Carbohydrate Recognition Mechanism of the Mushroom Galectin ACG

Hirabayashi, Jun; Hu, Dan; Tateno, Hiroaki; Kuwabara, N.; Kato, Ryuichi; Yagi, Fumio

doi:10.4052/tigg.1736.1se

Cited by 3 publications

(1 citation statement)

References 32 publications

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“…ACG is a suitable target for lectin engineering [ 32 ] because its stable recombinant protein can be easily produced in Escherichia coli. Additionally, various ACG mutants that modify specificity have been reported [ 31 , 32 , 33 , 34 , 35 ].…”

Section: Introductionmentioning

confidence: 99%

Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans

Irumagawa

Hiemori

Saito

et al. 2022

IJMS

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Lectins, carbohydrate-binding proteins, are attractive biomolecules for medical and biotechnological applications. Many lectins have multiple carbohydrate recognition domains (CRDs) and strongly bind to specific glycans through multivalent binding effect. In our previous study, protein nano-building blocks (PN-blocks) were developed to construct self-assembling supramolecular nanostructures by linking two oligomeric proteins. A PN-block, WA20-foldon, constructed by fusing a dimeric four-helix bundle de novo protein WA20 to a trimeric foldon domain of T4 phage fibritin, self-assembled into several types of polyhedral nanoarchitectures in multiples of 6-mer. Another PN-block, the extender PN-block (ePN-block), constructed by tandemly joining two copies of WA20, self-assembled into cyclized and extended chain-type nanostructures. This study developed novel functional protein nano-building blocks (lectin nano-blocks) by fusing WA20 to a dimeric lectin, Agrocybe cylindracea galectin (ACG). The lectin nano-blocks self-assembled into various oligomers in multiples of 2-mer (dimer, tetramer, hexamer, octamer, etc.). The mass fractions of each oligomer were changed by the length of the linkers between WA20 and ACG. The binding avidity of the lectin nano-block oligomers to glycans was significantly increased through multivalent effects compared with that of the original ACG dimer. Lectin nano-blocks with high avidity will be useful for various applications, such as specific cell labeling.

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Section: Introductionmentioning

confidence: 99%

Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans

Irumagawa

Hiemori

Saito

et al. 2022

IJMS

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Transformation of Agrocybe cylindracea Galectin into αGalNAc-Specific Lectin

Hirabayashi

2022

Methods in Molecular Biology

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Carbohydrate-Binding Specificity of Human Galectins: An Overview by Frontal Affinity Chromatography

Iwaki

Hirabayashi

2018

Trends in Glycoscience and Glycotechnology

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To understand the biological functions of lectins, it is important to investigate their sugar-binding specificity. Although galectins are characterized as β-galactoside-binding proteins comprising evolutionarily conserved amino-acid sequences, they have significantly divergent specificities depending on their individual carbohydrate-recognition domains (CRDs). Of the various methods available to analyze lectin-glycan interactions, frontal affinity chromatography is unique in that it provides a quantitative set of dissociation constants (K d's) between immobilized lectins and a panel of (>100) fluorescently labeled oligosaccharides. In this article, we provide an overview of the features of galectin specificities with a focus on human galectins based on published data. From the data obtained, comprehensive features of individual CRDs can be systematically understood in terms of branching, and 3′-modifications including sialylation, sulfation, αGal/GalNAc substitutions, β1-3Gal extension, and N-acetyllactosamine repeats. Additionally, we analyze evolutionarily more distant galectin molecules of non-human origins. These findings provide not only basic knowledge but also useful information for their applications: e.g., for engineering superior galectins improved in their specificity and affinity and developing galectin-targeted drugs. A. Introduction: Transforming Lectinomics Lectins are a group of carbohydrate-binding proteins with diverse structures and specificities. Recent analysis revealed that the number of protein families of lectins and those involving lectin domains is almost 50 (1). This is surprising considering that the number of representative lectin families at the end of 20th century was only 10: R-type lectins (ricin B chain-like lectins) of β-trefoil fold, L-type lectins (legume lectin-like lectins) of β-sandwich fold (jellyroll), GNA (Galanthus nivalis agglutinin)-related lectins of β-prism II fold, jacalin-related lectins (mJRLs and gJRLs) of β-prism I fold, hevein-like lectins (chitin-binding lectins) of hevein-type cystineknot motif, C-type lectins (Ca-dependent-type animal lectins) of Ctype α/β fold, galectins (β-galactoside-binding lectins), siglecs (sialic acid-binding immunoglobulin-like lectins), hyaladhesins (hyaluronan-binding proteins) of C-type α/β fold, and pentraxins (a class of pattern recognition receptors involved in innate immunity) of β-sandwich fold (jellyroll). The latest members of new lectin families include the 17-kDa α-D-galactose-binding lectin from the Mediterranean mussel Mytilus galloprovincialis termed MytiLec 1) (2) and a 15.5-kDa mannose-specific lectin from the oyster Crassostrea gigas termed CGL1 (3). Lectin domains are also known as carbohydraterecognition domains (CRDs) in hydrolytic enzymes, typically belonging to the R-type lectin family (4). They are termed "carbohydrate-binding modules" (CBMs) in the framework of Carbohydrate-Active enZymes (CAZy), with family numbers CBM 1-84 (http:// www.cazy.org/Carbohydrate-Binding-Modules.html). Lectin domains are also fo...

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Carbohydrate Recognition Mechanism of the Mushroom Galectin ACG

Cited by 3 publications

References 32 publications

Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans

Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans

Transformation of Agrocybe cylindracea Galectin into αGalNAc-Specific Lectin

Carbohydrate-Binding Specificity of Human Galectins: An Overview by Frontal Affinity Chromatography

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