期刊
PLANT BIOTECHNOLOGY JOURNAL
卷 12, 期 1, 页码 81-92出版社
WILEY
DOI: 10.1111/pbi.12119
关键词
antimicrobial peptide; BP100; cationic peptide; molecular farming; protein body; transgenic plant
资金
- Spanish Ministerio de Ciencia e Innovacion [AGL2010-17181/AGR, PLANT-KBBE EUI2008-03769, BMBF PLANT-KBBE FKZ0315456B]
Synthetic linear antimicrobial peptides with cationic -helical structures, such as BP100, are valuable as novel therapeutics and preservatives. However, they tend to be toxic when expressed at high levels as recombinant peptides in plants, and they can be difficult to detect and isolate from complex plant tissues because they are strongly cationic and display low extinction coefficient and extremely limited immunogenicity. We therefore expressed BP100 with a C-terminal tag which preserved its antimicrobial activity and demonstrated significant accumulation in plant cells. We used a fluorescent tag to trace BP100 following transiently expression in Nicotiana benthamiana leaves and showed that it accumulated in large vesicles derived from the endoplasmic reticulum (ER) along with typical ER luminal proteins. Interestingly, the formation of these vesicles was induced by BP100. Similar vesicles formed in stably transformed Arabidopsis thaliana seedlings, but the recombinant peptide was toxic to the host during latter developmental stages. This was avoided by selecting active BP100 derivatives based on their low haemolytic activity even though the selected peptides remained toxic to plant cells when applied exogenously at high doses. Using this strategy, we generated transgenic rice lines producing active BP100 derivatives with a yield of up to 0.5% total soluble protein.
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