title: Lytic activity of recombinant bacteriophage phi11 and phi12 endolysins on whole cells and biofilms of Staphylococcus aureus.
abstract: The recombinant phi11 endolysin hydrolyzed heat-killed staphylococci as well as staphylococcal biofilms. Cell wall targeting appeared to be a prerequisite for lysis of whole cells, and the combined action of the endopeptidase and amidase domains was necessary for maximum activity. In contrast, the phi12 endolysin was inactive and caused aggregation of the cells.
authors.affiliation: Institute for Medical Microbiology, Immunology and Parasitology, University of Bonn, Sigmund-Freud-Strasse 25, 53105 Bonn, Germany.
authors.forename: Peter
authors.initials: P
authors.lastname: Sass
authors.forename: Gabriele
authors.initials: G
authors.lastname: Bierbaum
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism; D001433:Bacteriolysis; D018441:Biofilms / Q000187:drug effects* / Q000254:growth & development; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D006358:Hot Temperature; D008242:Lysogeny; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D013204:Staphylococcus Phages / Q000235:genetics / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000166:cytology* / Q000187:drug effects* / Q000235:genetics / Q000254:growth & development
chemical_list: D011994:Recombinant Proteins; D010450:Endopeptidases; C001143:endolysin; D000581:Amidohydrolases; C019665:amidase