Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain.

We previously identified a novel lectin cDNA from the fall webworm [Shin et al. (1998) Insect Biochem. Mol. Biol. 28, 827-837], which encodes two carbohydrate recognition domains (CRD-N and CRD-C) and is up-regulated following bacterial challenge. The lipopolysaccharide (LPS) binding activities of the recombinant CRD-N and CRD-C (rCRD-N and rCRD-C) were investigated by enzyme-linked immunosorbent assay. The LPS binding of rCRD-N and rCRD-C was pH-dependent: at pH below 6.0, they show a higher binding ability to LPS. The binding of the rCRD-N was inhibited by both D-mannose and N-acetyl-D-glucosamine, whereas the binding of the rCRD-C was inhibited only by D-mannose. The binding of both rCRD-N and rCRD-C to Escherichia coli was mainly mediated through the O-specific chain.