Host-pathogen interactions during entry and actin-based movement of Listeria monocytogenes

Annu Rev Genet. 1997;31:113-38. doi: 10.1146/annurev.genet.31.1.113.


Listeria monocytogenes is a pathogenic bacterium that induces its own uptake into mammalian cells, and spreads from one cell to another by an actin-based motility process. Entry into host cells involves the bacterial surface proteins InlA (internalin) and InlB. The receptor for InlA is the cell adhesion molecule E-cadherin. InlB-mediated entry requires activation of the host protein phosphoinositide (PI) 3-kinase, probably in response to engagement of a receptor. Actin-based movement of L. monocytogenes is mediated by the bacterial surface protein ActA. The N-terminal region of this protein is necessary and sufficient for polymerization of host cell actin. Other host proteins involved in bacterial motility include profilin, Vasodilator-Stimulated Phosphoprotein (VASP), the Arp2/Arp3 complex, and cofilin. Studies of entry and intracellular movement of L. monocytogenes could lead to a better understanding of receptor-ligand signaling and dynamics of actin polymerization in mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / physiology*
  • Animals
  • Bacterial Proteins / physiology*
  • Humans
  • Listeria monocytogenes / physiology*
  • Mammals


  • Actins
  • Bacterial Proteins