Characterization of LysBC17, a Lytic Endopeptidase from Bacillus cereus

Abstract

Bacillus cereus, a Gram-positive bacterium, is an agent of food poisoning. B. cereus is closely related to Bacillus anthracis, a deadly pathogen for humans, and Bacillus thuringenesis, an insect pathogen. Due to the growing prevalence of antibiotic resistance in bacteria, alternative antimicrobials are needed. One such alternative is peptidoglycan hydrolase enzymes, which can lyse Gram-positive bacteria when exposed externally. A bioinformatic search for bacteriolytic enzymes led to the discovery of a gene encoding an endolysin-like endopeptidase, LysBC17, which was then cloned from the genome of B. cereus strain Bc17. This gene is also present in the B. cereus ATCC 14579 genome. The gene for LysBC17 encodes a protein of 281 amino acids. Recombinant LysBC17 was expressed and purified from E. coli. Optimal lytic activity against B. cereus occurred between pH 7.0 and 8.0, and in the absence of NaCl. The LysBC17 enzyme had lytic activity against strains of B. cereus, B. anthracis, and other Bacillus species.

Bacilli as sources of agrobiotechnology: recent advances and future directions

“…in controlling plant pathogens (26,27). Antagonistic activities of these bacilli take place primarily through the production and secretion of various bioactive secondary metabolites (11,14,(28)(29)(30)(31)(32) and lytic enzymes (33)(34)(35)(36). Verschuere et al (37) argued that among bacteriabased antagonists, B. subtilis is one of the most studied and used bacteria with a wide range of activities against phytopathogens.…”

Pharmaceutical Approaches on Antimicrobial Resistance: Prospects and Challenges

“…LysBC17, a recombinant endolysin prophage derived from the genome of B. cereus strain Bc17, was reported to have narrow-spectrum lytic activity against several Bacillus strains [ 153 ]. Swift et al reported similar activity in PlyCP10 and PlyCP41 endolysins obtained from the genome of Bacillus bacteria [ 154 ].…”

Bacteriophage-Derived Endolysins Applied as Potent Biocontrol Agents to Enhance Food Safety

“…Among the endolysins, muramidase, which is found in the Pseudomonas aeruginosa phage phiKZ gp144 lysin [15], is the rarest type; in contrast, amidases that hydrolyze the most conserved bonds in the peptidoglycan are most widely distributed [16][17][18][19]. Studies of endopeptidases have shown that Listeria endolysin Ply500, Ply118 [20], and some of the Bacillus cereus endolysins [21,22] possess L-alanyl-D-glutamate endopeptidases. Other, staphylococcal endolysin phi11 possess D-alanyl-glycyl endopeptidase and cleave within peptides that cross-link the cell wall [23].…”