title: Peptidoglycan hydrolase enterolysin a recognizes lipoteichoic acid chains in the cell walls of sensitive bacteria.
abstract: C-terminal domain of peptidoglycan hydrolase enterolysin A (EnlA) is involved in specific recognition and binding to the target cell envelopes and represents true cell wall binding (CWB) domain. Sensitivity/resistance to EnlA is dependent on binding ability/disability of its CWB domain. We assume that main mechanism of resistance against EnlA is absence of the specific receptor on the cell surface, which is necessary for binding of the enzyme molecule. Using competitive and enzymatic assays we have uncovered the chemical nature of the EnlA receptor, which is a lipoteichoic acid.
authors.affiliation: Institute of Animal Physiology, Slovak Academy of Sciences, Soltesovej 4-6, 04001 Kosice, Slovakia.
authors.forename: Lenka
authors.initials: L
authors.lastname: Malinicova
authors.forename: Katarina
authors.initials: K
authors.lastname: Dubikova
authors.forename: Maria
authors.initials: M
authors.lastname: Piknova
authors.forename: Peter
authors.initials: P
authors.lastname: Pristas
authors.forename: Peter
authors.initials: P
authors.lastname: Javorsky
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D001430:Bacteriocins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism*; D013293:Enterococcus faecalis / Q000737:chemistry / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013682:Teichoic Acids / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001430:Bacteriocins; D008070:Lipopolysaccharides; D013682:Teichoic Acids; C522987:enterolysin A, Enterococcus faecalis; C009900:lipoteichoic acid; D009238:N-Acetylmuramoyl-L-alanine Amidase