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Review
. 2017 Jun 12;18(6):1242.
doi: 10.3390/ijms18061242.

Legume Lectins: Proteins with Diverse Applications

Affiliations
Review

Legume Lectins: Proteins with Diverse Applications

Irlanda Lagarda-Diaz et al. Int J Mol Sci. .

Abstract

Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.

Keywords: antimicrobial; cancer; insecticidal; lectin; legume.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Overall structure of legume lectins. (A) tetramer with carbohydrate recognition domains (red); (B) amplified image of monomer with β-sheets (yellow), α-turns (purple), metal binding sites (area with green and gray spheres) and carbohydrate recognition domain (area occupied by the grey and red molecule). Image modified from Protein Data Bank (accession code 1GZ9).
Figure 2
Figure 2
Insecticidal action mechanism for lectins.

References

    1. Sharon N., Lis H. History of lectins: From hemagglutinins to biological recognition molecules. Glycobiology. 2004;14:53r–62r. doi: 10.1093/glycob/cwh122. - DOI - PubMed
    1. Hamid R., Masood A., Wani I.H., Rafiq S. Lectins: Proteins with diverse applications. J. Appl. Pharm. Sci. 2013;3:S93–S103.
    1. Loris R., Hamelryck T., Bouckaert J., Wyns L. Legume lectin structure. BBA-Protein Struct. Mol. Enzymol. 1998;1383:9–36. doi: 10.1016/S0167-4838(97)00182-9. - DOI - PubMed
    1. Sharon N., Lis H. Legume lectins a large family of homologous proteins. FASEB J. 1990;4:3198–3208. - PubMed
    1. Vázquez-Moreno L., Ortega-Nieblas M., Robles-Burgueño M.R., Ramos-Clamont G. Purification of complex carbohydrate specific lectins from Olneya tesota seeds using tandem affinity chromatography. Int. J. Biochromatogr. 2000;5:83–90.

MeSH terms