Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 23053636Publication DOI: 10.1007/s10719-012-9451-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: michael.wacker
glycovaxyn.com
Institutions: GlycoVaxyn AG, Grabenstrasse 3, 8952, Schlieren, Switzerland
State-of-the-art production technologies for conjugate vaccines are complex, multi-step processes. An alternative approach to produce glycoconjugates is based on the bacterial N-linked protein glycosylation system first described in Campylobacter jejuni. The C. jejuni N-glycosylation system has been successfully transferred into Escherichia coli, enabling in vivo production of customized recombinant glycoproteins. However, some antigenic bacterial cell surface polysaccharides, like the Vi antigen of Salmonella enterica serovar Typhi, have not been reported to be accessible to the bacterial oligosaccharyltransferase PglB, hence hamper development of novel conjugate vaccines against typhoid fever. In this report, Vi-like polysaccharide structures that can be transferred by PglB were evaluated as typhoid vaccine components. A polysaccharide fulfilling these requirements was found in Escherichia coli serovar O121. Inactivation of the E. coli O121 O antigen cluster encoded gene wbqG resulted in expression of O polysaccharides reactive with antibodies raised against the Vi antigen. The structure of the recombinantly expressed mutant O polysaccharide was elucidated using a novel HPLC and mass spectrometry based method for purified undecaprenyl pyrophosphate (Und-PP) linked glycans, and the presence of epitopes also found in the Vi antigen was confirmed. The mutant O antigen structure was transferred to acceptor proteins using the bacterial N-glycosylation system, and immunogenicity of the resulting conjugates was evaluated in mice. The conjugate-induced antibodies reacted in an enzyme-linked immunosorbent assay with E. coli O121 LPS. One animal developed a significant rise in serum immunoglobulin anti-Vi titer upon immunization.
O-antigen, Salmonella typhi, conjugate vaccine, Vi-antigen, Escherichia coli O121
Structure type: suggested polymer biological repeating unit
Location inside paper: fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_141807,IEDB_151531
Methods: SDS-PAGE, DNA techniques, chemical analysis, ELISA, Western blotting, biological assays, CID-MS/MS, HPLC
Related record ID(s): 4019, 20676, 23071, 25713, 25714, 27355, 28687
NCBI Taxonomy refs (TaxIDs): 1055537
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error