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Lectins have been increasingly utilized as carriers for targeted drug delivery based on their specific binding to glycans located on mammalian cells. This study employed two lectins, B subunit of bacterial Shiga holotoxin (Stx1B) and fungal <i>Clitocybe nebularis</i> lectin (CNL), for surface display on the lactic acid bacterium <i>Lactococcus lactis</i>. The specific adhesion of these engineered, lectin-displaying <i>L. lactis</i> to cancer cells was evaluated. The expression and surface display of both lectins on <i>L. lactis</i> were demonstrated by western blotting and flow cytometry, respectively. MTS assays revealed that recombinant Stx1B had no effect on Caco-2 cell viability at concentrations of ≤25 µg/mL, whereas CNL was non-toxic even at relatively high concentrations of ≤250 µg/mL. Stx1B bound to Caco-2, HT-29 and HeLa cells after 1 h of incubation. CNL bound to Caco-2 cells and recognized several glycoproteins in HT-29 and Caco-2 cell homogenates of which a 70 kDa protein predominated. Confocal microscopy revealed adhesion of Stx1B-displaying <i>L. lactis</i> to HeLa, Caco-2, and, to a lesser extent, HT-29 cells; CNL-displaying <i>L. lactis</i> showed a relatively similar level of adherence to HT-29 and Caco-2 cells. Thus, lectin-displaying <i>L. lactis</i> might serve as a carrier in targeted drug delivery when coupled to a therapeutic moiety.