Elucidating the glycan-binding specificity and structure of <i>Cucumis melo</i> agglutinin, a new R-type lectin.

ABSTRACT: 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 su

SUBMITTER: Lundstrom J 

PROVIDER: S-EPMC10896221 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature