Volume 60, November 2022, 108020Highlights•

An overview of methods for increasing or reducing binding site numbers in lectins.

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Reducing the number of binding sites in lectins decreases agglutination activity.

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Increasing binding site numbers improves interaction with glycosylated structures.

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Combining lectins in heteromultimeric complexes can create new functions.

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The spatial arrangement of binding sites in space is important for ligand-interaction.

Abstract

Carbohydrates are more than an energy-storage. They are ubiquitously found on cells and most proteins, where they encode biological information. Lectins bind these carbohydrates and are essential for translating the encoded information into biological functions and processes. Hundreds of lectins are known, and they are found in all domains of life. For half a century, researchers have been preparing variants of lectins in which the binding sites are varied. In this way, the traits of the lectins such as the affinity, avidity and specificity towards their ligands as well as their biological efficacy were changed. These efforts helped to unravel the biological importance of lectins and resulted in improved variants for biotechnological exploitation and potential medical applications. This review gives an overview on the methods for the preparation of artificial lectins and complexes thereof and how reducing or increasing the number of binding sites affects their function.

Keywords

Lectins

Synthetic biology

Neolectins

Artificial lectin multimers

Lectin engineering

AbbreviationsAgrocybe cylindracea galectin

ACG

Aleuria aurantia lectin

AAL

Allium sativum leaf lectin

ASAL

carbohydrate binding module

CBM

carbohydrate recognition domains

CRDs

cholera toxin B subunit

CTB

C-type lectin receptor

CLR

fluorescence activated cell sorting

FACS

fragment crystallizable region

Fc

giant unilamellar vesicles

GUVs

hemagglutinin of influenza A virus

HA

high-mannose-type N-glycans

HMGs

L-homopropargylglycine

Hpg

Maackia amurensis seed leukoagglutinin

MAL

non-canonical amino acids

ncAAs

PEG bismaleimide

PEGbisMal

Pseudomonas fluorescens agglutinin

PFA

Ralstonia solanacearum lectin

RSL

Sambucus sieboldiana bark lectin

MSSA

shiga toxin B subunit

StxB

© 2022 The Authors. Published by Elsevier Inc.