Premium
Metabolic profiling of Helicobacter pylori glycosylation
Author(s) -
Koenigs Maria B.,
Dube Danielle H.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.695.4
Subject(s) - glycome , helicobacter pylori , glycosylation , glycan , azide , chemistry , glycobiology , biochemistry , pathogen , virulence , intracellular , microbiology and biotechnology , biology , gene , glycoprotein , genetics , organic chemistry
Helicobacter pylori is a pathogenic bacterium that causes duodenal ulcers and some gastric cancers. Recent studies have revealed that H. pylori contain a unique glycan that is linked directly to its virulence. Here we set out to further explore the glycobiology of H. pylori by profiling this pathogen's glycome. We employed a technique termed metabolic oligosaccharide engineering that has been utilized extensively to profile glycosylation of mammalian cells. H. pylori were grown in liquid culture supplemented with the unnatural azide‐containing sugar peracetylated N ‐azidoacetylglucosamine (Ac 4 GlcNAz). H. pylori cells and lysates were then probed via Staudinger ligation to assess azide incorporation. Western blotting reveals that azides are metabolically incorporated into several intracellular H. pylori proteins. Further experiments reveal that azide‐dependent signal is diminished by beta‐elimination but not by treatment with peptide‐ N ‐glycosidase‐F, suggesting that the azide is metabolically incorporated into O ‐linked glycans. Future work will further establish the metabolic fate of Ac 4 GlcNAz in H. pylori and the identity of labeled proteins. Support was provided by the HHMI and the Dreyfus Foundation.