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Publication Abstract from PubMed

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.

Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin.,Lundstrom J, Gillon E, Chazalet V, Kerekes N, Di Maio A, Feizi T, Liu Y, Varrot A, Bojar D Beilstein J Org Chem. 2024 Feb 19;20:306-320. doi: 10.3762/bjoc.20.31. , eCollection 2024. PMID:38410776^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.