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Glycobiology Advance Access originally published online on December 1, 2004
Glycobiology 2005 15(4):361-367; doi:10.1093/glycob/cwi019
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Glycobiology vol. 15 no. 4 © Oxford University Press 2004; all rights reserved.

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

Mihai Nita-Lazar1, Michael Wacker, Belinda Schegg, Saba Amber and Markus Aebi2

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

2 To whom correspondence should be addressed; e-mail: aebi{at}micro.biol.ethz.ch

Received on August 23, 2004; revised on November 16, 2004; accepted on November 28, 2004

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 homolog 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 N-linked 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.

Key words: AcrA / Campylobacter jejuni / glycoproteins / N-glycosylation


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