High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans

Autores
King, Amy M.; Prêtre, Gabriela; Bartpho, Thanatchaporn; Sermswan, Rasana W.; Toma, Claudia; Suzuki, Toshihiko; Eshghi, Azad; Picardeau, Mathieu; Adler, Ben; Murray, Gerald L.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis and further elucidation of the mechanisms involved would therefore aid in vaccine development and prevention of infection. HtpG (High temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90, and is important in the stress response of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that HtpG of L. interrogans is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, nor altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor, and one of only a very small number identified to date.
Fil: King, Amy M.. Monash University; Australia
Fil: Prêtre, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina. Institut Pasteur de Paris.; Francia
Fil: Bartpho, Thanatchaporn. Khon Kaen University; Tailandia
Fil: Sermswan, Rasana W.. Khon Kaen University; Tailandia
Fil: Toma, Claudia. University of the Ryukyus; Japón
Fil: Suzuki, Toshihiko. University of the Ryukyus; Japón
Fil: Eshghi, Azad. Institut Pasteur de Paris.; Francia
Fil: Picardeau, Mathieu. Institut Pasteur de Paris.; Francia
Fil: Adler, Ben. Monash University; Australia
Fil: Murray, Gerald L.. Monash University; Australia
Materia
LEPTOSPIRA
HTPG
VIRULENCE
HSP90
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/102212
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/102212
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogansKing, Amy M.Prêtre, GabrielaBartpho, ThanatchapornSermswan, Rasana W.Toma, ClaudiaSuzuki, ToshihikoEshghi, AzadPicardeau, MathieuAdler, BenMurray, Gerald L.LEPTOSPIRAHTPGVIRULENCEHSP90https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis and further elucidation of the mechanisms involved would therefore aid in vaccine development and prevention of infection. HtpG (High temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90, and is important in the stress response of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that HtpG of L. interrogans is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, nor altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor, and one of only a very small number identified to date.Fil: King, Amy M.. Monash University; AustraliaFil: Prêtre, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina. Institut Pasteur de Paris.; FranciaFil: Bartpho, Thanatchaporn. Khon Kaen University; TailandiaFil: Sermswan, Rasana W.. Khon Kaen University; TailandiaFil: Toma, Claudia. University of the Ryukyus; JapónFil: Suzuki, Toshihiko. University of the Ryukyus; JapónFil: Eshghi, Azad. Institut Pasteur de Paris.; FranciaFil: Picardeau, Mathieu. Institut Pasteur de Paris.; FranciaFil: Adler, Ben. Monash University; AustraliaFil: Murray, Gerald L.. Monash University; AustraliaAmerican Society for Microbiology2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102212King, Amy M.; Prêtre, Gabriela; Bartpho, Thanatchaporn; Sermswan, Rasana W.; Toma, Claudia; et al.; High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans; American Society for Microbiology; Infection and Immunity; 82; 3; 3-2014; 1123-11310019-9567CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://iai.asm.org/content/early/2013/12/23/IAI.01546-13.longinfo:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.01546-13info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:41:30Zoai:ri.conicet.gov.ar:11336/102212instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:41:31.191CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
title High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
spellingShingle High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
King, Amy M.
LEPTOSPIRA
HTPG
VIRULENCE
HSP90
title_short High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
title_full High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
title_fullStr High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
title_full_unstemmed High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
title_sort High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans
dc.creator.none.fl_str_mv King, Amy M.
Prêtre, Gabriela
Bartpho, Thanatchaporn
Sermswan, Rasana W.
Toma, Claudia
Suzuki, Toshihiko
Eshghi, Azad
Picardeau, Mathieu
Adler, Ben
Murray, Gerald L.
author King, Amy M.
author_facet King, Amy M.
Prêtre, Gabriela
Bartpho, Thanatchaporn
Sermswan, Rasana W.
Toma, Claudia
Suzuki, Toshihiko
Eshghi, Azad
Picardeau, Mathieu
Adler, Ben
Murray, Gerald L.
author_role author
author2 Prêtre, Gabriela
Bartpho, Thanatchaporn
Sermswan, Rasana W.
Toma, Claudia
Suzuki, Toshihiko
Eshghi, Azad
Picardeau, Mathieu
Adler, Ben
Murray, Gerald L.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv LEPTOSPIRA
HTPG
VIRULENCE
HSP90
topic LEPTOSPIRA
HTPG
VIRULENCE
HSP90
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis and further elucidation of the mechanisms involved would therefore aid in vaccine development and prevention of infection. HtpG (High temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90, and is important in the stress response of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that HtpG of L. interrogans is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, nor altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor, and one of only a very small number identified to date.
Fil: King, Amy M.. Monash University; Australia
Fil: Prêtre, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina. Institut Pasteur de Paris.; Francia
Fil: Bartpho, Thanatchaporn. Khon Kaen University; Tailandia
Fil: Sermswan, Rasana W.. Khon Kaen University; Tailandia
Fil: Toma, Claudia. University of the Ryukyus; Japón
Fil: Suzuki, Toshihiko. University of the Ryukyus; Japón
Fil: Eshghi, Azad. Institut Pasteur de Paris.; Francia
Fil: Picardeau, Mathieu. Institut Pasteur de Paris.; Francia
Fil: Adler, Ben. Monash University; Australia
Fil: Murray, Gerald L.. Monash University; Australia
description Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis and further elucidation of the mechanisms involved would therefore aid in vaccine development and prevention of infection. HtpG (High temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90, and is important in the stress response of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that HtpG of L. interrogans is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, nor altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor, and one of only a very small number identified to date.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/102212
King, Amy M.; Prêtre, Gabriela; Bartpho, Thanatchaporn; Sermswan, Rasana W.; Toma, Claudia; et al.; High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans; American Society for Microbiology; Infection and Immunity; 82; 3; 3-2014; 1123-1131
0019-9567
CONICET Digital
CONICET
url http://hdl.handle.net/11336/102212
identifier_str_mv King, Amy M.; Prêtre, Gabriela; Bartpho, Thanatchaporn; Sermswan, Rasana W.; Toma, Claudia; et al.; High-Temperature Protein G Is an Essential Virulence Factor of Leptospira interrogans; American Society for Microbiology; Infection and Immunity; 82; 3; 3-2014; 1123-1131
0019-9567
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://iai.asm.org/content/early/2013/12/23/IAI.01546-13.long
info:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.01546-13
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846082912452083712
score 13.22299

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