Characterization of LysBC17, a Lytic Endopeptidase from <i>Bacillus cereus</i>

• Main Authors: Steven M. Swift (Author), Irina V. Etobayeva (Author), Kevin P. Reid (Author), Jerel J. Waters (Author), Brian B. Oakley (Author), David M. Donovan (Author), Daniel C. Nelson (Author)
• Format: Book
• Published: MDPI AG, 2019-09-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Summary

<i>Bacillus cereus</i>, a Gram-positive bacterium, is an agent of food poisoning. <i>B. cereus</i> is closely related to <i>Bacillus anthracis</i>, a deadly pathogen for humans, and <i>Bacillus thuringenesis</i>, 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 <i>B. cereus</i> strain Bc17. This gene is also present in the <i>B. cereus</i> ATCC 14579 genome. The gene for LysBC17 encodes a protein of 281 amino acids. Recombinant LysBC17 was expressed and purified from <i>E. coli</i>. Optimal lytic activity against <i>B. cereus</i> occurred between pH 7.0 and 8.0, and in the absence of NaCl. The LysBC17 enzyme had lytic activity against strains of <i>B. cereus</i>, <i>B. anthracis</i>, and other <i>Bacillus</i> species.

Item Description

2079-6382
10.3390/antibiotics8030155