Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 27357519Publication DOI: 10.2217/fmb-2015-0028Journal NLM ID: 101278120Publisher: London: Future Medicine
Correspondence: jtomas
ub.edu
Institutions: Departamento de Microbiologia, Facultad de Biologia, Universidad de Barcelona, Diagonal 643, 08071 Barcelona, Spain, Institute of Virology, Hannover Medical School, Hannover, Germany
In the Wzx/Wzy-dependent assembled pathway, the assembled O-antigen repeat units are translocated from the cytosolic to the periplasmic face of the inner membrane by a Wzx translocase and then, polymerized by the integral membrane protein Wzy to form a glycan chain. We demonstrate that the activity of the Escherichia coli O-antigen polymerase (Wzy) is dependent on the first sugar of the O-antigen repeat unit to produce the O-antigen polymerization and therefore, there is a need for a concerted action with the enzyme transferring the initial HexNAc to undecaprenyl phosphate (UDP-HexNAc: polyprenol-P HexNAc-1-P transferase). Furthermore, in the case of Aeromonas hydrophila Wzy-O34 polymerization activity, the enzyme is permissive with the sugar at the nonreducing end of the O-antigen repeat unit.
Lipopolysaccharide, Escherichia coli, Aeromonas hydrophila, O-antigen polymerization, Wzy O-antigen assembly pathway
Structure type: suggested polymer biological repeating unit
Location inside paper: p.907, fig.1C
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_133754,IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_142488,IEDB_143253,IEDB_146664,IEDB_151531,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: PCR, GC-MS, SDS-PAGE, DNA techniques, acid hydrolysis, GLC, genetic methods, computer sequence analysis
Biosynthesis and genetic data: topology of O-antigen polymerases (Wzy)
Related record ID(s): 11356, 11786, 11788, 11789, 21743, 23079
NCBI Taxonomy refs (TaxIDs): 2067427
Show glycosyltransferases
There is only one chemically distinct structure:
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