title: Interaction of the staphylococcin-like peptide Pep 5 with cell walls and isolated cell wall components of Gram-positive bacteria.
abstract: Unlike bacteriocins of Gram-negative bacteria, the strongly basic staphylococcin-like peptide Pep 5 lacked specific receptor mediated binding to sensitive Gram-positive bacteria. Studies with whole cells, purified cell walls, teichoic acids, and lipoteichoic acids strongly suggested that it binds reversibly via electrostatic interaction to negatively charged groups. Thus, Pep 5 binding could be reversed by sufficiently high concentrations of monovalent (K+, 150-250 mM) and divalent (Ca2+, 15-30 mM) cations (Fig. 1, 2) and by low pH (pH 2), where Pep 5 binding groups are protonated. Cells of Staphylococcus cohnii 22 with a reduced teichoic acid content showed a reduced Pep 5 binding capacity (Fig. 3). The results indicate that teichoic, teichuronic, and lipoteichoic acids are the unspecific cell wall binding sites for Pep 5.
mesh_terms: D000327:Adsorption; D001430:Bacteriocins / Q000378:metabolism*; D001665:Binding Sites; D002473:Cell Wall / Q000378:metabolism; D004347:Drug Interactions; D006094:Gram-Positive Bacteria / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008070:Lipopolysaccharides; D010455:Peptides / Q000378:metabolism*; D010712:Phosphatidic Acids / Q000378:metabolism; D011485:Protein Binding; D013212:Staphylococcus epidermidis / Q000378:metabolism; D013682:Teichoic Acids / Q000378:metabolism
chemical_list: D001430:Bacteriocins; D008070:Lipopolysaccharides; D010455:Peptides; D010712:Phosphatidic Acids; D013682:Teichoic Acids; C017724:staphylococcin; C009900:lipoteichoic acid