Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
Publication DOI: 10.1186/s12934-016-0538-zJournal NLM ID: 101139812Publisher: London: BioMed Central
Correspondence: chenmin
sdu.edu.cn; xianweiliu
sdu.edu.cn
Institutions: The Institute of Medical Molecular Genetics, Department of Biochemistry and Molecular Biology, Bin Zhou Medical University, No. 346, Guan Hai Road, Lai Shan District, Yan Tai City, Shan Dong Province, 264003, People's Republic of China, The State Key Laboratory of Microbial Technology, National Glycoengineering Research Center, School of Life Sciences and Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, Shandong, 250100, People's Republic of China
BACKGROUND: In the process of ABO-incompatible (ABOi) organ transplantation, removal of anti-A and/or B antibodies from blood plasma is a promising method to overcome hyperacute rejection and allograft loss caused by the immune response between anti-A and/or B antibodies and the A and/or B antigens in the recipient. Although there are commercial columns to do this work, the application is still limited because of the high production cost. RESULTS: In this study, the PglB glycosylation pathway from Campylobacter jejuni was exploited to produce glycoprotein conjugated with Escherichia coli O86:B7 O-antigen, which bears the blood group B antigen epitope to absorb blood group B antibody in blood. The titers of blood group B antibody were reduced to a safe level without changing the clotting function of plasma after glycoprotein absorption of B antibodies in the plasma. CONCLUSIONS: We developed a feasible strategy for the specific adsorption/removal of blood group antibodies. This method will be useful in ABOi organ transplantation and universal blood transfusion.
PglB, blood group B antigen, Conjugated glycoprotein, E.coli O-antigen, Immunoadsorption
Structure type: suggested polymer biological repeating unit
Location inside paper: fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_140125,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_149558,IEDB_150766,IEDB_150948,IEDB_150952,IEDB_151528,IEDB_152212,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461718,IEDB_461719,IEDB_549285,IEDB_885822,IEDB_918314,SB_148,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_87,SB_88
Methods: SDS-PAGE, ELISA, Western blotting, MALDI-TOF MS, serological methods, genetic methods, statistical analysis, binding assays, conjugation
Biological activity: binding of anti-B antibody to MBPmut-OPS (MBP is maltose-binding protein) from E. coli O86:B7
Related record ID(s): 10715, 11314, 20507, 21563, 22686, 30311
NCBI Taxonomy refs (TaxIDs): 2162909Reference(s) to other database(s): GTC:G64231CD, GlycomeDB:
27794
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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