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A Bacteriophage Endolysin that Eliminates Intracellular Streptococci



Yang Shen, Marilia Barros, Tarek Vennemann, David Travis Gallagher, Yizhou Yin, Sara B. Linden, Ryan D. Heselpoth, Dennis J. Spencer, David M. Donovan, John Moult, Vincent A. Fischetti, Frank Heinrich, Mathias Loesche, Daniel C. Nelson


PlyC, a bacteriophage-encoded A-B endolysin, lyses Streptococcus pyogenes (Spy) on contact and protects mice from upper respiratory Spy colonization. Here, we demonstrate that PlyC is a novel, potent agent for targeting and controlling intracellular Spy which often lead to refractory streptococcal infections. We find that the PlyC holoenzyme translocates epithelial cell membranes mediated by its B subunit, PlyCB, colocalizes with Spy and clears intracellular Spy in a dose-dependent manner. Quantitative Studies using model membranes with well-defined lipid compositions show that PlyCB interacts strongly with phosphatidylserine (PS) whereas its interaction with other anionic or zwitterionic lipids is weak, suggesting specificity for PS as its cellular receptor. Neutron reflection indeed demonstrates that PlyC penetrates bilayers above a PS threshold concentration, consistent with the binding assays. X-ray crystallography and docking studies identify key residues that mediate PlyCB-PS interactions, and these verified in binding assays with site-directed mutants.


enzybiotics, PlyC


Shen, Y. , Barros, M. , Vennemann, T. , Gallagher, D. , Yin, Y. , Linden, S. , Heselpoth, R. , Spencer, D. , Donovan, D. , Moult, J. , Fischetti, V. , Heinrich, F. , Loesche, M. and Nelson, D. (2016), A Bacteriophage Endolysin that Eliminates Intracellular Streptococci, eLIFE, [online], (Accessed June 25, 2024)


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Created March 14, 2016, Updated October 12, 2021