Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
Murphy, Paul V. Romero, Antonio Xiao, Qi Ludwig, Anna-Kristin Jogula, Srinivas Shilova, Nadezhda V. Singh, Tanuja Gabba, Adele Javed, Bilal Zhang, Dapeng
Murphy, Paul V.
Romero, Antonio
Xiao, Qi
Ludwig, Anna-Kristin
Jogula, Srinivas
Shilova, Nadezhda V.
Singh, Tanuja
Gabba, Adele
Javed, Bilal
Zhang, Dapeng
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Publication Date
2021-01-22
Type
Article
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Citation
Murphy, Paul V., Romero, Antonio, Xiao, Qi, Ludwig, Anna-Kristin, Jogula, Srinivas, Shilova, Nadezhda V., Singh, Tanuja, Gabba, Adele, Javed, Bilal, Zhang, Dapeng, Medrano, Francisco J., Kaltner, Herbert, Kopitz, Jürgen, Bovin, Nicolai V., Wu, Albert M., Klein, Michael L., Percec, Virgil, Gabius, Hans-Joachim. (2021). Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes. iScience, 24(1), 101919. doi:https://doi.org/10.1016/j.isci.2020.101919
Abstract
The small 3-O-sulfated galactose head group of sulfatides, an abundant glycosphingolipid class, poses the (sphinx-like) riddle on involvement of glycan bridging by tissue lectins (sugar code). First, synthesis of head group derivatives for functionalization of amphiphilic dendrimers is performed. Aggregation of resulting (biomimetic) vesicles, alone or in combination with lactose, demonstrates bridging by a tissue lectin (galectin-4). Physiologically, this can stabilize glycolipid-rich microdomains (rafts) and associate sulfatide-rich regions with specific glycoproteins. Further testing documents importance of heterobivalency and linker length. Structurally, sulfatide recognition by galectin-8 is shown to involve sphingosine's OH group as substitute for the 3′-hydroxyl of glucose of lactose. These discoveries underscore functionality of this small determinant on biomembranes intracellularly and on the cell surface. Moreover, they provide a role model to examine counterreceptor capacity of more complex glycans of glycosphingolipids and to start their bottom-up glycotope surface programming.
Publisher
Cell Press
Publisher DOI
10.1016/j.isci.2020.101919
Rights
Attribution 4.0 International (CC BY 4.0)