Functional expression and mutant analysis of thioredoxin-fused CEL-III, a hemolytic lectin from the marine invertebrate Cucumaria echinata.

Abstract

CEL-III is a hemolytic lectin purified from the marine invertebrate Cucumaria echinata. New expression system of CEL-III was constructed, and the recombinant thioredoxin-fused CEL-III (Trx-CEL-III) showed strong hemolytic and carbohydrate-binding activity as same as authentic CEL-III. Mutation analysis of Trx-CEL-III suggested that carbohydrate binding to subdomain 1α and 2β of CEL-III might be important for the hemolytic activity.