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Sci. Signal., 20 September 2011
Vol. 4, Issue 191, p. rs9
[DOI: 10.1126/scisignal.2001668]


Editor's Summary

Profiling Pathogen-Induced Phosphorylation
Contamination of food with the pathogenic bacterium Salmonella enterica is a leading source of food poisoning. Salmonella induces inflammation in the intestine, a process that requires the bacterial enzyme SopB. Rogers et al. provide a temporal profile of sites in Salmonella-infected host cell proteins with increased or decreased phosphorylation, many of which were predicted to be targeted by the kinases Akt and Pim. Deficiency in members of the Pim family in host cells attenuated release of the proinflammatory cytokine interleukin-8. Many of these changes in the phosphorylation of host cell proteins were reduced in cells infected with Salmonella lacking SopB, which activates Akt in host cells. Activation of Akt by Salmonella was originally shown to promote survival of host cells, but some of the predicted Akt-mediated phosphorylation events may promote invasion by Salmonella as well. This work provides a map of the phosphorylation events that occur in Salmonella-infected cells and identifies the host cell kinases that the pathogen manipulates during the initial stages of infection.

Citation: L. D. Rogers, N. F. Brown, Y. Fang, S. Pelech, L. J. Foster, Phosphoproteomic Analysis of Salmonella-Infected Cells Identifies Key Kinase Regulators and SopB-Dependent Host Phosphorylation Events. Sci. Signal. 4, rs9 (2011).

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