Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 28513100Publication DOI: 10.1111/mmi.13710Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: letarov
gmail.com; pgleiman
utmb.edu
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Research Center of Biotechnology, Russian Academy of Sciences, Winogradsky Institute of Microbiology, 7b2 pr. 60-letiya Oktyabrya, Moscow, Russia, Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, Lausanne, 1015, Switzerland, Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya St, Moscow, Russia, Faculty of Biology, Lomonosov Moscow State University, 1-12 Leninskie Gory, Moscow, Russia
Bacteriophages recognize and bind to their hosts with the help of receptor-binding proteins (RBPs) that emanate from the phage particle in the form of fibers or tailspikes. RBPs show a great variability in their shapes, sizes, and location on the particle. Some RBPs are known to depolymerize surface polysaccharides of the host while others show no enzymatic activity. Here we report that both RBPs of podovirus G7C - tailspikes gp63.1 and gp66 - are essential for infection of its natural host bacterium E. coli 4s that populates the equine intestinal tract. We characterize the structure and function of gp63.1 and show that unlike any previously described RPB, gp63.1 deacetylates surface polysaccharides of E. coli 4s leaving the backbone of the polysaccharide intact. We demonstrate that gp63.1 and gp66 form a stable complex, in which the N-terminal part of gp66 serves as an attachment site for gp63.1 and anchors the gp63.1-gp66 complex to the G7C tail. The esterase domain of gp63.1 as well as domains mediating the gp63.1-gp66 interaction is widespread among all three families of tailed bacteriophages.
Escherichia coli, bacteriophage, surface polysaccharide
Structure type: polymer chemical repeating unit
Location inside paper: p.388, fig.3C
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_115136,IEDB_130648,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_140630,IEDB_141794,IEDB_142488,IEDB_144990,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_167071,IEDB_190606,IEDB_423153,IEDB_983931,SB_192,SB_21,SB_7
Methods: NMR, SDS-PAGE, genetic methods, crystallography, acid degradation, phage assay
3D data: Gp63.1 crystal structure
Related record ID(s): 12221
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G63217BV
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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