umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Control of Bacterial Virulence through the Peptide Signature of the Habitat
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Show others and affiliations
2019 (English)In: Cell reports, ISSN 2211-1247, E-ISSN 2211-1247, Vol. 26, no 7, p. 1815-1827Article in journal (Refereed) Published
Abstract [en]

To optimize fitness, pathogens selectively activate their virulence program upon host entry. Here, we report that the facultative intracellular bacterium Listeria monocytogenes exploits exogenous oligopeptides, a ubiquitous organic N source, to sense the environment and control the activity of its virulence transcriptional activator, PrfA. Using a genetic screen in adsorbent- treated ( PrfA-inducing) medium, we found that PrfA is functionally regulated by the balance between activating and inhibitory nutritional peptides scavenged via the Opp transport system. Activating peptides provide essential cysteine precursor for the PrfA-inducing cofactor glutathione ( GSH). Non-cysteine-containing peptides cause promiscuous PrfA inhibition. Biophysical and co-crystallization studies reveal that peptides inhibit PrfA through steric blockade of the GSH binding site, a regulation mechanism directly linking bacterial virulence and metabolism. L. monocytogenes mutant analysis in macrophages and our functional data support a model in which changes in the balance of antagonistic Oppimported oligopeptides promote PrfA induction intra-cellularly and PrfA repression outside the host.

Place, publisher, year, edition, pages
Elsevier, 2019. Vol. 26, no 7, p. 1815-1827
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-156873DOI: 10.1016/j.celrep.2019.01.073ISI: 000458403600013PubMedID: 30759392OAI: oai:DiVA.org:umu-156873DiVA, id: diva2:1295481
Available from: 2019-03-11 Created: 2019-03-11 Last updated: 2019-03-11Bibliographically approved

Open Access in DiVA

fulltext(8704 kB)53 downloads
File information
File name FULLTEXT01.pdfFile size 8704 kBChecksum SHA-512
23cfcfc91df92668bdfb19f9e10864144a6e383a66c896257b7130c975d93809e2c0f6c38c4781dbb6d7231114e78d549aac38b215b0ad1af78b10d29ebdc368
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Grundström, ChristinOelker, MelanieSauer-Eriksson, A. Elisabeth

Search in DiVA

By author/editor
Grundström, ChristinOelker, MelanieSauer-Eriksson, A. Elisabeth
By organisation
Department of ChemistryUmeå Centre for Microbial Research (UCMR)
In the same journal
Cell reports
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 53 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 173 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf