期刊
JOURNAL OF INVERTEBRATE PATHOLOGY
卷 142, 期 -, 页码 71-81出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jip.2016.11.008
关键词
GPI-anchored protein; Oligomer; Parasporin; Cry protein; Receptor
类别
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [18687007]
- New Energy and Industrial Technology Development Organization (NEDO) [08A02203a]
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [18687007, 15K07448] Funding Source: KAKEN
Parasporin-2 (PS2), alternatively named Cry46Aa1, an anticancer protein derived from Bacillus thuringiensis strain A1547, causes specific cell damage via PS2 oligomerization in the cell membrane. Although PS2 requires glycosylphosphatidylinositol (GPI)-anchored proteins for its cytocidal action, their precise role is unknown. Here, we report that the glycan of GPI induces PS2 oligomerization, which causes cell death. Cytotoxicity, cell-binding and oligomerization of the toxin were not observed in GPI-anchored protein deficient Chinese hamster ovary cells. Expression and protease-treatment analyses showed that the actions of the toxin were dependent on the glycan core, not the polypeptide moiety, of GPI-anchored proteins. However, surface expression of some GPI-anchored proteins is observed in PS2-insensitive cells. These data suggest that GPI-anchored proteins do not determine the target specificity, but instead function as a kind of coreceptor, in the cytocidal action of PS2. (C) 2016 Elsevier Inc. All rights reserved.
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