Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 31325442Publication DOI: 10.1016/j.jmb.2019.07.022Journal NLM ID: 2985088RPublisher: Elsevier
Correspondence: Petr G. Leiman <pgleiman
utmb.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.
NMR, X-ray crystallography, bacterial surface polysaccharides, bacteriophage attachment, host-cell recognition
Structure type: polymer chemical repeating unit
Location inside paper: p.3731, fig.10(a), O157 OPS
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_136045,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_146664,IEDB_152214,IEDB_174333,IEDB_885822,IEDB_983931,SB_192,SB_86
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
Comments, role: chemical repeat frame is different in the paper
3D data: 3D data
Related record ID(s): 2673, 2674, 2675, 2676, 2677, 2678
NCBI Taxonomy refs (TaxIDs): 83334Reference(s) to other database(s): GTC:G60704LX, GlycomeDB:
3513
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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