Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 18842005Publication DOI: 10.1021/bi801067sJournal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: csc
chem.wayne.edu; wang.892
osu.edu
Institutions: Department of Chemistry, Wayne State UniVersity, Detroit, Michigan 48202, and Department of Biochemistry, The Ohio State UniVersity, Columbus, Ohio 43210
Escherichia coli O86 possesses high human blood group B activity because of its O-antigen structure, sharing the human blood group B epitope. In this study, the wbwK gene of E. coli O86:B7 was expressed and purified as the GST fusion protein. Thereafter, the wbwK gene was biochemically identified to encode an α1,2-fucosyltransferase through radioactivity assays, as well as mass spectrometry and NMR spectroscopy. WbwK shows strict substrate specificity and only recognizes Galβ1,3GalNAcα-OR (T-antigen and derivatives) as the acceptor to generate the H-type 3 blood group antigen. In contrast to other α1,2-fucosyltransferases, WbwK does not display activity toward the simple substrate Galβ-OMe. Comparison with another recently characterized α1,2-fucosyltransferase (WbsJ) of E. coli O128:B12 indicates a low level of amino acid identity between them; however, they share a common acceptor substrate, Galβ1,3GalNAcα-OR. Domain swapping between WbwK and WbsJ revealed that the smaller variable domains located in the C-terminus determine substrate specificity, whereas the larger variable domain in the N-terminus might play a role in forming the correct conformation for substrate binding or for localization of the α1,2-fucosyltransferase involved in O-antigen biosynthesis. In addition, milligram scale biosynthesis of the H-type 3 blood group antigen was explored using purified recombinant WbwK. WbwK may have potential applications in masking T-antigen, the tumor antigen, in vivo
biosynthesis, gene, O-antigen, Escherichia coli, epitope, Substrate Specificity, T-Antigen, human blood group B
Structure type: oligomer
Location inside paper: p. 11591, fig.S1
Trivial name: fucosylated trisaccharide
Contained glycoepitopes: IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_144562,IEDB_149554,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,SB_100,SB_137,SB_154,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88
Methods: 13C NMR, 1H NMR, ESI-MS, NMR-1D, serological methods, genetic methods, biochemical methods
Enzymes that release or process the structure: WbwK a1,2-fucosyltransferase
Biosynthesis and genetic data: genetic data
Synthetic data: enzymatic
Related record ID(s): 22686, 23041
NCBI Taxonomy refs (TaxIDs): 2162909Reference(s) to other database(s): GlycomeDB:
443
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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