Activation of Akt by the Bacterial Inositol Phosphatase, SopB, is Wortmannin Insensitive
2011

How Salmonella Activates the Akt Pathway

publication 10 minutes Evidence: moderate

Author Information

Author(s): Cooper Kendal G., Winfree Seth, Malik-Kale Preeti, Jolly Carrie, Ireland Robin, Knodler Leigh A., Steele-Mortimer Olivia, Abu Kwaik Yousef

Primary Institution: Laboratory of Intracellular Parasites, National Institutes of Allergy and Infectious Disease, National Institutes of Health

Hypothesis

Salmonella activates the Akt pathway through a mechanism that is independent of the canonical PI3K pathway.

Conclusion

Salmonella activates Akt via a wortmannin-insensitive mechanism that likely does not involve class I PI3K.

Supporting Evidence

  • SopB is necessary and sufficient for Akt phosphorylation in HeLa cells.
  • Wortmannin does not inhibit SopB-dependent Akt phosphorylation.
  • LY294002 effectively inhibits SopB-dependent Akt phosphorylation.
  • Depletion of class I PI3K regulatory subunits does not affect Salmonella-induced Akt phosphorylation.
  • PDK1 and mTORC2 are required for SopB-mediated Akt phosphorylation.

Takeaway

Salmonella can trick our cells into activating a survival signal called Akt without using the usual method, which is surprising.

Methodology

HeLa cells were infected with Salmonella and Akt phosphorylation was assessed using immunoblotting and ELISA.

Limitations

The study primarily focused on HeLa cells, which may not fully represent other cell types.

Statistical Information

P-Value

p<0.05

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0022260

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