Stalling autophagy: a new function for Listeria phospholipases

Authors:

Ivan Tattoli1,2, Matthew T. Sorbara2, Dana J. Philpott2 and Stephen E. Girardin1,*

doi: 10.15698/mic2014.01.124
Volume 1, pp. 48 to 50, published 06/01/2014.

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Affiliations:

1 Department of Laboratory Medicine and Pathobiology, University of Toronto, M6G 2T6, Toronto, Canada

2 Department of Immunology, University of Toronto, M6G 2T6, Toronto, Canada

Keywords: 

Listeria, Autophagy, mTOR.

Corresponding Author(s):

Stephen E. Girardin, Department of Laboratory Medicine and Pathobiology, University of Toronto, M6G 2T6, Toronto, Canada stephen.girardin@utoronto.ca

Conflict of interest statement:

The authors declare no conflict of interest.

Please cite this article as:

Ivan Tattoli, Matthew T. Sorbara, Dana J. Philpott and Stephen E. Girardin (2014). Stalling autophagy: a new function for Listeria phospholipases. Microbial Cell 1(1): 48-50.

© Tattoli et al. This is an open-access article released under the terms of the Creative Commons Attribution-NonCommercial-NonDerivative 3.0 license, which allows readers to download the article and share it with others, provided that the original authors and source are acknowledged. The article cannot be changed in any way or used commercially.

Abstract:

Listeria monocytogenes is a Gram-positive bacterial pathogen that induces its own uptake in non-phagocytic cells. Following invasion, Listeria escapes from the entry vacuole through the secretion of a pore-forming toxin, listeriolysin O (LLO) that acts to damage and disrupt the vacuole membrane. Listeria then replicates in the cytosol and is able to spread from cell-to-cell using actin-based motility. In addition to LLO, Listeria produces two phospholipase toxins, a phosphatidylinositol-specific phospholipase C (PI-PLC, encoded by plcB) and a broad-range phospholipase C (PC-PLC, encoded by plcA), which contribute to bacterial virulence. It has long been recognized that secretion of PI- and PC-PLC enables the disruption of the double membrane vacuole during cell-to-cell spread, and those phospholipases have also been shown to augment LLO-dependent escape from the entry endosome. However, a specific role for Listeria phospholipases during the cytosolic stage of infection has not been previously reported. In a recent study, we demonstrated that Listeria PI-PLC and PC-PLC contribute to the bacterial escape from autophagy through a mechanism that involves direct inhibition of the autophagic flux in the infected cells [Tattoli et al. EMBO J (2013), 32, 3066-3078].