AI Article Synopsis
- CEL-III is a lectin derived from the sea cucumber, Cucumaria echinata, known for its ability to bind to galactose and cause cell lysis.
- The protein has three distinct domains: two carbohydrate-binding domains that allow it to attach to cell surfaces, and a third domain responsible for oligomerization, which helps form pores in cell membranes.
- The chapter details methods for purifying CEL-III and conducting a binding assay on carbohydrate-coated microplates to study its properties.
Article Abstract
CEL-III is a Ca-dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata; it exhibits hemolytic and hemagglutinating activities. CEL-III consists of the following three distinct domains: two N-terminal carbohydrate-binding domains (1 and 2), which adopt β-trefoil folds such as the B-chain of ricin and are members of the (QXW) motif family, and domain 3, an oligomerization domain. After binding to the cell surface carbohydrate chains through domains 1 and 2, domain 3 self-associates to form transmembrane pores composed of CEL-III heptamers, leading to cell lysis or death. In this chapter, the purification and carbohydrate-coated microplate binding assay of CEL-III are described.
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Article Synopsis
- CEL-III is a lectin derived from the sea cucumber, Cucumaria echinata, known for its ability to bind to galactose and cause cell lysis.
- The protein has three distinct domains: two carbohydrate-binding domains that allow it to attach to cell surfaces, and a third domain responsible for oligomerization, which helps form pores in cell membranes.
- The chapter details methods for purifying CEL-III and conducting a binding assay on carbohydrate-coated microplates to study its properties.
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