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Overview of the Structure–Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi

Authors
  • Barre, Annick
  • Bourne, Yves
  • Van Damme, Els J. M.
  • Rougé, Pierre
Type
Published Article
Journal
International Journal of Molecular Sciences
Publisher
MDPI AG
Publication Date
Jan 10, 2019
Volume
20
Issue
2
Identifiers
DOI: 10.3390/ijms20020254
PMID: 30634645
PMCID: PMC6359319
Source
PubMed Central
Keywords
License
Green

Abstract

To date, a number of mannose-binding lectins have been isolated and characterized from plants and fungi. These proteins are composed of different structural scaffold structures which harbor a single or multiple carbohydrate-binding sites involved in the specific recognition of mannose-containing glycans. Generally, the mannose-binding site consists of a small, central, carbohydrate-binding pocket responsible for the “broad sugar-binding specificity” toward a single mannose molecule, surrounded by a more extended binding area responsible for the specific recognition of larger mannose-containing N -glycan chains. Accordingly, the mannose-binding specificity of the so-called mannose-binding lectins towards complex mannose-containing N -glycans depends largely on the topography of their mannose-binding site(s). This structure–function relationship introduces a high degree of specificity in the apparently homogeneous group of mannose-binding lectins, with respect to the specific recognition of high-mannose and complex N -glycans. Because of the high specificity towards mannose these lectins are valuable tools for deciphering and characterizing the complex mannose-containing glycans that decorate both normal and transformed cells, e.g., the altered high-mannose N -glycans that often occur at the surface of various cancer cells.

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