期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 47, 期 1, 页码 186-193出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2005.10.030
关键词
hemolysin; pore-forming toxins; alpha toxins; Bacillus cereus; pathogenicity; dye affinity chromatography; secreted proteins
The hemolysin 11 from Bacillus cereus, HlyII, is a member of the beta-barrel pore-forming toxin family of secreted microbial proteins that includes the Staphylococcus aureus a-toxin. Compared with other proteins of the family, hemolysin 11 has 90 extra amino acids at its C-terminus. To examine more closely the cytotoxic and pore-forming properties of the protein, we have cloned and expressed it in Escherichia coli. We developed a purification procedure for the matured HlyII protein from both culture media and cell extracts using a combination of cation exchange and affinity chromatography together with gel-filtration. In both cases, the fully processed HlyII protein was purified as confirmed by N-terminal sequence analysis. The HlyII protein exhibits cytolytic activity of different extent on erythrocytes from various kinds of mammals. The results presented here show for the first time that two types of human cells are sensitive to HlyII action. In view of its broad cytotoxic activity as well as the ability to interact with artificial membranes, we assume that HlyII needs no specific receptor to bind to cell membranes. (c) 2005 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据