A new active antimicrobial peptide from PD-L4, a type 1 ribosome inactivating protein of Phytolacca dioica L.: A new function of RIPs for plant defence?

被引:23
|
作者
Pizzo, Elio [1 ]
Zanfardino, Anna [1 ]
Di Giuseppe, Antonella M. A. [2 ]
Bosso, Andrea [1 ]
Landi, Nicola [2 ]
Ragucci, Sara [2 ]
Varcamonti, Mario [1 ]
Notomista, Eugenio [1 ]
Di Maro, Antimo [2 ]
机构
[1] Univ Naples Federico II, Dept Biol, I-80126 Naples, Italy
[2] Univ Naples 2, Dept Environm Biol & Pharmaceut Sci & Technol, I-81100 Caserta, Italy
来源
FEBS LETTERS | 2015年 / 589卷 / 19期
关键词
Antimicrobial peptide; Cationic antimicrobial peptide; Ribosome inactivating protein; Phytolacca dioica; GLYCOSIDASE ACTIVITY; EXPRESSION; RESISTANCE; MECHANISM; LYSOZYME; BACTERIA; TOBACCO; LEAVES; RICIN; SEEDS;
D O I
10.1016/j.febslet.2015.08.018
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We investigated the antimicrobial activity of PD-L4, a type 1 RIP from Phytolacca dioica. We found that this protein is active on different bacterial strains both in a native and denatured/alkylated form and that this biological activity is related to a cryptic peptide, named PDL4(40-65), identified by chemical fragmentation. This peptide showed the same antimicrobial activity of full-length protein and possessed, similarly to several antimicrobial peptides, an immunomodulatory effect on human cells. It assumes an alpha-helical conformation when interact with mimic membrane agents as TFE and likely bacterial membranes are a target of this peptide. To date PDL4(40-65) is the first antimicrobial peptide identified in a type 1 RIP. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2812 / 2818
页数:7
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