Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Pseudomonas aeruginosa [ICD11:
XN5L6 
];
infection due to Bordetella pertussis [ICD11:
XN23B ]
The structure was elucidated in this paperNCBI PubMed ID: 18621892Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: jlam
uoguelph.ca
Institutions: Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada, School of Clinical Veterinary Science, University of Bristol, Langford, Bristol, UK, Department of Biological Chemistry, John Innes Centre, Norwich, UK
Pseudomonas aeruginosa and Bordetella pertussis produce lipopolysaccharide (LPS) that contains 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid (D-ManNAc3NAcA). A five-enzyme biosynthetic pathway that requires WbpA, WbpB, WbpE, WbpD and WbpI has been proposed for the production of this sugar in P. aeruginosa, based on analysis of genes present in the B-band LPS biosynthesis cluster. In the analogous B. pertussis cluster, homologs of wbpB-I are present but a putative dehydrogenase was missing; therefore, the biosynthetic mechanism for UDP-D-ManNAc3NAcA was unclear. Non-polar knockout mutants of each P. aeruginosa gene were constructed. Complementation analysis of the mutants demonstrated that B-band LPS production was restored to P. aeruginosa knockout mutants when the relevant B. pertussis genes were supplied in trans. Thus, the genes that encode the putative oxidase, transaminase, N-acetyltransferase, and epimerase enzymes in B. pertussis are functional homologs of those in P. aeruginosa. Two candidate dehydrogenase genes were located by searching the B. pertussis genome; these have 80% identity to P. aeruginosa wbpO (serotype O6) and 32% identity to wbpA (serotype O5). These genes, wbpO1629 and wbpO3150, were shown to complement a wbpA knockout in P. aeruginosa. Capillary electrophoresis was used to characterize the enzymatic activities of purified WbpO1629 and WbpO3150, and mass spectrometry analysis confirmed that the two enzymes are dehydrogenases capable of converting UDP-D-GlcNAc, to a lesser extent UDP-D-GalNAc, and to a much lesser extent, UDP-D-Glc. Together, these results suggest that B. pertussis produces UDP-D-ManNAc3NAcA through the same pathway proposed in P. aeruginosa, despite differences in the genomic context of the genes involved
Lipopolysaccharide, biosynthesis, Pseudomonas aeruginosa, gene cluster, Bordetella pertussis, WbpA, WbpI
Structure type: monomer
Location inside paper: p. 6061, fig. 1, UDP-D-GlcNAc3NAcA
Trivial name: UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid, UDP-ManNAc(3NAc)A, UDP-D-ManNAc3NAcA
Methods: MALDI-MS, Western blotting, genetic methods, biochemical methods, capillary electrophoresis (CE)
Enzymes that release or process the structure: WbPl / WlbD 2-epimerase
Biosynthesis and genetic data: genetic data, biochemical data
Synthetic data: enzymatic
Comments, role: Proposed substrate for biosynthesis of UDP-D-ManNAc3NAcA.
Related record ID(s): 21686, 22756, 23329, 23330, 23331, 23332, 24073, 24264, 25735
NCBI Taxonomy refs (TaxIDs): 287,
520
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There is only one chemically distinct structure:
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