Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
];
infection due to Neisseria meningitidis [ICD11:
XN1DV ]
NCBI PubMed ID: 26927318Publication DOI: 10.1093/glycob/cww027Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: Bernard.Priem
cermav.cnrs.fr
Institutions: Univ. Grenoble Alpes, CERMAV, F-38000 Grenoble, France CNRS, CERMAV, F-38000 Grenoble, France
Bacterial polysialyltransferases (PSTs) are processive enzymes involved in the synthesis of polysialic capsular polysaccharides. They can also synthesize polysialic acid in vitro from disialylated and trisialylated lactoside acceptors, which are the carbohydrate moieties of GD3 and GT3 gangliosides, respectively. Here, we engineered a non-pathogenic Escherichia coli strain that overexpresses recombinant sialyltransferases and sialic acid synthesis genes and can convert an exogenous lactoside into polysialyl lactosides. Several PSTs were assayed for their ability to synthesize polysialyl lactosides in the recombinant strains. Fed-batch cultures produced α-2,8 polysialic acid or alternate α-2,8-2,9 polysialic acid in quantities reaching several grams per liter. Bacterial culture in the presence of propargyl-beta-lactoside as the exogenous acceptor led to the production of conjugatable polysaccharides by means of copper-assisted click chemistry.
capsular polysaccharide, polysialic acid, bacterial glycosylation, Escherichia coli K12, click chemistry, glyco-engineering
Structure type: homopolymer
Location inside paper: p.723
Trivial name: polysialic acid
Compound class: CPS
Methods: 13C NMR, 1H NMR, DNA sequencing, TLC, genetic methods, HPAEC-PAD, chemoenzymatic modifications, conjugation
NCBI Taxonomy refs (TaxIDs): 1392869,
562,
487Reference(s) to other database(s): GTC:G89228EH, GlycomeDB:
27240
Show glycosyltransferases
There is only one chemically distinct structure:
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