Merolectins are composed of a single carbohydrate binding domain and are unable to precipitate glycoconjugates or cause cell agglutination [45]. Hololectins are exclusively composed of carbohydrate binding domains, containing two or more domains and being able to agglutinate cells and/or precipitate glycoconjugates [45]. Finally, chimerolectins are characterized by one or more carbohydrate binding domains and an additional domain responsible for another biological activity

(e.g. chitinase activity) [45]. Due to lectins’ functional plasticity, they are involved in numerous biological processes including defense against pathogens, symbiosis and cell signaling [12]. learn more Among pathogen defense functions, lectins can perform bactericidal [40], fungicidal [40] and [64] and antiviral activities [39]. Indeed, lectins have an enormous potential for developing

novel drugs, pesticides and/or transgenic organisms, since they can bind specifically to carbohydrates normally absent in vertebrates and plants, such as chitin or the bacterial cell wall peptidoglycan carbohydrate. Furthermore, by chitin targeting, several pests can be tackled, since chitin is the main component of the fungal cell wall and also of the exoskeleton of invertebrates, such as nematodes and insects [20] and [43]. Among the lectins, the hevein domain is extremely common, being found in chimerolectins, hololectins and merolectins (Fig. 1) [7]. The name ‘hevein’ was proposed by Archer in 1960 [4], when the first peptide with this domain was isolated from the latex of the rubber see more tree (Hevea brasiliensis). This domain is rarely found in proteins that do not belong to the plant kingdom. As an Fulvestrant solubility dmso exception, a protein containing an hevein domain from the phytopathogenic fungus Magnaporthe grisea was identified by Kamakura et al. [29] (GenBank ID: BAB79692.1). The overall hevein domain

structure is composed of an anti-parallel β-sheet and occasional short helices; the scaffold is stabilized by three to five disulfide bonds [40] and [64]. This structural framework exposes four amino acid residues (one serine and three aromatic) involved in chitin-binding and related oligomers [40] and [64]. The amino acid residues involved are arranged as follows, Xi-Xi+2-Xi+4-Xi+11, where the residue Xi is normally a serine residue and Xi+11, a tyrosine residue; Xi+2 and Xi+4 are normally an aromatic residue. The residues in Xi+2 and Xi+4 stabilize the complex through CH-π stacking. If the residues in Xi+2 and Xi+4 are tyrosine or tryptophan, they also contribute through hydrogen bonds [10]. Although the mechanism of action of hevein-like peptides has not been completely elucidated, it is known that hevein-like peptides are able to inhibit the development of chitin-containing fungi [37] and [40]. This fungicidal activity has been related to its chitin-binding domain, where the cell wall elongation is retarded or stopped after the chitin-binding step.