Plattner M, Shneider MM, Arbatsky NP, Shashkov AS, Chizhov AO, Nazarov S, Taylor NMI, Prokhorov NS, Buth SA, Gambino M, Gencay YE, Brondsted L, Kutter EM, Knirel YA, Leiman PG Structure and function of the branched receptor-binding complex of bacteriophage CBA120 Journal of Molecular Biology431 (2019)
3718-3719
The structure was elucidated in this paper NCBI PubMed ID:31325442 Publication DOI:10.1016/j.jmb.2019.07.022 Journal NLM ID:2985088R Publisher: Elsevier Correspondence: Petr G. Leiman <pgleimanutmb.edu> Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555-0647, USA, Ecole Polytechnique Federale de Lausanne, Lausanne CH-1015, Switzerland, Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya St., 117997 Moscow, Russia, Structural Biology of Molecular Machines Group, Protein Structure & Function Programme, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen 2200, Denmark, Department of Veterinary and Animal Sciences, University of Copenhagen, Stigbojlen 4, 1870 Frederiksberg C, Denmark, The Evergreen State College, Olympia, WA 98505, USA
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 O157, O77, and O78 Escherichia coli O-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 O157, O77, and O78, 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 ViI-like phages.
Methods: 13C NMR, 1H NMR, NMR-2D, X-ray, SDS-PAGE, electron microscopy, cloning, bioinformatic analysis, crystallization, binding assays, HR-ESI-MS, bacteriophage digestion, phage characterization Biological activity: TSP2ΔN digested this OPS down to small oligosaccharides, whereas TSP4ΔN showed very weak, activity Enzymes that release or process the structure: TSP2 hydrolase 3D data: 3D data
Related record ID(s): 1170, 2674, 2675, 2676, 2677, 2678 NCBI Taxonomy refs (TaxIDs):83334 Reference(s) to other database(s): GTC:G56054MW Show glycosyltransferases
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