Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021;46(4):104.
doi: 10.1007/s12038-021-00225-8.

Research advances and prospects of legume lectins

Affiliations
Review

Research advances and prospects of legume lectins

Rajan Katoch et al. J Biosci. 2021.

Abstract

Lectins are widely distributed proteins having ability of binding selectively and reversibly with carbohydrates moieties and glycoconjugates. Although lectins have been reported from different biological sources, the legume lectins are the best-characterized family of plant lectins. Legume lectins are a large family of homologous proteins with considerable similarity in amino acid sequence and their tertiary structures. Despite having strong sequence conservation, these lectins show remarkable variability in carbohydrate specificity and quaternary structures. The ability of legume lectins in recognizing glycans and glycoconjugates on cells and other intracellular structures make them a valuable research tool in glycomic research. Due to variability in binding with glycans, glycoconjugates and multiple biological functions, legume lectins are the subject of intense research for their diverse application in different fields such as glycobiology, biomedical research and crop improvement. The present review specially focuses on structural and functional characteristics of legume lectins along with their potential areas of application.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Lectin mediated signalling in plant defense. (The binding of lectin domains with PAMP’s or DAMP’s at cell surface starts an intracellular signaling pathway, which includes downstream proteins phosphorylation cascade, activation of transcription factors, and ultimately regulation of stress-responsive genes. Nucleocytoplasmic lectins bind with intracellular effectors and generate defense response).
Figure 2
Figure 2
(a) Tertiary structure of Vigna unguiculata lectin; (b) carbohydrate binding loops in dimeric structure of Vigna unguiculata lectin and corresponding amino acid sequence of each loop (Conserved amino acid residues in each loop are underlined).

References

    1. Adar R, Moreno JE, Karlsson KA, Streicher H, Sharon N. Structural studies of the combining site of Erythrina collarodendron lectin. Protein Sci. 1998;7:52–63. - PMC - PubMed
    1. Adar R, Sharon N. Mutational studies of the combining site residues of Erythrina corallodendron lectin. Eur. J. Biochem. 1996;239:668–674. - PubMed
    1. Ahmed SF, Quadeer AA, McKay MR. Preliminary identification of potential vaccine targets for the COVID-19 coronavirus (SARS-CoV-2) based on SARS-CoV immunological studies. Viruses. 2020;12:1–12. - PMC - PubMed
    1. Akkouh O, Ng TB, Singh SS, Yin C, Dan X, et al. Lectins with anti-HIV activity: A review. Molecules. 2015;20:648–668. - PMC - PubMed
    1. Amin ARMR, Paul RK, Thakur VS, Agarwal ML. A novel role for p73 in the regulation of Akt-Foxo1a-Bim signaling and apoptosis induced by the plant lectin, Concanavalin A. Cancer Res. 2007;67:5617–5621. - PubMed

MeSH terms

LinkOut - more resources