Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: meningitis [ICD11:
1D01 
];
urinary tract infections (UTI) [ICD11:
GC08 ];
infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 33730261Publication DOI: 10.1007/s10719-021-09985-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: michael.kowarik
lmtbio.com
Institutions: GlycoVaxyn AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Department of Chemistry, University of Cape Town, Rondebosch, 7701, South Africa, LimmaTech Biologics AG, Grabenstrasse 3, 8952, Schlieren, Switzerland, Institute of Microbiology, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093, Zurich, Switzerland, Molecular Partners AG, Wagistrasse 14, 8952, Schlieren, Switzerland, Numab Therapeutics AG, Einsiedlerstrasse 34, 8820, Wadenswil, Switzerland, Dip. di Scienze della Vita, University di Trieste, 34127, Trieste, Italy, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire, EN6 3QG, UK, Wacker Biotech Consulting AG, Heuelstrasse 22, 8800, Thalwil, Switzerland
Extraintestinal pathogenic Escherichia coli (ExPEC) cause a wide range of clinical diseases such as bacteremia and urinary tract infections. The increase of multidrug resistant ExPEC strains is becoming a major concern for the treatment of these infections and E. coli has been identified as a critical priority pathogen by the WHO. Therefore, the development of vaccines has become increasingly important, with the surface lipopolysaccharide constituting a promising vaccine target. This study presents genetic and structural analysis of clinical urine isolates from Switzerland belonging to the serotype O25. Approximately 75% of these isolates were shown to correspond to the substructure O25B only recently described in an emerging clone of E. coli sequence type 131. To address the high occurrence of O25B in clinical isolates, an O25B glycoconjugate vaccine was prepared using an E. coli glycosylation system. The O antigen cluster was integrated into the genome of E. coli W3110, thereby generating an E. coli strain able to synthesize the O25B polysaccharide on a carrier lipid. The polysaccharide was enzymatically conjugated to specific asparagine side chains of the carrier protein exotoxin A (EPA) of Pseudomonas aeruginosa by the PglB oligosaccharyltransferase from Campylobacter jejuni. Detailed characterization of the O25B-EPA conjugate by use of physicochemical methods including NMR and GC-MS confirmed the O25B polysaccharide structure in the conjugate, opening up the possibility to develop a multivalent E. coli conjugate vaccine containing O25B-EPA.
Escherichia coli, physicochemical characterization, bioconjugate vaccine, serotype O25B, ST131
Structure type: polymer chemical repeating unit
Location inside paper: p. 426, Fig. 1b, O25A
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, SDS-PAGE, sugar analysis, GC, de-O-acetylation, genetic methods, immunoblotting, RP-HPLC, MALDI-MS/MS, bioconjugation, HPAEC-CD
Related record ID(s): 9660, 9661
NCBI Taxonomy refs (TaxIDs): 1095709Reference(s) to other database(s): GTC:G18223OD, GlycomeDB:
28106
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error