Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae

Photobacterium damselae subsp. damselae (Pdd) is an emerging pathogen of marine animals that sometimes causes serious infections in humans. Two related pore forming toxins, phobalysins P and C, and damselysin, a phospholipase D, confer strong virulence of Pdd in mice. Because infections by Pdd are t...

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Autores: Von Hoven, Gisela, Neukirch, Claudia, Meyenburg, Martina, Schmidt, Sabine, Vences Lorenzo, Ana, Rodríguez Osorio, Carlos, Husmann, Matthias, Rivas Fontenla, Amable José
Tipo de recurso: artículo
Fecha de publicación:2018
País:España
Institución:Universidad de Santiago de Compostela (USC)
Repositorio:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
Idioma:inglés
OAI Identifier:oai:minerva.usc.gal:10347/22628
Acceso en línea:http://hdl.handle.net/10347/22628
Access Level:acceso abierto
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spelling Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselaeVon Hoven, GiselaNeukirch, ClaudiaMeyenburg, MartinaSchmidt, SabineVences Lorenzo, AnaRodríguez Osorio, CarlosHusmann, MatthiasRivas Fontenla, Amable JoséPhotobacterium damselae subsp. damselae (Pdd) is an emerging pathogen of marine animals that sometimes causes serious infections in humans. Two related pore forming toxins, phobalysins P and C, and damselysin, a phospholipase D, confer strong virulence of Pdd in mice. Because infections by Pdd are typically caused following exposure of wounds to sea water we investigated how salinity impacts toxin activity, swimming, and association of Pdd with epithelial cells. These activities were low when bacteria were pre-cultured in media with 3.5% NaCl, the global average salinity of sea water. In contrast, lower salinity increased swimming of wild type Pdd peaking at 2% NaCl, hemolysis, and association with epithelial cells peaking at 1–1.5%. Previously, we have found that hemolysin genes enhance the association of Pdd with epithelial cells, but the underlying mechanisms have remained ill-defined. We here searched for potential links between hemolysin-production, chemotaxis and association of Pdd with target cells at varying salt concentrations. Unexpectedly, disruption of chemotaxis regulator cheA not only affected bacterial swimming and association with epithelial cells at intermediate to low salinity, but also reduced the production of plasmid-encoded phobalysin (PhlyP). The results thus reveal unforeseen links between chemotaxis regulators, a pore forming toxin and the association of a marine bacterium with target cellsFrontiers MediaUniversidade de Santiago de Compostela. Departamento de Microbioloxía e ParasitoloxíaUniversidade de Santiago de Compostela. Instituto de Acuicultura20182018-01-0120182018-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10347/22628reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostelainstname:Universidad de Santiago de Compostela (USC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Copyright © 2018 von Hoven, Neukirch, Meyenburg, Schmidt, Vences, Osorio, Husmann and Rivas. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these termshttps://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:minerva.usc.gal:10347/226282026-06-15T12:47:27Z
dc.title.none.fl_str_mv Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
title Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
spellingShingle Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
Von Hoven, Gisela
title_short Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
title_full Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
title_fullStr Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
title_full_unstemmed Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
title_sort Cytotoxin- and chemotaxis-genes cooperate to promote adhesion of photobacterium damselae subsp. damselae
dc.creator.none.fl_str_mv Von Hoven, Gisela
Neukirch, Claudia
Meyenburg, Martina
Schmidt, Sabine
Vences Lorenzo, Ana
Rodríguez Osorio, Carlos
Husmann, Matthias
Rivas Fontenla, Amable José
author Von Hoven, Gisela
author_facet Von Hoven, Gisela
Neukirch, Claudia
Meyenburg, Martina
Schmidt, Sabine
Vences Lorenzo, Ana
Rodríguez Osorio, Carlos
Husmann, Matthias
Rivas Fontenla, Amable José
author_role author
author2 Neukirch, Claudia
Meyenburg, Martina
Schmidt, Sabine
Vences Lorenzo, Ana
Rodríguez Osorio, Carlos
Husmann, Matthias
Rivas Fontenla, Amable José
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de Santiago de Compostela. Departamento de Microbioloxía e Parasitoloxía
Universidade de Santiago de Compostela. Instituto de Acuicultura

description Photobacterium damselae subsp. damselae (Pdd) is an emerging pathogen of marine animals that sometimes causes serious infections in humans. Two related pore forming toxins, phobalysins P and C, and damselysin, a phospholipase D, confer strong virulence of Pdd in mice. Because infections by Pdd are typically caused following exposure of wounds to sea water we investigated how salinity impacts toxin activity, swimming, and association of Pdd with epithelial cells. These activities were low when bacteria were pre-cultured in media with 3.5% NaCl, the global average salinity of sea water. In contrast, lower salinity increased swimming of wild type Pdd peaking at 2% NaCl, hemolysis, and association with epithelial cells peaking at 1–1.5%. Previously, we have found that hemolysin genes enhance the association of Pdd with epithelial cells, but the underlying mechanisms have remained ill-defined. We here searched for potential links between hemolysin-production, chemotaxis and association of Pdd with target cells at varying salt concentrations. Unexpectedly, disruption of chemotaxis regulator cheA not only affected bacterial swimming and association with epithelial cells at intermediate to low salinity, but also reduced the production of plasmid-encoded phobalysin (PhlyP). The results thus reveal unforeseen links between chemotaxis regulators, a pore forming toxin and the association of a marine bacterium with target cells
publishDate 2018
dc.date.none.fl_str_mv 2018
2018-01-01
2018
2018-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10347/22628
url http://hdl.handle.net/10347/22628
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname:Universidad de Santiago de Compostela (USC)
instname_str Universidad de Santiago de Compostela (USC)
reponame_str Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
collection Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
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repository.mail.fl_str_mv
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