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Functional Aspects of Lectins

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Macromolecular Chemistry".

Deadline for manuscript submissions: closed (31 December 2019) | Viewed by 6897

Special Issue Editor


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Guest Editor
Faculty of Biosciences and Aquaculture, Nord University, 8049 Bodø, Norway
Interests: molecular cell biology; immunology; mucosal surfaces; lectins

Special Issue Information

Dear Colleagues,

Lectins are sugar-binding proteins important for control and fine-tuning of biological processes, both intracellularly and extracellularly. These proteins are found ubiquitously in a wide range of organisms from single cell bacteria to multicellular animals and plants, and in viruses. Lectins are important in, for example, the immune system, cell cycle control, and development. At the molecular level, lectin interactions are involved in RNA splicing, apoptosis, autophagy, cell-cell communication, and pathogen interaction, among others.

In this timely Special Issue, articles and reviews on the functional aspects of lectins will be welcome. Relevant topics could be the ones listed in the keywords; however, any functional aspects of lectins are of interest.

Prof. Monica Fengsrud Brinchmann
Guest Editor

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Keywords

  • Lectins
  • Immunology
  • Inflammation
  • Pathogen recognition receptors
  • Hemagglutination
  • Cell–cell interaction
  • Cell cycle/cancer
  • Cell signalling
  • Endocytosis/phagocytosis
  • Autophagy
  • Protein folding

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Published Papers (2 papers)

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Research

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17 pages, 3151 KiB  
Article
Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
by Son Thai Le, Lenka Malinovska, Michaela Vašková, Erika Mező, Viktor Kelemen, Anikó Borbás, Petr Hodek, Michaela Wimmerová and Magdolna Csávás
Molecules 2019, 24(12), 2262; https://doi.org/10.3390/molecules24122262 - 18 Jun 2019
Cited by 7 | Viewed by 3595
Abstract
Series of multivalent α-l-fucoside containing glycoclusters and variously decorated l-fucosides were synthesized to find potential inhibitors of fucose-specific lectins and study the structure-binding affinity relationships. Tri- and tetravalent fucoclusters were built using copper-mediated azide-alkyne click chemistry. Series of fucoside monomers [...] Read more.
Series of multivalent α-l-fucoside containing glycoclusters and variously decorated l-fucosides were synthesized to find potential inhibitors of fucose-specific lectins and study the structure-binding affinity relationships. Tri- and tetravalent fucoclusters were built using copper-mediated azide-alkyne click chemistry. Series of fucoside monomers and dimers were synthesized using various methods, namely glycosylation, an azide-alkyne click reaction, photoinduced thiol-en addition, and sulfation. The interactions between compounds with six fucolectins of bacterial or fungal origin were tested using a hemagglutination inhibition assay. As a result, a tetravalent, α-l-fucose presenting glycocluster showed to be a ligand that was orders of magnitude better than a simple monosaccharide for tested lectins in most cases, which can nominate it as a universal ligand for studied lectins. This compound was also able to inhibit the adhesion of Pseudomonas aeruginosa cells to human epithelial bronchial cells. A trivalent fucocluster with a protected amine functional group also seems to be a promising candidate for designing glycoconjugates and chimeras. Full article
(This article belongs to the Special Issue Functional Aspects of Lectins)
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Review

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15 pages, 1755 KiB  
Review
Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties
by Irina Chikalovets, Alina Filshtein, Valentina Molchanova, Tatyana Mizgina, Pavel Lukyanov, Olga Nedashkovskaya, Kuo-Feng Hua and Oleg Chernikov
Molecules 2020, 25(1), 150; https://doi.org/10.3390/molecules25010150 - 30 Dec 2019
Cited by 7 | Viewed by 3019
Abstract
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil [...] Read more.
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers. Full article
(This article belongs to the Special Issue Functional Aspects of Lectins)
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