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Papers In Press, published online ahead of print April 25, 2003
J. Biol. Chem, 10.1074/jbc.M301273200
Submitted on February 5, 2003
Revised on April 25, 2003
Accepted on April 25, 2003

Detection of conserved N-linked glycans and phase variable lipo-oligosaccharides and capsules from campylobacter cells by mass spectrometry and high resolution magic angle spinning NMR spectroscopy

Christine M. Szymanski, Frank St. Michael, Harold C. Jarrell, Jianjun Li, Michel Gilbert, Suzon Larocque, Evgeny Vinogradov, and Jean-Robert Brisson

Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6

Corresponding Author: jean-robert.brisson{at}cnrc-nrc.gc.ca

Glycomics, the study of microbial polysaccharides and genes responsible for their formation, requires the continuous development of rapid and sensitive methods for the identification of glycan structures. In this study, methods for the direct analysis of sugars from 10**8-10**10 cells are outlined using the human gastrointestinal pathogen, Campylobacter jejuni. Using capillary-electrophoresis coupled with sensitive electrospray mass spectrometry, we demonstrate variability in the lipid A component of C. jejuni lipooligosaccharides (LOS). In addition, these sensitive methods have permitted the detection of phase variable LOS core structures that were not observed previously. High resolution magic angle spinning (HR-MAS) NMR was used to examine capsular polysaccharides from campylobacter whole cells and showed profiles similar to those observed for purified polysaccharides analyzed by solution NMR. This method also exhibited the potential for campylobacter serotyping, mutant verification, and preliminary sugar analysis. HR-MAS NMR examination of growth from individual colonies of C. jejuni NCTC11168 indicated that the capsular glycan modifications are also phase variable. These variants show different staining patterns on deoxycholate-PAGE and reactivity with immune sera. One of the identified modifications was a novel –OP=O(NH2)OMe phosphoramide, not observed previously in nature. In addition, HR-MAS NMR detected the N-linked glycan, GalNAc-a1,4-GalNAc-a1,4-[Glcb1,3-]GalNAc-a1,4-GalNAc-a1,4-GalNAc-a1,3-Bac, where Bac is 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose, in C. jejuni and C. coli. The presence of this common heptasaccharide in multiple campylobacter isolates demonstrates the conservation of this N-linked protein glycosylation pathway in this organism and describes the first report of HR-MAS NMR detection of N-linked glycans on glycoproteins from intact bacterial cells.


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