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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/61471
Aeromonas surface glucan attached throught the O-antigen ligase represents a new way to obtain UDP-Glucose
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We previously reported that A. hydrophila GalU mutants were still able to produce UDP-glucose introduced as a glucose residue in their lipopolysaccharide core. In this study, we found the unique origin of this UDP-glucose from a branched α-glucan surface polysaccharide. This glucan, surface attached through the O-antigen ligase (WaaL), is common to the mesophilic Aeromonas strains tested. The Aeromonas glucan is produced by the action of the glycogen synthase (GlgA) and the UDP-Glc pyrophosphorylase (GlgC), the latter wrongly indicated as an ADP-Glc pyrophosphorylase in the Aeromonas genomes available. The Aeromonas glycogen synthase is able to react with UDP or ADP-glucose, which is not the case of E. coli glycogen synthase only reacting with ADP-glucose. The Aeromonas surface glucan has a role enhancing biofilm formation. Finally, for the first time to our knowledge, a clear preference on behalf of bacterial survival and pathogenesis is observed when choosing to produce one or other surface saccharide molecules to produce (lipopolysaccharide core or glucan).
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MERINO MONTERO, Susana, et al. Aeromonas surface glucan attached throught the O-antigen ligase represents a new way to obtain UDP-Glucose. PLoS One. 2012. Vol. 7, num. 5, pags. e35707. ISSN 1932-6203. [consulted: 17 of June of 2026]. Available at: https://hdl.handle.net/2445/61471