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000207430 1001_ $$0P:(DE-HGF)0$$aZhang, Gongyi$$b0$$eCorresponding Author
000207430 245__ $$aThe CD27L and CTP1L Endolysins Targeting Clostridia Contain a Built-in Trigger and Release Factor
000207430 260__ $$aLawrence, Kan.$$bPLoS$$c2014
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000207430 520__ $$aThe bacteriophage ΦCD27 is capable of lysing Clostridium difficile, a pathogenic bacterium that is a major cause for nosocomial infection. A recombinant CD27L endolysin lyses C. difficile in vitro, and represents a promising alternative as a bactericide. To better understand the lysis mechanism, we have determined the crystal structure of an autoproteolytic fragment of the CD27L endolysin. The structure covers the C-terminal domain of the endolysin, and represents a novel fold that is identified in a number of lysins that target Clostridia bacteria. The structure indicates endolysin cleavage occurs at the stem of the linker connecting the catalytic domain with the C-terminal domain. We also solved the crystal structure of the C-terminal domain of a slow cleaving mutant of the CTP1L endolysin that targets C. tyrobutyricum. Two distinct dimerization modes are observed in the crystal structures for both endolysins, despite a sequence identity of only 22% between the domains. The dimers are validated to be present for the full length protein in solution by right angle light scattering, small angle X-ray scattering and cross-linking experiments using the cross-linking amino acid p-benzoyl-L-phenylalanine (pBpa). Mutagenesis on residues contributing to the dimer interfaces indicates that there is a link between the dimerization modes and the autocleavage mechanism. We show that for the CTP1L endolysin, there is a reduction in lysis efficiency that is proportional to the cleavage efficiency. We propose a model for endolysin triggering, where the extended dimer presents the inactive state, and a switch to the side-by-side dimer triggers the cleavage of the C-terminal domain. This leads to the release of the catalytic portion of the endolysin, enabling the efficient digestion of the bacterial cell wall.
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000207430 7001_ $$0P:(DE-H253)PIP1020991$$aMertens, Haydyn$$b1
000207430 7001_ $$0P:(DE-HGF)0$$aGarefalaki, Vasiliki$$b2
000207430 7001_ $$0P:(DE-H253)PIP1018937$$aJeffries, Cy$$b3
000207430 7001_ $$0P:(DE-HGF)0$$aThompson, Andrew$$b4
000207430 7001_ $$0P:(DE-HGF)0$$aLemke, Edward A.$$b5
000207430 7001_ $$0P:(DE-H253)PIP1001422$$aSvergun, Dmitri$$b6
000207430 7001_ $$0P:(DE-HGF)0$$aMayer, Melinda J.$$b7
000207430 7001_ $$0P:(DE-HGF)0$$aNarbad, Arjan$$b8
000207430 7001_ $$0P:(DE-H253)PIP1013457$$aMeijers, Rob$$b9
000207430 7001_ $$0P:(DE-HGF)0$$aZhang, Gongyi$$b10
000207430 773__ $$0PERI:(DE-600)2205412-1$$a10.1371/journal.ppat.1004228$$gVol. 10, no. 7, p. e1004228 -$$n7$$pe1004228 -$$tPLoS pathogens$$v10$$x1553-7374$$y2014
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