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Glycobiology Advance Access published online on December 1, 2004
Glycobiology, doi:10.1093/glycob/cwi019
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Received August 23, 2004
Revised November 16, 2004
Accepted November 28, 2004

Article

The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation

Mihai Nita-Lazar 1, Michael Wacker 2, Belinda Schegg 2, Saba Amber 2, and Markus Aebi 2*

1 present address: Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215
2 Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland

* To whom correspondence should be addressed.
Markus Aebi, E-mail: aebi{at}micro.biol.ethz.ch


  Abstract

In the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homologue of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for Nlinked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes.

Keywords: Campylobacter jejuni/glycoproteins/N-glycosylation/AcrA..
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