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- Title
Aeromonas surface glucan attached through the O-antigen ligase represents a new way to obtain UDP-glucose.
- Authors
Merino, Susana; Bouamama, Lamiaa; Knirel, Yuriy A; Senchenkova, Sofya N; Regué, Miguel; Tomás, Juan M
- Abstract
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).
- Publication
PloS one, 2012, Vol 7, Issue 5, pe35707
- ISSN
1932-6203
- Publication type
Journal Article
- DOI
10.1371/journal.pone.0035707