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dc.contributor.author
Rico-Pérez, Gadea
dc.contributor.author
Pezza, Alejandro
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Pucciarelli, M. Graciela
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de Pedro, Miguel A.
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Soncini, Fernando Carlos
dc.contributor.author
García del Portillo, Francisco
dc.date.available
2018-07-17T19:38:39Z
dc.date.issued
2016-02
dc.identifier.citation
Rico-Pérez, Gadea; Pezza, Alejandro; Pucciarelli, M. Graciela; de Pedro, Miguel A.; Soncini, Fernando Carlos; et al.; A novel peptidoglycan D,L-endopeptidase induced by Salmonella inside eukaryotic cells contributes to virulence; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 99; 3; 2-2016; 546-556
dc.identifier.issn
0950-382X
dc.identifier.uri
http://hdl.handle.net/11336/52497
dc.description.abstract
Bacteria remodel peptidoglycan structure in response to environmental changes. Many enzymes are involved in peptidoglycan metabolism; however, little is known about their responsiveness in a defined environment or the modes they assist bacteria to adapt to new niches. Here, we focused in peptidoglycan enzymes that intracellular bacterial pathogens use inside eukaryotic cells. We identified a peptidoglycan enzyme induced by Salmonella enterica serovar Typhimurium in fibroblasts and epithelial cells. This enzyme, which shows γ-D-glutamyl-meso-diaminopimelic acid D,L-endopeptidase activity, is also produced by the pathogen in media with limited nutrients and in resting conditions. The enzyme, termed EcgA for endopeptidase responding to cessation of growth', is encoded in a S. Typhimurium genomic island absent in Escherichia coli. EcgA production is strictly dependent on the virulence regulator PhoP in extra- and intracellular environments. Consistent to this regulation, a mutant lacking EcgA is attenuated in the mouse typhoid model. These findings suggest that specialised peptidoglycan enzymes, such as EcgA, might facilitate Salmonella adaptation to the intracellular lifestyle. Moreover, they indicate that readjustment of peptidoglycan metabolism inside the eukaryotic cell is essential for host colonisation. Many enzymes direct peptidoglycan metabolism but little it is known about their regulation.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Salmonella
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Host Colonisation
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Peptidoglycan Metabolism
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Phop-Regulated
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
A novel peptidoglycan D,L-endopeptidase induced by Salmonella inside eukaryotic cells contributes to virulence
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-07-17T13:56:11Z
dc.journal.volume
99
dc.journal.number
3
dc.journal.pagination
546-556
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Rico-Pérez, Gadea. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Pezza, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Pucciarelli, M. Graciela. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: de Pedro, Miguel A.. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Soncini, Fernando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: García del Portillo, Francisco. Consejo Superior de Investigaciones Científicas; España
dc.journal.title
Molecular Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1111/mmi.13248
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info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/mmi.13248