Fucoidan/Chitosan Nanoparticles Inhibit the Adhesion of Campylobacter jejuni to Human Intestinal Cells

Campylobacter jejuni (C. jejuni) is a leading cause of bacterial gastroenteritis worldwide. Its adherence to host cells decreases when glycoconjugates bear the Fucα1,2-Galβ1,4-GlcNAc epitope, suggesting a lectin-mediated adhesion mechanism. Certain molecular characteristics facilitate the adhesin’s binding to a wide range of glycan ligands, enabling the selection of glycomimetic antagonists. This study tested whether fucoidan, a fucose-containing molecule, could mimic host glycans recognized by C. jejuni and inhibit adhesion to Caco-2 cells. Fucoidan’s glycomimetic potential was evaluated using complex coacervation to form fucoidan–chitosan nanoparticles (F/C-NPs) at the F3:C1 ratio. Infrared spectroscopy confirmed the coacervation of fucoidan with chitosan. The F/C-NPs exhibited a zeta potential of −37.35 ± 0.69 mV, as measured by dynamic light scattering, suggesting the presence of fucoidan on their surface. Their mean size and polydispersity index were 433.95 ± 10.66 nm and 0.15 ± 0.04, respectively. Energy dispersive X-ray spectroscopy detect sulfur from fucoidan’s sulfate groups. ELISA-like lectin assay and confocal microscopy (CM) showed that C. jejuni recognized the F/C-NPs. CM confirmed a ~67% reduction in C. jejuni adhesion to Caco-2 cells in the presence of F/C NPs. These results indicate that F/C NPs could act as glycomimetic antagonists, offering potential for controlling campylobacteriosis.