English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The CrbS/R two-component signal transduction system is a conserved regulatory mechanism through which specific Gram-negative bacteria control acetate flux into primary metabolic pathways. CrbS/R governs expression of acetyl-CoA synthase ( acsA ), an enzyme that converts acetate to acetyl-CoA, a metabolite at the nexus of the cell’s most important energy-harvesting and biosynthetic reactions. During infection, bacteria can utilize this system to hijack host acetate metabolism and alter the course of colonization and pathogenesis. In toxigenic strains of  Vibrio cholerae , CrbS/R-dependent expression of  acsA  is required for virulence in an arthropod model. Here, we investigate the function of the CrbS/R system in  Pseudomonas aeruginosa ,  Pseudomonas entomophila , and non-toxigenic  V .  cholerae  strains. We demonstrate that its role in acetate metabolism is conserved; this system regulates expression of the  acsA  gene and is required for growth on acetate as a sole carbon source. As a first step towards describing the mechanism of signaling through this pathway, we identify residues and domains that may be critical for phosphotransfer. We further demonstrate that although CrbS, the putative hybrid sensor kinase, carries both a histidine kinase domain and a receiver domain, the latter is not required for  acsA  transcription. In order to determine whether our findings are relevant to pathogenesis, we tested our strains in a  Drosophila  model of oral infection previously employed for the study of acetate-dependent virulence by  V .  cholerae . We show that non-toxigenic  V .  cholerae  strains lacking CrbS or CrbR are significantly less virulent than are wild-type strains, while  P .  aeruginosa  and  P .  entomophila  lacking CrbS or CrbR are fully pathogenic. Together, the data suggest that the CrbS/R system plays a central role in acetate metabolism in  V .  cholerae ,  P .  aeruginosa , and  P .  entomophila . However, each microbe’s unique environmental adaptations and pathogenesis strategies may dictate conditions under which CrbS/R-mediated  acs  expression is most critical.

Regulation of acetyl-CoA synthetase transcription by the CrbS/R two-component system is conserved in genetically diverse environmental pathogens