title: Characterization of an endolysin, LysBPS13, from a Bacillus cereus bacteriophage.
abstract: Use of bacteriophages as biocontrol agents is a promising tool for controlling pathogenic bacteria including antibiotic-resistant bacteria. Not only bacteriophages but also endolysins, the peptidoglycan hydrolyzing enzymes encoded by bacteriophages, have high potential for applications as biocontrol agents against food-borne pathogens. In this study, a putative endolysin gene was identified in the genome of the bacteriophage BPS13, which infects Bacillus cereus. In silico analysis of this endolysin, designated LysBPS13, showed that it consists of an N-terminal catalytic domain (PGRP domain) and a C-terminal cell wall binding domain (SH3_5 domain). Further characterization of the purified LysBPS13 revealed that this endolysin is an N-acetylmuramyl-l-alanine amidase, the activity of which was not influenced by addition of EDTA. In addition, LysBPS13 demonstrated remarkable thermostability in the presence of glycerol, and it retained its lytic activity even after incubation at 100 °C for 30 min. Taken together, these results indicate that LysBPS13 can be considered a favorable candidate for a new antimicrobial agent to control B. cereus.
authors.affiliation: Department of Food and Animal Biotechnology, Center for Agricultural Biomaterials Seoul National University, Seoul, South Korea.
authors.forename: Jaeeun
authors.initials: J
authors.lastname: Park
authors.forename: Jiae
authors.initials: J
authors.lastname: Yun
authors.forename: Jeong-A
authors.initials: JA
authors.lastname: Lim
authors.forename: Dong-Hyun
authors.initials: DH
authors.lastname: Kang
authors.forename: Sangryeol
authors.initials: S
authors.lastname: Ryu
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism; D001409:Bacillus cereus / Q000737:chemistry / Q000821:virology*; D001435:Bacteriophages / Q000235:genetics*; D001665:Binding Sites; D003902:Detergents; D004492:Edetic Acid; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004795:Enzyme Stability; D005814:Genes, Viral; D005990:Glycerol; D006863:Hydrogen-Ion Concentration; D009112:Muramic Acids / Q000378:metabolism; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009994:Osmolar Concentration; D010457:Peptidoglycan / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013696:Temperature; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D003902:Detergents; D009112:Muramic Acids; D010457:Peptidoglycan; D011994:Recombinant Proteins; D014764:Viral Proteins; D004492:Edetic Acid; D010450:Endopeptidases; C001143:endolysin; D009238:N-Acetylmuramoyl-L-alanine Amidase; D005990:Glycerol