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UniLectin, A One‐Stop‐Shop to Explore and Study Carbohydrate‐Binding Proteins

Abstract : All eukaryotic cells are covered with a dense layer of glycoconjugates, and the cell walls of bacteria are made of various polysaccharides, putting glycans in key locations for mediating protein-protein interactions at cell interfaces. Glycan function is therefore mainly defined as binding to other molecules, and lectins are proteins that specifically recognize and interact non-covalently with glycans. UniLectin was designed based on insight into the knowledge of lectins, their classification, and their biological role. This modular platform provides a curated and periodically updated classification of lectins along with a set of comparative and visualization tools, as well as structured results of screening comprehensive sequence datasets. UniLectin can be used to explore lectins, find precise information on glycan-protein interactions, and mine the results of predictive tools based on HMM profiles. This usage is illustrated here with two protocols. The first one highlights the fine-tuned role of the O blood group antigen in distinctive pathogen recognition, while the second compares the various bacterial lectin arsenals that clearly depend on living conditions of species even in the same genus.
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https://hal.archives-ouvertes.fr/hal-03452596
Contributor : Anne Imberty Connect in order to contact the contributor
Submitted on : Saturday, November 27, 2021 - 9:12:38 AM
Last modification on : Tuesday, January 4, 2022 - 6:13:56 AM
Long-term archiving on: : Monday, February 28, 2022 - 6:18:02 PM

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Anne Imberty, François Bonnardel, Frédérique Lisacek. UniLectin, A One‐Stop‐Shop to Explore and Study Carbohydrate‐Binding Proteins. Current Protocols, Wiley, 2021, 1 (11), ⟨10.1002/cpz1.305⟩. ⟨hal-03452596⟩

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