Sw. Shin et al., Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain, FEBS LETTER, 467(1), 2000, pp. 70-74
We previously identified a novel lectin cDNA from the fall webworm [Shin et
al, (1998) Insect Biochem, Mel. Biol, 28, 827-837], which encodes two carb
ohydrate recognition domains (CRD-N and CRD-C) and is up-regulated followin
g bacterial challenge. The lipopolysaccharide (LPS) binding activities of t
he recombinant CRD-N and CRD-C (rCRD-N and rCRD-C) were investigated by enz
yme-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-gluco
samine, 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 mas mainly mediat
ed through the O-specific chain. (C) 2000 Federation of European Biochemica
l Societies.