An overview of methods for increasing or reducing binding site numbers in lectins.
•Reducing the number of binding sites in lectins decreases agglutination activity.
•Increasing binding site numbers improves interaction with glycosylated structures.
•Combining lectins in heteromultimeric complexes can create new functions.
•The spatial arrangement of binding sites in space is important for ligand-interaction.
AbstractCarbohydrates 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.
KeywordsLectins
Synthetic biology
Neolectins
Artificial lectin multimers
Lectin engineering
AbbreviationsAgrocybe cylindracea galectinACG
Aleuria aurantia lectinAAL
Allium sativum leaf lectinASAL
carbohydrate binding moduleCBM
carbohydrate recognition domainsCRDs
cholera toxin B subunitCTB
C-type lectin receptorCLR
fluorescence activated cell sortingFACS
fragment crystallizable regionFc
giant unilamellar vesiclesGUVs
hemagglutinin of influenza A virusHA
high-mannose-type N-glycansHMGs
L-homopropargylglycineHpg
Maackia amurensis seed leukoagglutininMAL
non-canonical amino acidsncAAs
PEG bismaleimidePEGbisMal
Pseudomonas fluorescens agglutininPFA
Ralstonia solanacearum lectinRSL
Sambucus sieboldiana bark lectinMSSA
shiga toxin B subunitStxB
© 2022 The Authors. Published by Elsevier Inc.
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