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Article Dans Une Revue Beilstein Journal of Organic Chemistry Année : 2024

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

Résumé

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.
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hal-04542095 , version 1 (11-04-2024)

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Jon Lundstrøm, Emilie Gillon, Valérie Chazalet, Nicole Kerekes, Antonio Di Maio, et al.. Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin. Beilstein Journal of Organic Chemistry, 2024, 20, pp.306-320. ⟨10.3762/bjoc.20.31⟩. ⟨hal-04542095⟩
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