Abstract
Wheat germ agglutinin (WGA) is a lectin composed of 4 homologous hevein domains. It has been shown that WGA binds N-acetyl glucosamine (GlcNAc)-related oligosaccharides and has applications as commercial reagent to detect glycans containing such modified residues. Peptidoglycan (PGN), the main component of the bacterial cell wall, is a polymeric material made of repeating disaccharide units of GlcNAc- N-acetylmuramic acid cross-linked with short polypeptide fragments. Wheat germ agglutinin is able to bind bacterial cells, a phenomenon that could correlate with its plant-defense capacities, but there is no information at the molecular level about how WGA binds to the PGN. Herein, we present structural data on the binding of a short PGN fragment to WGA by means of saturation transfer difference nuclear magnetic resonance studies. The results show that the GlcNAc residue establishes the major contacts with WGA, followed by the N-acetylmuramic acid residue. In contrast, the peptide moiety displays minor contacts at the binding site.
Highlights
Many plants express chitin-binding lectins that have been identified as plant-defense proteins
The hevein domain has become a powerful tool in several fields of biological research and its lectin properties have been extensively studied in the field of glycosciences.[1]
Because chitin is the major component of fungi cell walls as well as of invertebrates exoskeleton, the implication of these peptides in plant defense and antifungal activities has been associated with their lectin character as chitin ligands.[22]
Summary
Many plants express chitin-binding lectins that have been identified as plant-defense proteins.
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