A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii.

The adherence of Actinomyces naeslundii to human epithelial (KB) cells is mediated by the interaction of a fimbrial lectin on this oral bacterium with epithelial cell receptors exposed by sialidase. The D-galactose- and N-acetyl-D-galactosamine-reactive plant lectins from peanut and from Bauhinia purpurea inhibit this interaction. This report describes the partial purification and characterization of a 160-kilodalton (kDa) cell surface glycoprotein which is the principal receptor for these lectins. Radioiodinated lectins detected a band of 160 kDa on sialidase-treated Western blots of epithelial cell extracts but did not detect bands on nontreated filters. However, wheat germ agglutinin was reactive with the 160-kDa band on filters that were not treated with sialidase, suggesting that this lectin recognizes the sialic acid residues of this molecule. The 160-kDa component was partially purified from n-octylglucoside extracts of the epithelial cells by wheat germ agglutinin affinity chromatography. This molecule was metabolically labeled with D-[14C]glucosamine and labeled at the cell surface by lactoperoxidase-catalyzed iodination or periodate oxidation followed by sodium borotritide reduction. Incubation of epithelial cells with sialidase before extraction resulted in the loss of the 160-kDa band and the appearance of a band at 200 kDa which was directly reactive with 125I-labeled peanut agglutinin. These results indicate that the 160-kDa glycoprotein on the surface of the epithelial cell serves as a receptor for the agglutinins from the peanut and B. purpurea and presumably the fimbrial lectin of actinomyces.