期刊
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
卷 184, 期 1, 页码 44-47出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2012.04.006
关键词
Plasmodium falciparum; Malaria; Cyclophilin; Molecular chaperone; Protein folding; Cyclosporin A
资金
- Health Research Board [GHRA-06-03]
- Science Foundation Ireland [09/RFP/BMT2128]
- Science Foundation Ireland (SFI) [09/RFP/BMT2128] Funding Source: Science Foundation Ireland (SFI)
The cyclophilins are a large family of proteins implicated in folding, transport and regulation of other proteins and are potential drug targets in cancer and in some viral and parasitic infections. The functionality of cyclophilins appears to depend on peptidyl-prolyl cis-trans isomerase (foldase) and/or molecular chaperone activities. In this study we assessed the peptidyl-prolyl isomerase and chaperone activities of 8 members of the Plasmodium falciparum cyclophilin family, all produced recombinantly using a common host/vector system. While only two of these proteins had isomerase activity, all of them displayed chaperone function as judged by the ability to prevent the thermal aggregation of model substrates. We suggest that the cyclophilins constitute a family of molecular chaperones in malarial parasites that complement the functions of other chaperones such as the heat-shock proteins. (C) 2012 Elsevier B.V. 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