Enhanced antimicrobial lytic activity of a chimeric Ply187 endolysin
AssigneeThe United States of America as represented by the Secretary of Agriculture
InventorsDavid M. Donovan, Jinzhe Mao
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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.
Claims17
An isolated or recombinant cDNA encoding an antimicrobial fusion peptidoglycan hydrolase polypeptide comprising a truncated Staphylococcus aureus bacteriophage 187 endolysin, Ply187 polypeptide, said truncated Ply187 polypeptide is Ply187AN, the truncated N-terminal Ply187CHAP domain and one or more of the SH3b cell wall binding domain(s) of the native bacteriophage Phage K endolysin, LysK, wherein said cDNA encodes an antimicrobial fusion peptidoglycan hydrolase polypeptide Ply187AN-KSH3b having the sequence of SEQ ID NO:
- 6.
An isolated recombinant antimicrobial fusion peptidoglycan hydrolase protein comprising a truncated S. aureus bacteriophage 187 endolysin, Ply187 polypeptide, said truncated Ply187 polypeptide is Ply187AN, the truncated N-terminal Ply187CHAP domain, in combination with one or more of the SH3b cell wall binding domain(s) of the native bacteriophage Phage K endolysin, LysK, wherein said fusion peptidoglycan hydrolase protein is the Ply187AN-KSh3b fusion protein.
Dependencies are inferred from the claim text.