Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 34194667Publication DOI: 10.1016/j.csbj.2021.06.001Journal NLM ID: 101585369Publisher: Amsterdam: Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology
Correspondence: M.Dunne <matthew.dunne
hest.ethz.ch>
Institutions: Micreos Food Safety B.V., Wageningen, Nieuwe Kanaal 7P, 6709PA, The Netherlands, Institute of Food Nutrition and Health, ETH Zürich, Schmelzbergstrasse 7, 8092 Zürich, Switzerland, Evolutionary Genomics Group, Universidad Miguel Hernández, San Juan de Alicante, Spain
Bacteriophages (phages) are widely used as biocontrol agents in food and as antibacterial agents for treatment of food production plant surfaces. An important feature of such phages is broad infectivity towards a given pathogenic species. Phages attach to the surfaces of bacterial cells using receptor binding proteins (RBPs), namely tail fibers or tailspikes (TSPs). The binding range of RBPs is the primary determinant of phage host range and infectivity, and therefore dictates a phage's suitability as an antibacterial agent. Phages EP75 and EP335 broadly infect strains of E. coli serotype O157. To better understand host recognition by both phages, here we focused on characterizing the structures and functions of their RBPs. We identified two distinct tail fibers in the genome of the podovirus EP335: gp12 and gp13. Using fluorescence microscopy, we reveal how gp13 recognizes strains of E. coli serotypes O157 and O26. Phage EP75 belongs to the Kuttervirus genus within the Ackermannviridae family and features a four TSP complex (TSPs 1-4) that is universal among such phages. We demonstrate enzymatic activity of TSP1 (gp167) and TSP2 (gp168) toward the O18A and O157 O-antigens of E. coli, respectively, as well as TSP3 activity (gp169.1) against O4, O7, and O9 Salmonella O-antigens. TSPs of EP75 present high similarity to TSPs from E. coli phages CBA120 (TSP2) and HK620 (TSP1) and Salmonella myovirus Det7 (TSP3), which helps explain the cross-genus infectivity observed for EP75.
Lipopolysaccharide, O-antigen, Escherichia coli O157, Salmonella, bacteriophage, STEC, Tailspike, receptor binding protein, tail fiber
Structure type: polymer chemical repeating unit
Location inside paper: p.3424, Fig. 4F
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_136105,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144144,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983931,SB_173,SB_192,SB_7
Methods: SDS-PAGE, statistical analysis, bioinformatic analysis, LC-ESI-MS, fluorescence microscopy, dialysis, phage characterization, bacteriophage assays, protein expression
Related record ID(s): 10966
NCBI Taxonomy refs (TaxIDs): 1095706Reference(s) to other database(s): GTC:G56904CO, GlycomeDB:
28102
Show glycosyltransferases
There is only one chemically distinct structure:
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