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Abstract
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.
Acknowledgements
The authors would like to thank Maite Polo for her technical assistance and the Servicios Científico-Técnicos from University of Barcelona.
Financial & competing interests disclosure
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 authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed. No writing assistance was utilized in the production of this manuscript.
No writing assistance was utilized in the production of this manuscript.