Cytoskeleton rearrangements during Listeria infection: clathrin and septins as new players in the game

Cell Motil Cytoskeleton. 2009 Oct;66(10):816-23. doi: 10.1002/cm.20353.


The study of an infection process can reveal how microbes exploit the host, and can illuminate unknown host cellular functions. Invasive pathogens have evolved efficient strategies to promote their internalization within normally non-phagocytic host cells. The so-called "zippering" bacteria present to host cell receptors molecules that mimic endogenous ligands, thereby inducing specific intracellular signaling cascades ultimately resulting in actin polymerization and uptake. Here we review how the bacterial pathogen Listeria monocytogenes enters into cells, and present a series of studies revealing that in addition to actin rearrangements this bacterium exploits the clathrin-mediated endocytosis machinery together with septins, a novel cytoskeleton element. The challenge is now to decipher how all of these components orchestrate themselves to permit entry into normally non-phagocytic cells.

Publication types

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

MeSH terms

  • Actins / metabolism*
  • Bacterial Proteins / physiology
  • Cadherins / physiology
  • Clathrin / physiology*
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / physiology
  • Cytoskeleton / metabolism*
  • Endocytosis
  • GTP-Binding Proteins / physiology
  • Humans
  • Listeria monocytogenes / physiology
  • Listeriosis / physiopathology*
  • Membrane Proteins / physiology
  • Proto-Oncogene Proteins c-met / metabolism
  • Septins


  • Actins
  • Bacterial Proteins
  • Cadherins
  • Clathrin
  • Cytoskeletal Proteins
  • Membrane Proteins
  • inlB protein, Listeria monocytogenes
  • Proto-Oncogene Proteins c-met
  • GTP-Binding Proteins
  • SEPTIN9 protein, human
  • Septins