Title: Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme. Authors
|Mao, Jinzhe -|
Submitted to: Applied and Environmental Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: February 11, 2013
Publication Date: May 1, 2013
Citation: Mao, J., Donovan, D.M. 2013. Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme. Applied and Environmental Microbiology. 342(1):30-36. Interpretive Summary: Brief explanation of the reason for, accomplishment of, and significance of the research in language intelligible to the general public. C. Problem— Mastitis causes the dairy industry in the USA over $2 billion in losses every year. Staphylococcus aureus is a notorious pathogen for both humans and animals, causing up to 40% of the bovine mastitis in the USA. There is a need for novel antimicrobials due to the high incidence of resistance development and multi-drug resistant strains of this pathogen. C. Accomplishment— This manuscript describes a phage endolysin (phage phi187) that has staphylolytic properties when purified and exposed to S. aureus cells. In addition, the lytic activity is enhanced when the lytic domain is fused to a staphylococcal cell wall binding domain such that the activity is sufficient to consider testing in animal models. C. Contribution of Accomplishment to Solving the Problem-- This fusion antimicrobial is a candidate for treating bovine mastitis and other staphylococcal infections and because it is active in a fusion setting might be amenable for use in other potentially more active fusion protein antimicrobials.
Technical Abstract: Peptidoglycan hydrolases are an effective new source of antimicrobials. A chimeric fusion protein of the Ply187 endopeptidase domain and LysK SH3b cell wall binding domain is a potent agent against Staphylococcus aureus in three functional assays.