Abstract
The mushroom Hericium erinaceus contains isolectins, including the ricin B-like lectin HEL1 and the core 1 O-glycan-binding lectin HEL2. Recombinant HEL2 reportedly binds O-linked glycans, but recombinant HEL1 (rHEL1) has not been characterized. HEL1 and Stereum hirsutum lectin (SHL1) orthologues, which contain the typical (QxW)3 ricin-B like motif, were evaluated. Interestingly, under non-denaturing conditions, recombinant SHL1 (rSHL1) existed as a trimer and exhibited agglutination activity, whereas rHEL1 existed as a monomer with no agglutination activity. The hemagglutination activity of rSHL1 was inhibited by N-linked glycoprotein transferrin. A glycan-array analysis revealed that the two recombinant lectins had different binding intensities toward fucosylated N-glycans harboring fucose-α(1,2) galactose or fucose-α(1,4) N-acetylglucosamine. Isothermal calorimetry showed that compared with rHEL1, rSHL1 interacted more strongly with transferrin, a fucosylated glycoprotein, than with other fucosylated disaccharide glycoconjugates. Finally, rSHL1 and rHEL1 were comparable in their ability to detect highly fucosylated N-glycans within glycoproteins on the surface of SW1116 human colorectal carcinoma cells. Therefore, these ricin B-like lectins might enable detection of highly fucosylated glycoepitopes on cancer cells for diagnostic applications.
Published Version
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