Characterization of an Endolysin Targeting That Affects Spore Outgrowth.

is a spore-forming enteric pathogen causing life-threatening diarrhoea and colitis. Microbial disruption caused by antibiotics has been linked with susceptibility to, and transmission and relapse of, infection. Therefore, there is an urgent need for novel therapeutics that are effective in preventing growth, spore germination, and outgrowth. In recent years bacteriophage-derived endolysins and their derivatives show promise as a novel class of antibacterial agents. In this study, we recombinantly expressed and characterized a cell wall hydrolase (CWH) lysin from phage, phiMMP01. The full-length CWH displayed lytic activity against selected strains. However, removing the N-terminal cell wall binding domain, creating CWH, resulted in increased and/or an expanded lytic spectrum of activity. specificity was retained versus commensal clostridia and other bacterial species. As expected, the putative cell wall binding domain, CWH, was completely inactive. We also observe the effect of CWH on preventing spore outgrowth. Our results suggest that CWH has therapeutic potential as an antimicrobial agent against infection.