Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
];
infection due to Legionella pneumophila [ICD11:
XN9YS ]
The structure was elucidated in this paperNCBI PubMed ID: 20978010Publication DOI: 10.1093/glycob/cwq135Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: martin.young
nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Drive, Ottawa, Ontario, Canada
In addition to sialic acid, bacteria produce several other nonulosonic acids, including legionaminic acid (Leg). This has exactly the same stereochemistry as sialic acid, with the added features of 9-deoxy and 7-amino groups. In order to explore the biological effects of replacing sialic acid residues (Neu5Ac) in glycoconjugates with Leg in its diacetylated form, diacetyllegionaminic acid (Leg5Ac7Ac), we tested CMP-Leg5Ac7Ac as a donor substrate with a selection of bacterial and mammalian sialyltransferases. The CMP-Leg5Ac7Ac was synthesized in vitro by means of cloned enzymes from the bacillosamine portion of the Campylobacter jejuni N-glycan pathway and from the Leg pathway of Legionella pneumophila. Using fluorescent derivatives of lactose, Galβ1,4GlcNAcβ and T-antigen (Galβ1,3GalNAcα) as acceptors, we tested eight different sialyltransferases and found that the Pasteurella multocida PM0188h and porcine ST3Gal1 sialyltransferases were significantly active with CMP-Leg5Ac7Ac, showing approximately 60% activity when compared with CMP-Neu5Ac. The Photobacterium α2,6 sialyltransferase was weakly active, with approximately 6% relative activity. The Leg5Ac7Ac-α-2,3-lactose product was then tested as a substrate with six sialidases of viral, bacterial and mammalian origin. All showed much lower activities than with the corresponding sialic acid substrate, with the influenza virus N1 being the most active and human NEU2 being the least active. These results show the feasibility of producing glycoconjugates with Leg5Ac7Ac residues as the terminal sugars, which should display novel biological properties.
sialyltransferase, sialic acid, legionaminic acid, glycoconjugate, neuraminidase
Structure type: monomer
Location inside paper: p.100, fig.2
Trivial name: UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose, UDP-2,4-diacetamido-Bacillose, UDP-N,N-diacetylbacillosamine, UPD-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose, UDP-N,N'-diacetyl-bacillosamine, UDP-Bac2Ac4Ac, UDP-diNAcBac
Compound class: nucleoside diphosphate sugar
Methods: DNA cloning, genetic methods, biochemical methods, CE-MS, CE
Biological activity: reactivity of Leg5Ac7Ac-Lac-FCHASE with sialidases
Enzymes that release or process the structure: PglD (acetyltransferase)
Biosynthesis and genetic data: genetic data, biochemical data
Synthetic data: enzymatic and chemoenzymatic
3D data: 3D data
Related record ID(s): 26388, 27009, 27010
NCBI Taxonomy refs (TaxIDs): 197,
446
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There is only one chemically distinct structure:
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