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Several plant lectins are known as potent immunomodulatory agents, and they are applied in different experimental models of infection (Afonso-Cardoso et al., [@B1]; Oliveira et al., [@B13]). Recent research has characterized these proteins as potential agonists of Toll-like receptors (TLRs or TLR), a family of mammalian homologs of *Drosophila* Toll protein involved in the detection of microbes and initiating inflammatory responses (O\'Neill et al., [@B14]). In this opinion article, we highlighted some studies of plant lectins as modulators or agonists of TLRs in order to stimulate research interest in this fascinating area and promote knowledge sharing and scientific collaboration. A short view on plant lectins ============================= Lectins are a very large class of carbohydrate-binding proteins of non-immune origin. Through the interaction with sugars, they trigger several important cellular processes. Lectins are universally expressed and have been shown to function in animals, plants, and microorganisms as cell and molecular recognition proteins. However, the carbohydrate-binding domains have been studied most intensively within the plant kingdom (Sharon, [@B16]; Vandenborre et al., [@B20]). The discovery of plant lectins occurred in the 19th century, however, many questions about the biological role of these molecules remain obscure. Lectins may be involved in sugar transport, carbohydrate storage and they are associated as molecular chaperones (Van Damme et al., [@B18a]; Liu and Li, [@B10]). The adhesion and agglutination properties of lectins have been related in the interaction of both symbiotic and pathogenic interaction of some microorganisms and host (Audfray et al., [@B2]). Plant lectins represent a group of proteins with obvious differences in their biochemical/physicochemical properties, molecular structure, carbohydrate-binding specificity and biological activities (Liu et al., [@B9]). Lectins are oligomeric which exhibit a large structural diversity and the molecular size range from 60 to 400 kDa. Each lectin polypeptide contains many molecular domains, one of which is the non-catalytic carbohydrate recognition domain, responsible for their ability to recognize and interact with specific glycoconjugates, without altering their structure. In the past few years, hundreds of plant lectins have been purified and characterized in details with respect to their biochemical properties, carbohydrate-binding specificities, these approaches allowed their classification (Van Dammes et al., [@B19]). Toll-like receptors =================== Plant materials represent an excellent source of immune modulators, which have been appointed as a new approach for combating infections caused by resistant microorganisms (Hancock et al., [@B5]). In this sense, a range of potential compounds have been proposed as agonists or inductors of immune receptors, including TLRs. The TLR family is the best characterized group of innate immune receptors in terms of known ligands, downstream signaling pathways and functional relevance. They comprise a family of receptors homologous to Toll receptor from Drosophila melanogaster. In humans, the TLR family includes 10 transmembrane proteins that play a crucial role in host defense: they recognize molecular characteristics of microorganisms, known as pathogen-associated molecular patterns (PAMPs) highly conserved between different classes of microorganisms. For example, TLR4 and accessory proteins recognize lipopolysaccharide (LPS), while TLR2 recognizes lipoteichoic acid and various lipopeptides (when in complex with either TLR-1 or