S
Stephen C. Becker
Researcher at United States Department of Agriculture
Publications - 22
Citations - 1002
Stephen C. Becker is an academic researcher from United States Department of Agriculture. The author has contributed to research in topics: Lysin & Lysostaphin. The author has an hindex of 14, co-authored 21 publications receiving 908 citations. Previous affiliations of Stephen C. Becker include University of Maryland, Baltimore County & University of Maryland, Baltimore.
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Journal ArticleDOI
The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA
TL;DR: In this article, the optimal reaction conditions for the recombinant His-tagged LysK protein (pH range pH 6-10, and 0.3-0.5 M NaCl), and C-His-LysK MIC (32.85+/-4.87 mug mL(-1)).
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Chimeric Phage Lysins Act Synergistically with Lysostaphin To Kill Mastitis-Causing Staphylococcus aureus in Murine Mammary Glands
TL;DR: The animal model results demonstrate the potential of fusion peptidoglycan hydrolases as antimicrobials for the treatment of S. aureus-induced mastitis.
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LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells.
Stephen C. Becker,Shengli Dong,John Baker,Juli Foster-Frey,David G. Pritchard,David M. Donovan +5 more
TL;DR: In the checkerboard assay, the CHAP-SH3b fusion achieves the same level of antimicrobial synergy with lysostaphin as the full-length LysK, suggesting the need for a C-terminal binding domain.
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Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection
Mathias Schmelcher,Yang Shen,Daniel C. Nelson,Marcel R. Eugster,Fritz Eichenseher,Daniela C. Hanke,Martin J. Loessner,Shengli Dong,David G. Pritchard,Jean C. Lee,Stephen C. Becker,Juli Foster-Frey,David M. Donovan +12 more
TL;DR: The results corroborate the high potential of PGHs for treatment of S. aureus infections and reveal unique antimicrobial and biochemical properties of the different enzymes, suggesting a high diversity of potential applications despite highly conserved peptidoglycan target sites.
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Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain.
TL;DR: Through the collection of peptidoglycan hydrolase sequences, three new putative intron-containing phage endolysin genes were identified in public data sets for the phages G1, X2 and 85 and could be exploited to specifically enhance anti-staphylococcal efficacy in heterologous protein fusion constructs.