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Functional Aspects of Lectins
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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 6220

Special Issue Editor

Prof. Dr. Monica Fengsrud Brinchmann

E-Mail Website
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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

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 3277
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 6 | Viewed by 2701
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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