Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling
Name
Imperiali_Chemoenzymatic Assembly.pdf
Size
906.75 KB
Format
Adobe PDF
Checksum (MD5)
8b8bfa4d53aa0d9dd31cd68b70a7faa9
Author(s)
Lukose, Vinita
Whitworth, Garrett
Guan, Ziqiang
Imperiali, Barbara
Date Issued
September 2015
Journal
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
Abstract
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
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/jacs.5b07146
