Back2Basics: animal lectins: an insight into a highly versatile recognition protein.

Abstract

The rapid advancement of molecular research has contributed to the discovery of 'Lectin', a carbohydrate-binding protein which specifically interacts with receptors on surface glycan moieties that regulate various critical cellular activities. The first animal lectin reported was 'the asialoglycoprotein receptor' in mammalian cells which helped analyze how animal lectins differ in glycoconjugate binding. Animal lectins are classified into several families, depending on their diverse cellular localization, and the binding specificities of their Carbohydrate-Recognition Domain (CRD) modules. Earlier characterization of animal lectins classified them into two structural families, the C-type (Ca2+-dependent binding) and S-type galectins (sulfhydryl-dependent binding) lectins. The C-type lectin includes the most significant animal lectins, such as endocytic receptors, mannose receptors, selectins, and collectins. The recent developments in research based on the complexity of the carbohydrate ligands, the metabolic processes they perform, their expression levels, and their reliance on divalent cations have identified more than 100 animal lectins and classified them into around 13 different families, such as Calnexin, F-lectin, Intelectin, Chitinase-like lectin, F-box lectin, etc. Understanding their structure and expression patterns have aided in defining their significant functions including cell adhesion, antimicrobial activity, innate immunity, disease diagnostic biomarkers, and drug delivery through specific carbohydrate-protein interactions. Such extensive potential roles of animal lectins made it equally important to plant lectins among researchers. Hence, the review focuses on providing an overview of animal lectins, their taxonomy, structural characteristics, and functions in diverse aspects interconnected to their specific carbohydrate and glycoconjugate binding.