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Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin

Jon Lundstrøm, Emilie Gillon, Valérie Chazalet, Nicole Kerekes, Antonio Di Maio, Ten Feizi, Yan Liu, Annabelle Varrot and Daniel Bojar

Beilstein J. Org. Chem. 2024, 20, 306–320. https://doi.org/10.3762/bjoc.20.31

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Supporting Information File 1: Full array data regarding the binding specificity of CMA1.
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Supporting Information File 2: Additional figures.
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Supporting Information File 3: Supplementary glycan microarray document (MIRAGE) for the ICL glycan arrays.
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Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin

Jon Lundstrøm, Emilie Gillon, Valérie Chazalet, Nicole Kerekes, Antonio Di Maio, Ten Feizi, Yan Liu, Annabelle Varrot and Daniel Bojar

Beilstein J. Org. Chem. 2024, 20, 306–320. https://doi.org/10.3762/bjoc.20.31

How to Cite

Lundstrøm, J.; Gillon, E.; Chazalet, V.; Kerekes, N.; Di Maio, A.; Feizi, T.; Liu, Y.; Varrot, A.; Bojar, D. Beilstein J. Org. Chem. 2024, 20, 306–320. doi:10.3762/bjoc.20.31

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TY  - JOUR
A1  - Lundstrøm, Jon
A1  - Gillon, Emilie
A1  - Chazalet, Valérie
A1  - Kerekes, Nicole
A1  - Di Maio, Antonio
A1  - Feizi, Ten
A1  - Liu, Yan
A1  - Varrot, Annabelle
A1  - Bojar, Daniel
T1  - Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin
JF  - Beilstein Journal of Organic Chemistry
PY  - 2024///
VL  - 20
SP  - 306
EP  - 320
SN  - 1860-5397
DO  - 10.3762/bjoc.20.31
PB  - Beilstein-Institut
JA  - Beilstein J. Org. Chem.
UR  - https://doi.org/10.3762/bjoc.20.31
KW  - carbohydrate
KW  - glycan array
KW  - melon
KW  - plant lectin
KW  - R-type
N2  - Plant lectins have garnered attention for their roles as laboratory probes and potential therapeutics. Here, we report the discovery and characterization of Cucumis melo agglutinin (CMA1), a new R-type lectin from melon. Our findings reveal CMA1’s unique glycan-binding profile, mechanistically explained by its 3D structure, augmenting our understanding of R-type lectins. We expressed CMA1 recombinantly and assessed its binding specificity using multiple glycan arrays, covering 1,046 unique sequences. This resulted in a complex binding profile, strongly preferring C2-substituted, beta-linked galactose (both GalNAc and Fuca1-2Gal), which we contrasted with the established R-type lectin Ricinus communis agglutinin 1 (RCA1). We also report binding of specific glycosaminoglycan subtypes and a general enhancement of binding by sulfation. Further validation using agglutination, thermal shift assays, and surface plasmon resonance confirmed and quantified this binding specificity in solution. Finally, we solved the high-resolution structure of the CMA1 N-terminal domain using X-ray crystallography, supporting our functional findings at the molecular level. Our study provides a comprehensive understanding of CMA1, laying the groundwork for further exploration of its biological and therapeutic potential.
ER  -

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