Ats-1: a novel bacterial molecule that links autophagy to bacterial nutrition

Autophagy. 2013 May;9(5):787-8. doi: 10.4161/auto.23693. Epub 2013 Feb 6.

Abstract

Obligatory intracellular life style and a small number of genes for biosynthesis and metabolism necessitate the Gram-negative bacterium, Anaplasma phagocytophilum, to depend on the host cell for nutrients. A. phagocytophilum resides in a membrane-bound inclusion, and secretes a protein, Ats-1 (Anaplasma translocated substrate-1), into the host cell cytoplasm. Ats-1 binds BECN1, a protein critical for autophagy nucleation, and induces autophagosome formation. The autophagosomes traffic to, and fuse with, A. phagocytophilum inclusions, delivering autophagic cargo into the inclusions, which can serve as nutrients for bacterial growth. This finding demonstrates that A. phagocytophilum subverts host cell autophagic machinery to facilitate infection by secreting a BECN1-binding molecule.

Keywords: ATG14; Anaplasma phagocytophilum; Ats-1; BECN1; autophagy; bacterial nutrition; obligatory intracellular bacterium; omegasome; type IV secretion.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anaplasma phagocytophilum / cytology*
  • Anaplasma phagocytophilum / physiology*
  • Autophagy*
  • Bacterial Proteins / metabolism*
  • Ehrlichiosis / metabolism
  • Ehrlichiosis / microbiology
  • Ehrlichiosis / pathology
  • Host-Pathogen Interactions
  • Humans
  • Membrane Fusion
  • Phagosomes / metabolism

Substances

  • Bacterial Proteins