Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 20801103Publication DOI: 10.1016/j.bbrc.2010.08.087Journal NLM ID: 0372516Publisher: Academic Press
Correspondence: P.G. Wang <Wang.892
osu.edu>
Institutions: Departments of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA
Escherichia coli O127:K63(B8) possesses high human blood group H (O) activity due to its O-antigen repeating unit structure. In this work, the wbiQ gene from E. coli O127:K63(B8) was expressed in E. coli BL21 (DE3) and purified as a fusion protein containing an N-terminal GST affinity tag. Using the GST-WbiQ fusion protein, the wbiQ gene was identified to encode an α1,2-fucosyltransferase using a radioactivity based assay, thin-layer chromatography assay, as well confirming product formation by using mass spectrometry and NMR spectroscopy. The fused enzyme (GST-WbiQ) has an optimal pH range from 6.5 to 7.5 and does not require the presence of a divalent metal to be enzymatically active. WbiQ displays strict substrate specificity, displaying activity only towards acceptors that contain Gal-β1,3-GalNAc-α-OR linkages; indicating that both the Gal and GalNAc residues are vital for enzymatic activity. In addition, WbiQ was used to prepare the H-type 3 blood group antigen, Fuc-α1,2-Gal-β1,3-GalNAc-α-OMe, on a milligram scale.
O-antigen, Escherichia coli, fucosyltransferase, WbiQ
Structure type: polymer chemical repeating unit
Location inside paper: p.191, fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_150766,IEDB_150948,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461719,IEDB_885822,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_88
Methods: 13C NMR, 1H NMR, SDS-PAGE, ESI-MS, Western blotting, genetic methods, biochemical methods, cloning
Biosynthesis and genetic data: fucosyltransferase activity data
Synthetic data: enzymatic
Related record ID(s): 7241, 10220, 20680, 25807, 108675, 117352
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G68080NF, GlycomeDB:
3548
Show glycosyltransferases
There is only one chemically distinct structure:
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