Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling
Author(s)
Lukose, Vinita; Whitworth, Garrett; Guan, Ziqiang; Imperiali, Barbara
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The cell surfaces of bacteria are replete with diverse glycoconjugates that play pivotal roles in determining how bacteria interact with the environment
and the hosts that they colonize. Studies to advance our understanding of these interactions rely on the availability of chemically defined glycoconjugates that can be selectively modified under orthogonal reaction conditions to serve as discrete ligands to probe biological interactions,
in displayed arrays and as imaging agents. Herein, enzymes in the N-linked protein glycosylation (Pgl) pathway of Campylobacter jejuni are evaluated for their tolerance for azide-modified UDP-sugar substrates, including derivatives of 2,4-diacetamidobacillosamine and N-acetylgalactosamine. In vitro analyses reveal that chemoenzymatic approaches are useful for the preparation of undecaprenol diphosphate-linked glycans and glycopeptides with site-specific introduction of azide functionality for orthogonal labeling at three specific sites in the heptasaccharide glycan. The uniquely modified glycoconjugates represent valuable tools for investigating the roles of C. jejuni cell surface glycoconjugates in host pathogen interactions
Date issued
2015-09Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of ChemistryJournal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Lukose, Vinita et al. “Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling.” Journal of the American Chemical Society 137.39 (2015): 12446–12449. © 2015 American Chemical Society
Version: Final published version
ISSN
0002-7863
1520-5126