硫氧还蛋白融合型 CEL-III 的功能表达和突变分析，CEL-III 是一种来自海洋无脊椎动物海仙人掌的溶血凝集素。

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

机构信息

Laboratory of Food Molecular Functionality, College of Agriculture, Ibaraki University, 3-21-1 Chuo, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.

出版信息

Biosci Biotechnol Biochem. 2022 Jul 22;86(8):1071-1074. doi: 10.1093/bbb/zbac073.

DOI:10.1093/bbb/zbac073

PMID:35583240

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.

摘要

CEL-III 是一种从海洋无脊椎动物海仙人掌中纯化得到的溶血凝集素。我们构建了 CEL-III 的新型表达系统，该系统表达的重组硫氧还蛋白融合 CEL-III（Trx-CEL-III）具有与天然 CEL-III 相同的强烈溶血和碳水化合物结合活性。Trx-CEL-III 的突变分析表明，碳水化合物与 CEL-III 的亚结构域 1α 和 2β 的结合可能对溶血活性很重要。