Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 16740931Publication DOI: 10.1128/JB.00273-06Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: castric
duq.edu
Institutions: Department of Biological Sciences, Duquesne University, 600 Forbes Ave., Pittsburgh, PA 15282, USA, Department of Microbiology, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
The pilin of Pseudomonas aeruginosa 1244 is glycosylated with an oligosaccharide that is structurally identical to the O-antigen repeating unit of this organism. Concordantly, the metabolic source of the pilin glycan is the O-antigen biosynthetic pathway. The present study was conducted to investigate glycan substrate recognition in the 1244 pilin glycosylation reaction. Comparative structural analysis of O subunits that had been previously shown to be compatible with the 1244 glycosylation machinery revealed similarities among sugars at the presumed reducing termini of these oligosaccharides. We therefore hypothesized that the glycosylation substrate was within the sugar at the reducing end of the glycan precursor. Since much is known of PA103 O-antigen genetics and because the sugars at the reducing termini of the O7 (strain 1244) and O11 (strain PA103) are identical (β-N-acetyl fucosamine), we utilized PA103 and strains that express lipopolysaccharide (LPS) with a truncated O-antigen subunit to test our hypothesis. LPS from a strain mutated in the wbjE gene produced an incomplete O subunit, consisting only of the monosaccharide at the reducing end (β-D-N-acetyl fucosamine), indicating that this moiety contained substrate recognition elements for WaaL. Expression of pilAO(1244) in PA103 wbjE::aacC1, followed by Western blotting of extracts of these cells, indicated that pilin produced has been modified by the addition of material consistent with a single N-acetyl fucosamine. This was confirmed by analyzing endopeptidase-treated pilin by mass spectrometry. These data suggest that the pilin glycosylation substrate recognition features lie within the reducing-end moiety of the O repeat and that structures of the remaining sugars are irrelevant.
Lipopolysaccharide, O-antigen, Pseudomonas aeruginosa, recognition, pilin, glycosylation
Structure type: oligomer
Location inside paper: p.4247, fig.1
Aglycon: Und-PP
Trivial name: O-unit
Contained glycoepitopes: IEDB_130648,IEDB_136045,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_146664,IEDB_152214,IEDB_174333,IEDB_885822,IEDB_983931,SB_192,SB_86
Methods: MALDI-TOF MS, genetic methods
Biological activity: serological data
Biosynthesis and genetic data: genetic data, biosynthetic data
Related record ID(s): 20047, 20329, 20330, 20331, 20332, 20333, 20334
NCBI Taxonomy refs (TaxIDs): 1045010Reference(s) to other database(s): GTC:G71952BR, GlycomeDB:
27935
Show glycosyltransferases
There is only one chemically distinct structure:
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