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首页> 外文期刊>Journal of Molecular Biology >Structure and Function of the Branched Receptor-Binding Complex of Bacteriophage CBA120
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Structure and Function of the Branched Receptor-Binding Complex of Bacteriophage CBA120

机译：噬菌体CBA120分枝受体结合复合物的结构和功能

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摘要

Bacteriophages recognize their host cells with the help of tail fiber and tailspike proteins that bind, cleave, or modify certain structures on the cell surface. The spectrum of ligands to which the tail fibers and tailspikes can bind is the primary determinant of the host range. Bacteriophages with multiple tailspike/tail fibers are thought to have a wider host range than their less endowed relatives but the function of these proteins remains poorly understood. Here, we describe the structure, function, and substrate specificity of three tailspike proteins of bacteriophage CBA120-TSP2, TSP3 and TSP4 (orf211 through orf213, respectively). We show that tailspikes TSP2, TSP3 and TSP4 are hydrolases that digest the 0157, 077, and 078 Escherichia coli 0 antigens, respectively. We demonstrate that recognition of the E. coli O157:H7 host by CBA120 involves binding to and digesting the O157 O-antigen by TSP2. We report the crystal structure of TSP2 in complex with a repeating unit of the O157 O-antigen. We demonstrate that according to the specificity of its tailspikes TSP2, TSP3, and TSP4, CBA120 can infect E. coli 0157, 077, and 078, respectively. We also show that CBA120 infects Salmonella enterica serovar Minnesota, and this host range expansion is likely due to the function of TSP1. Finally, we describe the assembly pathway and the architecture of the TSP1 TSP2 TSP3 TSP4 branched complex in CBA120 and its related Vil-like phages. (C) 2019 Elsevier Ltd. All rights reserved.
机译：噬菌体在尾纤维和尾剂蛋白的帮助下识别它们的宿主细胞，其在细胞表面上结合，切割或改变某些结构。尾纤维和尾丝可以结合的配体的光谱是主机范围的主要决定因素。具有多种尾纤维/尾纤维的噬菌体被认为具有比其较少赋予的亲属更宽的宿主范围，但这些蛋白质的功能仍然明显。在这里，我们描述了噬菌体CBA120-TSP2，TSP3和TSP4（分别通过ORF213的TSP4（ORF211）的三种尾铜蛋白的结构，功能和衬底特异性。我们表明，尾标TSP2，TSP3和TSP4分别是消化0157,077和078大肠杆菌0抗原的水解酶。我们证明CBA120的大肠杆菌O157：H7宿主的识别涉及通过TSP2与O157 O-抗原结合并消化O157 O-抗原。我们报告了与O157 O-抗原的重复单元复合物中TSP2的晶体结构。我们证明根据其尾标TSP2，TSP3和TSP4的特异性，CBA120可以分别感染大肠杆菌0157,077和078。我们还表明CBA120感染了Salmonella entenica Serovar Minnesota，并且该主机范围扩展可能是由于TSP1的功能。最后，我们描述了CBA120中TSP1 TSP2 TSP3 TSP4分支复合体的组装途径和其相关的VIL样噬菌体。 （c）2019 Elsevier Ltd.保留所有权利。

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