Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity

Gao, Chao and Stavenhagen, Kathrin and Eckmair, Barbara and McKitrick, Tanya R. and Mehta, Akul Y. and Matsumoto, Yasuyuki and McQuillan, Alyssa M. and Hanes, Melinda S. and Eris, Deniz and Baker, Kelly J. and Jia, Nan and Wei, Mohui and Heimburg-Molinaro, Jamie and Ernst, Beat and Cummings, Richard D.. (2021) Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity. Science Advances, 7 (24). eabf6834.

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The recognition of oligomannose-type glycans in innate and adaptive immunity is elusive due to multiple closely related isomeric glycan structures. To explore the functions of oligomannoses, we developed a multifaceted approach combining mass spectrometry assignments of oligomannose substructures and the development of a comprehensive oligomannose microarray. This defined microarray encompasses both linear and branched glycans, varying in linkages, branching patterns, and phosphorylation status. With this resource, we identified unique recognition of oligomannose motifs by innate immune receptors, including DC-SIGN, L-SIGN, Dectin-2, and Langerin, broadly neutralizing antibodies against HIV gp120,; N; -acetylglucosamine-1-phosphotransferase, and the bacterial adhesin FimH. The results demonstrate that each protein exhibits a unique specificity to oligomannose motifs and suggest the potential to rationally design inhibitors to selectively block these protein-glycan interactions.
Faculties and Departments:05 Faculty of Science > Departement Pharmazeutische Wissenschaften > Ehemalige Einheiten Pharmazie > Molekulare Pharmazie (Ernst)
UniBasel Contributors:Ernst, Beat and Eris, Deniz
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:06 Sep 2021 08:39
Deposited On:06 Sep 2021 08:39

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