Glycomimicry: display of fucosylation on the lipo-oligosaccharide of recombinant Escherichia coli K12

We recently described the design of Escherichia coli K12 and Salmonella enterica sv Typhimurium to display the gangliomannoside 3 (GM3) antigen on the cell surface [1]. We report here the fucosylation of modified lipooligosaccharide in a recombinant E.coli strain with a truncated lipid A core due to deletion of the core glycosyltransferases genes waaO and waaB. This truncated structure was used as a scaffold to assemble the Lewis Y motif by consequent action of the heterologously expressed beta-1,4 galactosyltransferase LgtE (Neisseria gonorrheae), the beta-1,3 N-acetylglucosaminyltransferase LgtA and the beta-1,3 galactosyltransferase LgtB from Neisseria meningitidis, as well as the alpha-1,2 and alpha-1,3 fucosyltransferases FutC and FutA from Helicobacter pylori. We show the display of the Lewis Y structure by immunological and chemical analysis.