Open AccessCell wall sorting of lipoproteins in Staphylococcus aureus
Author(s) -
William Wiley Navarre,
Simon Daefler,
Olaf Schneewind
Publication year - 1996
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.178.2.441-446.1996
Subject(s) - cell wall , biology , staphylococcus aureus , protein sorting signals , n terminus , cell , cell membrane , cell sorting , peptidoglycan , bacterial cell structure , microbiology and biotechnology , bacterial outer membrane , bacteria , lipid ii , signal peptide , biochemistry , peptide sequence , escherichia coli , gene , genetics
Many surface proteins are thought to be anchored to the cell wall of gram-positive organisms via their C termini, while the N-terminal domains of these molecules are displayed on the bacterial surface. Cell wall anchoring of surface proteins in Staphylococcus aureus requires both an N-terminal leader peptide and a C-terminal cell wall sorting signal. By fusing the cell wall sorting of protein A to the C terminus of staphylococcal beta-lactamase, we demonstrate here that lipoproteins can also be anchored to the cell wall of S. aureus. The topology of cell wall-anchored beta-lactamase is reminiscent of that described for Braun's murein lipoprotein in that the N terminus of the polypeptide chain is membrane anchored whereas the C-terminal end is tethered to the bacterial cell wall.