Subcellular location of the soluble lytic transglycosylase homologue in Staphylococcus aureus

Curr Microbiol. 2005 Jan;50(1):47-51. doi: 10.1007/s00284-004-4381-9. Epub 2004 Dec 8.

Abstract

The immunodominant antigen A, IsaA, of Staphylococcus aureus was found to include a putative soluble lytic transglycosylase domain in its C-terminal region. Since the presence of this distinctive domain suggested that the protein might participate in peptidoglycan turnover, as indicated in Gram-negative bacteria, its cellular location was investigated. The protein was found not only in the culture supernatant but also in the cell wall fraction. To estimate its physiological role for the bacterium, its cell surface distribution was studied by immunoelectron microscopy. Protein A-gold particles binding to the immune complex were mainly located on the septal region of the bacterial cell surface. These data suggested that IsaA might be involved in bacterial cell separation through a preferential interaction with peptidoglycan chain.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Bacterial / analysis*
  • Antigens, Bacterial / chemistry
  • Antigens, Bacterial / physiology
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Peptidoglycan / metabolism
  • Peptidoglycan Glycosyltransferase / analysis*
  • Staphylococcus aureus / chemistry*

Substances

  • Antigens, Bacterial
  • IsaA antigen, staphylococcus
  • Peptidoglycan
  • Peptidoglycan Glycosyltransferase

Associated data

  • GENBANK/AB042839