Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma.
2016
The Aleuria aurantia lectin (AAL) derived from orange peel
fungus contains five fucose-binding sites that recognizes
fucose bound in -1,2, -1,3, -1,4, and -1,6 linkages to
N-acetylglucosamine and galactose. Recently, we have created
several recombinant AAL (rAAL) proteins that had altered
binding affinity to fucose linkages. In this report, we further
characterize the binding specificity of one of the mutated
lectins, N224Q lectin. This lectin was characterized by lectin
Western blotting, surface plasmon resonance, and glycan
microarray and shown to have increased binding to fucosylated
glycan. Subsequently, we used this lectin to identify secreted
fucosylated glycoproteins from a fetal hepatic cell line.
Proteomic analysis revealed several glycoproteins secreted by
the fetal cell line that were bound by N224Q lectin. These
findings were confirmed by subsequent proteomic analysis of
human serum from control patients or patients with
hepatocellular carcinoma. These represent candidate oncofetal
markers for liver cancer.
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