Involvement of Listeria monocytogenes phosphatidylinositol-specific phospholipase C and host protein kinase C in permeabilization of the macrophage phagosome

Infect Immun. 2005 Jul;73(7):4410-3. doi: 10.1128/IAI.73.7.4410-4413.2005.

Abstract

We have previously shown that phosphatidylinositol-specific phospholipase C (PI-PLC) produced by Listeria monocytogenes activates a host protein kinase C (PKC) cascade which promotes escape of the bacterium from a macrophage-like cell phagosome. Here, we provide evidence linking bacterial PI-PLC and host PKC beta to phagosome permeabilization, which precedes escape.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Toxins
  • Heat-Shock Proteins / physiology
  • Hemolysin Proteins
  • Hydrogen-Ion Concentration
  • Indoles / pharmacology
  • Listeria monocytogenes / enzymology*
  • Macrophages / metabolism*
  • Maleimides / pharmacology
  • Mice
  • Permeability
  • Phagosomes / metabolism*
  • Phosphatidylinositol Diacylglycerol-Lyase / physiology*
  • Phosphoinositide Phospholipase C
  • Protein Kinase C / physiology*

Substances

  • Bacterial Toxins
  • Heat-Shock Proteins
  • Hemolysin Proteins
  • Indoles
  • Maleimides
  • Ro 31-8425
  • Protein Kinase C
  • Phosphoinositide Phospholipase C
  • Phosphatidylinositol Diacylglycerol-Lyase
  • hlyA protein, Listeria monocytogenes