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Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O‐specific chain
Author(s) -
Shin Sang Woon,
Park Doo-Sang,
Kim Sun Chang,
Park Ho-Yong
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01127-3
Subject(s) - lectin , mannose , biochemistry , escherichia coli , recombinant dna , lipopolysaccharide , microbiology and biotechnology , complementary dna , chemistry , binding site , mannan binding lectin , biology , gene , endocrinology
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.