An engineered multidomain fungicidal peptide against plant fungal pathogens.
- Author:
Xiao-Qing QIU
1
,
2
,
3
,
4
,
5
,
6
,
7
;
Chong-Yi TONG
;
Zhen-Qi ZHONG
;
Wan-Qi WANG
;
Yue-Wen ZUO
;
Yun HUANG
;
Lu ZHANG
;
Xiang-Li ZHANG
;
Hong-Xia ZHANG
;
Rong-Qi LI
;
Jing WANG
;
Hao CHEN
;
Yun-Yun LI
;
George WU
;
He WANG
Author Information
1. Laboratory of Biomembrane and Membrane Protein, West China Hospital
2. Laboratory of Genetics, West China Second University Hospital, Sichuan University, Chengdu 610041, China
3. Department of Pathology, Chengdu Traditional Medicine University, Chengdu 610072, China
4. Division of Plant Protection, Yaan Agriculture Bureau, Yaan 625000, China
5. Department of Plant Pathology, Sichuan Agricultural University, Yaan 625000, China
6. Beijing Created Biotechnology Ltd., Beijing 100080, China
7. Division of Gastroenterology, University of Connecticut Health Center, Farmington 06030, USA. E-mail: 491607484@qq.com.
- Publication Type:Journal Article
- MeSH:
Candida albicans;
chemistry;
Colicins;
chemistry;
Fungicides, Industrial;
chemistry;
Mating Factor;
Peptides;
chemistry;
Protein Engineering
- From:
Acta Physiologica Sinica
2013;65(4):417-432
- CountryChina
- Language:English
-
Abstract:
Fungal pathogens represent major problems for human health and agriculture. As eukaryotic organisms, fungi share some important features with mammalian cells. Therefore, current anti-fungal antibiotics often can not distinguish between fungi and mammalian cells, resulting in serious side effects in mammalian cells. Accordingly, there is strong impetus to develop antifungal alternatives that are both safe and effective. The E1 family of colicin are channel-forming bacteriocins produced by Escherichia coli, which are bactericidal only to E. coli and related species. To target the channel-forming domain of colicin to fungal cell membrane, we engineered a sexual mating pheromone of Candida albicans, α-factor pheromone to colicin Ia. A peptide was constructed consisting of an α mating pheromone of C. albicans fused to the channel-forming domain of colicin Ia to create a new fusion protein, pheromonicin-CA (PMC-CA). Indirect immunolabeling showed that the PMC-CA bound to fungal cells and inhibited growth in the laboratory and field. In the field, the protective activity of pheromonicin against rice blast disease was significantly greater, on a molar basis, than that of triazoles, tricyclazole or isoprothiolane. These results suggest that fusion peptides may be of value as fungicidal agents under agricultural conditions.
