130 years of Plant Lectin Research

Abstract

Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. The history of lectins started with the discovery of ricin about 130 years ago but since then our understanding of lectins has dramatically changed. Over the years the research focus was shifted from 'the characterization of carbohydrate-binding proteins' to 'understanding the biological function of lectins'. Nowadays plant lectins attract a lot of attention especially because of their potential for crop improvement and biomedical research, as well as their application as tools in glycobiology. The present review aims to give an overview of plant lectins and their applications, and how the field evolved in the last decades.

Gene Expression Patterns for Proteins With Lectin Domains in Flax Stem Tissues Are Related to Deposition of Distinct Cell Wall Types

“…Low level of expression specificity between various stem tissues of flax was also detected for the genes encoding plasma membrane-localized proteins from several other lectin families, like legume lectins, GNA lectins, C-type, and LysM (Table 2). C-type (PF00059) lectins are scarce in plant genomes, but are widely present in vertebrates (Tsaneva and Van Damme, 2020); flax has only two C-type lectins (Table 1) and both were expressed in all analyzed stem tissues (Table 2). Legume lectins (PF00139) (such as concanavalin A from jack beans (Leguminosae family), found in abundance in seeds of this taxonomic group) are quite numerous in the flax genome (Figure 4), which is similar to findings in other plant species (Bellande et al, 2017;Van Holle et al, 2017).…”

“…Within the framework of used classification, proteins with the PP2 domain belong to the Nictaba lectin family. The Nictaba domain specifically recognizes highmannose N-glycans, complex N-glycans, and, to a lesser extent, -GlcNAc oligomers (Tsaneva and Van Damme, 2020). Proteins with a Nictaba domain are considered nucleocytoplasmic and were confirmed to interact with O-GlcNAc-modified histones in the nucleus (Delporte et al, 2014).…”

“…The term lectins joins a number of protein families capable of selectively recognizing various types of carbohydrates, while not interacting enzymatically with the recognized targets (Peumans and Van Damme, 1995). Lectins are widespread and present in all biological kingdoms (Sharon, 2008;Tsaneva and Van Damme, 2020). Initially, lectins were identified by the agglutination reaction; therefore, this group of proteins was often referred to as agglutinins.…”

“…Sequence bioinformatics studies across all available databases have shown that some of the lectin motifs are widespread (from plants to animals, fungi, and bacteria), while others are present only in certain plant families. Several informative papers with generalizations on plant lectin families have been published (Bellande et al, 2017;Van Holle et al, 2017;Tsaneva and Van Damme, 2020).…”

Structure-Function Insights of Jaburetox and Soyuretox: Novel Intrinsically Disordered Polypeptides Derived from Plant Ureases

“…Plant tissues accumulate, constitutively or after induction, various classes of defensive compounds that confer resistance against herbivores and infection by fungi, bacteria, viruses, as well as nematodes. The most known plant proteins involved in defense mechanisms against insect pests include lectins [ 22 ], ribosome-inactivating proteins of types 1 and 2 [ 23 ], inhibitors of proteolytic enzymes and glycohydrolases [ 24 ], modified forms of storage proteins [ 25 , 26 ], among others. Several plant peptides display antifungal properties such as defensins [ 27 ], lipid transport proteins [ 28 ], chitinases [ 29 ], lectins [ 30 ], thionins [ 31 ], cyclopeptide alkaloids [ 32 ] and other less common types.…”