trypanosome gp85/trans-sialidase supergene family (VTVXNVFLYNR), Even though Tc85-11 binds to laminin, the 19-residue cell-binding peptide (peptide J) does not contain the laminin-binding site, because it does not bind to laminin or inhibit cell binding to this glycoprotein, the host cell receptor for the peptide was characterized as cytokeratin 18, Addition of anti-cytokeratin antibodies to the culture medium significantly inhibited the infection of epithelial cells by T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one for cytokeratin 18, that allow the parasite to overcome the barriers imposed by cell membranes, extracellular matrices, and basal laminae to reach the definitive host cell. This is the first description of a direct interaction between cytokeratin and a protozoan parasite. |
publishDate |
2001 |
dc.date.issued.fl_str_mv |
2001-06-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T12:31:24Z |
dc.date.available.fl_str_mv |
2016-01-24T12:31:24Z |
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. 276, n. 22, p. 19382-19389, 2001. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/26560 http://dx.doi.org/10.1074/jbc.M011474200 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.M011474200 |
dc.identifier.wos.none.fl_str_mv |
WOS:000169091000099 |
identifier_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 276, n. 22, p. 19382-19389, 2001. 0021-9258 10.1074/jbc.M011474200 WOS:000169091000099 |
url |
http://repositorio.unifesp.br/handle/11600/26560 http://dx.doi.org/10.1074/jbc.M011474200 |
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 |
19382-19389 |
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 |
|
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1783460276498071552 |