Expression of δ-toxin by Staphylococcus aureus mediates escape from phago-endosomes of human epithelial and endothelial cells in the presence of β-toxin.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read Online Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: Hindawi Country of Publication: India NLM ID: 100883691 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1462-5822 (Electronic) Linking ISSN: 14625814 NLM ISO Abbreviation: Cell Microbiol Subsets: MEDLINE
    • Publication Information:
      Publication: 2022- : Mumbai : Hindawi
      Original Publication: Oxford : Wiley-Blackwell, c1999-
    • Subject Terms:
      Bacterial Toxins/*metabolism ; Endosomes/*microbiology ; Endothelial Cells/*microbiology ; Epithelial Cells/*microbiology ; Hemolysin Proteins/*metabolism ; Phagosomes/*microbiology ; Sphingomyelin Phosphodiesterase/*metabolism ; Staphylococcus aureus/*pathogenicity; Bacterial Proteins/metabolism ; Cell Line ; Humans ; Trans-Activators/metabolism ; Virulence Factors/metabolism
    • Abstract:
      Staphylococcus aureus is able to invade non-professional phagocytes by interaction of staphylococcal adhesins with extracellular proteins of mammalian cells and eventually resides in acidified phago-endosomes. Some staphylococcal strains have been shown to subsequently escape from this compartment. A functional agr quorum-sensing system is needed for phagosomal escape. However, the nature of this agr dependency as well as the toxins involved in disruption of the phagosomal membrane are unknown. Using a novel technique to detect vesicular escape of S. aureus, we identified staphylococcal virulence factors involved in phagosomal escape. Here we show that a synergistic activity of the cytolytic peptide, staphylococcal δ-toxin and the sphingomyelinase β-toxin enable the phagosomal escape of staphylococci in human epithelial as well as in endothelial cells. The agr dependency of this process can be directly explained by the location of the structural gene for δ-toxin within the agr effector RNAIII.
      (© 2010 Blackwell Publishing Ltd.)
    • Accession Number:
      0 (Agr protein, Staphylococcus aureus)
      0 (Bacterial Proteins)
      0 (Bacterial Toxins)
      0 (Hemolysin Proteins)
      0 (Trans-Activators)
      0 (Virulence Factors)
      0 (staphylococcal delta toxin)
      EC 3.1.4.12 (Sphingomyelin Phosphodiesterase)
      EC 3.1.4.12 (hlb protein, Staphylococcus aureus)
    • Publication Date:
      Date Created: 20101016 Date Completed: 20110414 Latest Revision: 20110113
    • Publication Date:
      20240829
    • Accession Number:
      10.1111/j.1462-5822.2010.01538.x
    • Accession Number:
      20946243