Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling
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 glycoc...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2017
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| Online Access: | http://hdl.handle.net/1721.1/106952 https://orcid.org/0000-0003-3761-3743 https://orcid.org/0000-0002-5749-7869 |
| _version_ | 1811070606101184512 |
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| author | Lukose, Vinita Whitworth, Garrett Guan, Ziqiang Imperiali, Barbara |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Lukose, Vinita Whitworth, Garrett Guan, Ziqiang Imperiali, Barbara |
| author_sort | Lukose, Vinita |
| collection | MIT |
| description | 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 |
| first_indexed | 2024-09-23T08:38:47Z |
| format | Article |
| id | mit-1721.1/106952 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T08:38:47Z |
| publishDate | 2017 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/1069522022-09-23T13:33:20Z Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling Lukose, Vinita Whitworth, Garrett Guan, Ziqiang Imperiali, Barbara Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Lukose, Vinita Whitworth, Garrett Imperiali, Barbara 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 National Institutes of Health (U.S.) (Grant GM-039334) Natural Sciences and Engineering Research Council of Canada (Fellowship) 2017-02-16T14:55:48Z 2017-02-16T14:55:48Z 2015-09 2015-07 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/106952 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 https://orcid.org/0000-0003-3761-3743 https://orcid.org/0000-0002-5749-7869 en_US http://dx.doi.org/10.1021/jacs.5b07146 Journal of the American Chemical Society 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. application/pdf American Chemical Society (ACS) ACS |
| spellingShingle | Lukose, Vinita Whitworth, Garrett Guan, Ziqiang Imperiali, Barbara Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title | Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title_full | Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title_fullStr | Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title_full_unstemmed | Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title_short | Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling |
| title_sort | chemoenzymatic assembly of bacterial glycoconjugates for site specific orthogonal labeling |
| url | http://hdl.handle.net/1721.1/106952 https://orcid.org/0000-0003-3761-3743 https://orcid.org/0000-0002-5749-7869 |
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