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

Yavuz, Elif ; Maffioli, Carola ; Ilg, Karin ; Aebi, Markus ; Priem, Bernard

In: Glycoconjugate Journal, 2011, vol. 28, no. 1, p. 39-47

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    Titel
    • Glycomimicry: display of fucosylation on the lipo-oligosaccharide of recombinant Escherichia coli K12
    Autor
    • Yavuz, Elif. CERMAV-CNRS, Grenoble, France
    • Maffioli, Carola. Institute of Microbiology, ETH, Zurich, Switzerland
    • Ilg, Karin. Institute of Microbiology, ETH, Zurich, Switzerland
    • Aebi, Markus. Institute of Microbiology, ETH, Zurich, Switzerland
    • Priem, Bernard. CERMAV-CNRS, Grenoble, France
    Dokumententyp
    • Postprint
    Sprache
    • Englisch
    Veröffentlicht in
    • Glycoconjugate Journal, 2011, vol. 28, no. 1, p. 39-47. Springer US; http://www.springer-ny.com
    Andere elektronische Ausgabe
    OAI-PMH-ID
    • oai:doc.rero.ch:322535
    Summary
    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 β-1,4 galactosyltransferase LgtE (Neisseria gonorrheae), the β-1,3 N-acetylglucosaminyltransferase LgtA and the β-1,3 galactosyltransferase LgtB from Neisseria meningitidis, as well as the α-1,2 and α-1,3 fucosyltransferases FutC and FutA from Helicobacter pylori. We show the display of the Lewis Y structure by immunological and chemical analysis