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Glycosylation of the Self-Recognizing Escherichia coli Ag43 Autotransporter Protein

Centre for Biomedical Microbiology, BioCentrum-DTU, Technical University of Denmark, Lyngby, Denmark,¹ Institut für Molekulare Infektionsbiologie, Universität Würzburg, Röntgenring Würzburg, Germany,² Department of Life Sciences, Aalborg University, Aalborg, Denmark³

Received 11 October 2005/ Accepted 10 December 2005

Glycosylation is a common modulation of protein function in eukaryotes and is biologically important. However, in bacteria protein glycosylation is rare, and relatively few bacterial glycoproteins are known. In Escherichia coli only two glycoproteins have been described to date. Here we introduce a novel member to this exclusive group, namely, antigen 43 (Ag43), a self-recognizing autotransporter protein. By mass spectrometry Ag43 was demonstrated to be glycosylated by addition of heptose residues at several positions in the passenger domain. Glycosylation of Ag43 by the action of the Aah and TibC glycosyltransferases was observed in laboratory strains. Importantly, Ag43 was also found to be glycosylated in a wild-type strain, suggesting that Ag43-glycosylation may be a widespread phenomenon. Glycosylation of Ag43 does not seem to interfere with its self-associating properties. However, the glycosylated form of Ag43 enhances bacterial binding to human cell lines, whereas the nonglycosylated version of Ag43 does not to confer this property.

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