Abstract
The repeat units of heteropolymeric O antigen are synthesized at the cytosolic side of the inner bacterial membrane via the Wzx/Wzy-dependent assembly pathway. After being translocated across the membrane by Wzx, each repeat unit is polymerized by Wzy to form a glycan chain. In this study, we demonstrate the need of the corresponding enzyme transferring the initial HexNAc to undecaprenol phosphate (lipid carrier), together with the corresponding O-antigen polymerase (Wzy), to produce the Aeromonas hydrophila O:34-antigen. We suggest, the concerted action of WecA or P enzyme (UDP-HexNAc: polyprenol-P HexNAc-1-P transferase) and Wzy is involved in the mechanism responsible for the A. hydrophila O-antigen polymerization.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aeromonas hydrophila / enzymology*
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Aeromonas hydrophila / immunology
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Aeromonas hydrophila / pathogenicity
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Animals
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Bacterial Adhesion
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Bacterial Proteins / physiology
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Biosynthetic Pathways
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Cell Line, Tumor
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Female
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Glycosyltransferases / physiology
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Humans
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Mice
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O Antigens / biosynthesis*
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O Antigens / immunology
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Oncorhynchus mykiss
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Polymerization
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Virulence
Substances
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Bacterial Proteins
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O Antigens
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Glycosyltransferases
Grants and funding
This work was supported by Plan Nacional de I + D + i (Ministerio de Educación, Ciencia y Deporte and Ministerio de Sanidad, Spain) and from Generalitat de Catalunya (Centre de Referència en Biotecnologia). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.