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Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes

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. Ag...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773886/
https://www.ncbi.nlm.nih.gov/pubmed/33409472
http://dx.doi.org/10.1016/j.isci.2020.101919
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author 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
author_facet 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
author_sort Murphy, Paul V.
collection PubMed
description 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.
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spelling pubmed-77738862021-01-05 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 Medrano, Francisco J. Kaltner, Herbert Kopitz, Jürgen Bovin, Nicolai V. Wu, Albert M. Klein, Michael L. Percec, Virgil Gabius, Hans-Joachim iScience Article 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. Elsevier 2020-12-10 /pmc/articles/PMC7773886/ /pubmed/33409472 http://dx.doi.org/10.1016/j.isci.2020.101919 Text en © 2020 The Author(s) http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
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
Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title_full Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title_fullStr Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title_full_unstemmed Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title_short Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
title_sort probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773886/
https://www.ncbi.nlm.nih.gov/pubmed/33409472
http://dx.doi.org/10.1016/j.isci.2020.101919
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