A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

Autores
Vieira, Monica L.; D'Atri, Lina P.; Schattner, Mirta; Habarta, Alejandra Mariel; Barbosa, Angela S.; De Morais, Zenaide M.; Vasconcellos, Silvio A.; Abreu, Patricia A.E.; Gómez, Ricardo Martín; Nascimento, Ana L.T.O.
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.
Instituto de Biotecnologia y Biologia Molecular
Materia
Bioquímica
E-selectin
ICAM-1
Leptospira interrogans
Recombinant protein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/83440

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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cellsVieira, Monica L.D'Atri, Lina P.Schattner, MirtaHabarta, Alejandra MarielBarbosa, Angela S.De Morais, Zenaide M.Vasconcellos, Silvio A.Abreu, Patricia A.E.Gómez, Ricardo MartínNascimento, Ana L.T.O.BioquímicaE-selectinICAM-1Leptospira interrogansRecombinant proteinIt has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.Instituto de Biotecnologia y Biologia Molecular2007info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf172-180http://sedici.unlp.edu.ar/handle/10915/83440enginfo:eu-repo/semantics/altIdentifier/issn/0378-1097info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1574-6968.2007.00924.xinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:15:41Zoai:sedici.unlp.edu.ar:10915/83440Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:15:42.055SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
title A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
spellingShingle A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
Vieira, Monica L.
Bioquímica
E-selectin
ICAM-1
Leptospira interrogans
Recombinant protein
title_short A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
title_full A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
title_fullStr A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
title_full_unstemmed A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
title_sort A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells
dc.creator.none.fl_str_mv Vieira, Monica L.
D'Atri, Lina P.
Schattner, Mirta
Habarta, Alejandra Mariel
Barbosa, Angela S.
De Morais, Zenaide M.
Vasconcellos, Silvio A.
Abreu, Patricia A.E.
Gómez, Ricardo Martín
Nascimento, Ana L.T.O.
author Vieira, Monica L.
author_facet Vieira, Monica L.
D'Atri, Lina P.
Schattner, Mirta
Habarta, Alejandra Mariel
Barbosa, Angela S.
De Morais, Zenaide M.
Vasconcellos, Silvio A.
Abreu, Patricia A.E.
Gómez, Ricardo Martín
Nascimento, Ana L.T.O.
author_role author
author2 D'Atri, Lina P.
Schattner, Mirta
Habarta, Alejandra Mariel
Barbosa, Angela S.
De Morais, Zenaide M.
Vasconcellos, Silvio A.
Abreu, Patricia A.E.
Gómez, Ricardo Martín
Nascimento, Ana L.T.O.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
E-selectin
ICAM-1
Leptospira interrogans
Recombinant protein
topic Bioquímica
E-selectin
ICAM-1
Leptospira interrogans
Recombinant protein
dc.description.none.fl_txt_mv It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.
Instituto de Biotecnologia y Biologia Molecular
description It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.
publishDate 2007
dc.date.none.fl_str_mv 2007
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/83440
url http://sedici.unlp.edu.ar/handle/10915/83440
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0378-1097
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1574-6968.2007.00924.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
172-180
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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