Journal of Glycobiology
Open Access

Carbohydrate Binding Proteins: Lectins

Mihika Tripati^{* *}Correspondence: Mihika Tripati, Department of Biochemistry, Kakatiya University, Warangal, India, Email:

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Introduction

Lectins are a sort of protein that can bind to sugar. They're in some cases referred to as antinutrients. Animal studies suggest that certain lectins can decrease the body's capacity to retain nutrients.

Lectins are carbohydrate-binding proteins that are profoundly specific for sugar groups that are part of other molecules and so cause agglutination of specific cells or precipitation of glycoconjugates and polysaccharides. Lectins play a part in recognition on the cellular and molecular level and play various parts in organic recognition phenomena including cells, carbohydrates, and proteins. Lectins too intervene connection and binding of microscopic organisms, infections, and fungi to their aiming targets.

Lectins are ubiquitous in nature and are found in numerous foods. A few foods, such as beans and grains, fermented to diminish lectin substance. A few lectins are useful, which promotes bone development, whereas others may be capable poisons such as ricin [1].

Biological functions of lectins in animals, are known to play vital roles in the natural immune system. Lectins such as the mannosebinding lectin, offer assistance mediate the first-line defense against attacking microorganisms. Other immune lectins play a role in self, nonself discrimination and balance inflammatory and autoreactive processes [2]. Intelectins bind microbial glycans and may work within the natural immune system as well. Lectins may be involved in pattern recognition and pathogen disposal within the intrinsic immunity of vertebrates including fishes [3]. The function of lectins in plants is still uncertain. Once. thought to be fundamental for rhizobia binding, this proposed work was ruled out through lectin-knockout transgene studies [4].

Purified lectins are vital in a clinical setting since they are utilized for blood typing [5]. A few of the glycolipids and glycoproteins on an individual's red blood cells can be identified by lectins.

Lectins initially called as proteins isolated from plants that were able to agglutinating mammalian erythrocytes . Agglutination happens since the lectin molecule binds numerous glycoprotein molecules on the cell surface and it may cross-link erythrocytes. From a histochemical point of view, lectins may be characterized as plant or animal proteins which bind particular carbohydrate moieties in tissue.

References

1. Brudner, Matthew, Karpel, Marshall, Lear, et al. Schneider, Bradley S. (ed.). "Lectin-Dependent Enhancement of Ebola Virus Infection via Soluble and Transmembrane C-type Lectin Receptors". PLOS ONE. J. Glycobiol. 2013;8: e60838.
2. Chan, Charles KF, Ransom, Ryan C; Longaker, et al. "Lectins bring benefits to bones". eLife. J. Glycobiol. 2016.
3. Maverakis E, Kim K, Shimoda M, Gershwin M, Patel F, et al. "Glycans in the immune system and The Altered Glycan Theory of Autoimmunity". J. Glycobiol. 2015;57: 1–13.
4. Arasu, Abirami, Kumaresan, Venkatesh, Sathyamoorthi, et al. "Fish lily type lectin-1 contains β-prism architecture: Immunological characterization". Molecular Immunology. J. Glycobiol. 2013;56: 497–506.
5. Oldroyd, Giles E.D, Downie, J. Allan. "Coordinating Nodule Morphogenesis with Rhizobial Infection in Legumes". Annual Review of Plant Biology. J. Glycobiol. 2008;59: 519–46.