Abstract
Bacteriophage endolysins have attracted attention as promising alternatives to antibiotics, and their modular structure facilitates endolysin engineering to develop novel endolysins with enhanced versatility. Here, we constructed hybrid proteins consisting of two different endolysins for simultaneous control of two critical foodborne pathogens, Staphylococcus aureus and Bacillus cereus. The full-length or enzymatically active domain (EAD) of LysB4, an endolysin from the B. cereus-infecting phage B4, was fused to LysSA11, an endolysin of the S. aureus-infecting phage SA11, via a helical linker in both orientations. The hybrid proteins maintained the lytic activity of their parental endolysins against both S. aureus and B. cereus, but they showed an extended antimicrobial spectrum. Among them, the EAD of LysB4 fused with LysSA11 (LysB4EAD-LyaSA11) showed significantly increased thermal stability compared to its parental endolysins. LysB4EAD-LysSA11 exhibited high lytic activity at pH 8.0–9.0 against S. aureus and at pH 5.0–10.0 against B. cereus, but the lytic activity of the protein decreased in the presence of NaCl. In boiled rice, treatment with 3.0 µM of LysB4EAD-LysSA11 reduced the number of S. aureus and B. cereus to undetectable levels within 2 h and also showed superior antimicrobial activity to LyB4EAD and LysSA11 in combination. These results suggest that LysB4EAD-LysSA11 could be a potent antimicrobial agent for simultaneous control of S. aureus and B. cereus.
Highlights
Food poisoning outbreaks caused by bacterial pathogens are a major concern worldwide
While most S. aureus endolysins are composed of three domains, LysSA11 is composed of two functional domains: a CHAP domain at its N-terminal region and a cell wall binding domain (CBD) at its
We proposed an endolysin engineering strategy to control S. aureus and B. cereus simultaneously by constructing hybrid proteins consisting of LysSA11 and LysB4
Summary
Food poisoning outbreaks caused by bacterial pathogens are a major concern worldwide. Donovan et al [13] reported that the full length and C-terminally truncated phage endolysin from Streptococcus agalactiae bacteriophage B30 was fused to the lysostaphin These proteins degraded both streptococcal and staphylococcal cells, and their lytic activities were tested in milk. This group created hybrid proteins with the endopeptidase of streptococcal phage λSA2 endolysin with the Staphylococcus-specific CBDs of either the endolysin LysK or lysostaphin. LysB4EAD-LysSA11 showed higher thermal stability than their parental endolysins and potent antimicrobial activity against S. aureus and B. cereus in boiled rice. This hybrid endolysin would be a promising antimicrobial agent for the simultaneous control of. This approach will provide an opportunity to design multifunctional and highly specific antimicrobials, thereby helping reduce the incidence of multidrug-resistant bacteria
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