Abstract
Lectins are proteins with a remarkably high affinity and specificity for carbohydrates. Many organisms naturally produce them, including animals, plants, fungi, protists, bacteria, archaea, and viruses. The present report focuses on lectins produced by marine or freshwater organisms, in particular algae and cyanobacteria. We explore their structure, function, classification, and antimicrobial properties. Furthermore, we look at the expression of lectins in heterologous systems and the current research on the preclinical and clinical evaluation of these fascinating molecules. The further development of these molecules might positively impact human health, particularly the prevention or treatment of diseases caused by pathogens such as human immunodeficiency virus, influenza, and severe acute respiratory coronaviruses, among others.
Highlights
Site-directed mutagenesis demonstrated that a single deglycosylation at N295 or N448 in HIV-1 isolates resulted in remarkable resistance to GRFT
Glycoprotein C and glycoprotein B bind to heparan sulfate on the cell surface to start the process of viral attachment to host cells
The participation of viral glycoproteins, highly glycosylated, is fundamental for the successful attachment and entry to target cells. These glycoproteins have been described as potential targets for lectins, such as GRFT, that can interfere with viral entry
Summary
The Latin root for “lectin” means to choose or select, an appropriate meaning given that lectins are proteins that “choose”: to bind carbohydrates in glycolipids or glycoproteins and that the interaction of lectins with carbohydrates can be very selective and as specific as the antigen/antibody interactions. The three-dimensional structures of these proteins and their binding to carbohydrates can be very different among various lectins. Several X-ray crystal structures of GRFT in complex with monosaccharides and disaccharides have been solved These include mannose (PDB IDs 2GUC, 2GUD, and 3LL2), N-acetylglucosamine (PDB ID 2GUE), 1→ 6α−mannobiose (PDB ID 2HYQ), and maltose (PDB ID 2HYR) [6,7,8]. GRFT mannose-binding site encloses Tyr and Asp residues in which both amino acids form. Six carbohydrate (mannose)-binding sites are shown; three for each monomer. Six carbohydrate (mannose)-binding sites are shown; threeinfor yellowdomain-swapped and purple, respectively. Right-Panel: Magnification of the GRFT six mannose-binding sites shown the each pres- monomer. GRFT-Mannoses main interactions hydrogen yellow and ence purple, Magnification of the GRFT six mannose-binding sitesviashown in the presence bonds are shown as yellow dashed lines. The three GRFT mannose-binding sites together form an almost perfect equilateral triangle
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