The 1.6 Å Crystal Structure of the Catalytic Domain of PlyB, a Bacteriophage Lysin Active Against Bacillus anthracis

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• 作者：Corrine J. Porter ; Raymond Schuch ; Adam J. Pelzek ; Ashley M. Buckle ; Sheena McGowan ; Matthew C.J. Wilce ; Jamie Rossjohn ; Ryann Russell ; Daniel Nelson ; Vincent A. Fischetti ; et al.
• 关键词：bacteriophage ; lysin ; Bacillus anthracis ; peptidoglycan ; glycosyl hydrolase 25 family
• 刊名：Journal of Molecular Biology
• 出版年：2007
• 出版时间：16 February 2007
• 年：2007
• 卷：366
• 期：2
• 页码：540-550
• 全文大小：1903 K

文摘

Lysins are peptidoglycan hydrolases that are produced by bacteriophage and act to lyse the bacterial host cell wall during progeny phage release. Here, we describe the structure and function of a novel bacteriophage-derived lysin, PlyB, which displays potent lytic activity against the Bacillus anthracis-like strain ATCC 4342. This molecule comprises an N-terminal catalytic domain (PlyB_cat) and a C-terminal bacterial SH3-like domain, SH3b. It is shown that both domains are required for effective catalytic activity against ATCC 4342. Further, PlyB has specific activity comparable to the phage lysin PlyG, an amidase being developed as a therapeutic against anthrax. In contrast to PlyG, however, the 1.6 Å X-ray crystal structure of PlyB_cat reveals that the catalytic domain adopts the glycosyl hydrolase (GH)-25, rather than phage T7 lysozyme-like fold. PlyB therefore represents a new class of anthrax lysin and a new defensive tool in the armament against anthrax-mediated bioterrorism.