Abstract
The binding and cleavage properties of the Influenza C virions hemagglutinin- esterase (CHE) protein for 9-O-acetyl groups on sialic acids have been taken advantage of in various assays using whole virions. Given the limitations of using whole virions for routine studies, a recombinant soluble molecule composed of the extracellular domain of CHE fused to the Fc region of human IgG (CHE-Fc) is engineered. Treatment of this chimeric molecule with diisopropyl fluorophosphate (DFP) selectively eliminates its esterase activity while preserving its binding property (CHE-FcD). So, this probe serves as a bifunctional tool for selectively removing (with CHE-Fc) or specifically detecting (with CHE-FcD) 9- O -acetylated sialic acids. The chapter describes the preparation of CHE-Fc chimera, chimera purification, the preparation of CHE-FcD, assay of esterase activity (CHE-Fc), CHE-FcD-binding activity assay, Use of CHE-Fc/FcD in flow cytometric analyses, and immunohistology.
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