Salmonella modulates vesicular traffic by altering phosphoinositide metabolism

Science. 2004 Jun 18;304(5678):1805-7. doi: 10.1126/science.1098188.

Abstract

Salmonella enterica, the cause of food poisoning and typhoid fever, induces actin cytoskeleton rearrangements and membrane ruffling to gain access into nonphagocytic cells, where it can replicate and avoid innate immune defenses. Here, we found that SopB, a phosphoinositide phosphatase that is delivered into host cells by a type III secretion system, was essential for the establishment of Salmonella's intracellular replicative niche. SopB mediated the formation of spacious phagosomes following bacterial entry and was responsible for maintaining high levels of phosphatidylinositol-three-phosphate [PtdIns(3)P] in the membrane of the bacteria-containing vacuoles. Absence of SopB caused a significant defect in the maturation of the Salmonella-containing vacuole and impaired bacterial intracellular growth.

Publication types

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

MeSH terms

  • Antigens, CD / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cell Line
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Cytoplasmic Vesicles / metabolism
  • Cytoplasmic Vesicles / microbiology*
  • Cytoplasmic Vesicles / ultrastructure
  • Epithelial Cells / microbiology
  • Gene Deletion
  • Genomic Islands
  • Humans
  • Intestinal Mucosa / cytology
  • Intestinal Mucosa / microbiology*
  • Lysosomal Membrane Proteins
  • Microscopy, Video
  • Mutation
  • Phagosomes / metabolism
  • Phagosomes / microbiology*
  • Phosphatidylinositol Phosphates / metabolism
  • Phosphatidylinositols / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / growth & development
  • Salmonella typhimurium / metabolism*
  • Salmonella typhimurium / pathogenicity
  • Vacuoles / metabolism
  • Vacuoles / microbiology
  • Vacuoles / ultrastructure

Substances

  • Antigens, CD
  • Bacterial Proteins
  • Lysosomal Membrane Proteins
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols
  • Recombinant Fusion Proteins
  • SopB protein, Bacteria
  • phosphatidylinositol 3,5-diphosphate
  • phosphatidylinositol 3-phosphate
  • SopB protein, Salmonella