Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
Publication DOI: 10.3389/fimmu.2014.00492Journal NLM ID: 101560960Publisher: Lausanne: Frontiers Research Foundation
Correspondence: brockhau
queensu.ca
Institutions: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, Canada, Department of Biomedical and Molecular Sciences, Queen's University, 18 Stuart Street, Kingston, ON K7L3N6
Bacterial glycosyltransferases (GT) often synthesize the same glycan linkages as mammalian GT; yet, they usually have very little sequence identity. Nevertheless, enzymatic properties, folding, substrate specificities, and catalytic mechanisms of these enzyme proteins may have significant similarity. Thus, bacterial GT can be utilized for the enzymatic synthesis of both bacterial and mammalian types of complex glycan structures. A comparison is made here between mammalian and bacterial enzymes that synthesize epitopes found in mammalian glycoproteins, and those found in the O antigens of Gram-negative bacteria. These epitopes include Thomsen-Friedenreich (TF or T) antigen, blood group O, A, and B, type 1 and 2 chains, Lewis antigens, sialylated and fucosylated structures, and polysialic acids. Many different approaches can be taken to investigate the substrate binding and catalytic mechanisms of GT, including crystal structure analyses, mutations, comparison of amino acid sequences, NMR, and mass spectrometry. Knowledge of the protein structures and functions helps to design GT for specific glycan synthesis and to develop inhibitors. The goals are to develop new strategies to reduce bacterial virulence and to synthesize vaccines and other biologically active glycan structures.
glycosyltransferases, protein structure, specificities, glycoprotein epitopes, glycan mimics
Structure type: suggested polymer biological repeating unit
Location inside paper: p.492-7
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_97
Comments, role: review article
Related record ID(s): 8632, 20671, 25692, 30045, 30153, 30209, 30210, 30211, 30212, 30213, 30214, 30215, 30216, 30217, 30218, 30219, 30220, 30221, 30222, 30223, 30224, 108671
NCBI Taxonomy refs (TaxIDs): 2072453Reference(s) to other database(s): GTC:G18884UL, GlycomeDB:
3545
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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