Two plant puroindolines colocalize in wheat seed and in vitro synergistically fight against pathogens

被引:58
作者
Capparelli, R
Amoroso, MG
Palumbo, D
Iannaccone, M
Faleri, C
Cresti, M
机构
[1] Univ Naples Federico II, Sch Biotechnol Sci, I-80055 Naples, Italy
[2] Univ Siena, Dipartimento Sci Ambientali, I-53100 Siena, Italy
关键词
antimicrobial activity; defensin; immunolocalization; preservant; puroindolines; synergism;
D O I
10.1007/s11103-005-8270-9
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
Puroindolines, for years largely investigated for their involvement in wheat kernel hardness, have recently attracted attention thanks to their possible role as antimicrobial proteins. With the aim to enhance our knowledge of these proteins we studied their localization in the kernel, and their antimicrobial activity in vitro against six different bacterial strains. Immunolocalization showed that both the PINs are strongly concentrated in the aleurone layer, but also highly present in the endosperm. Interestingly we observed that puroindolines not only have the same spatial distribution in the kernel, they are also always found co-localized. Their co-localization suggests that they could cooperate in defending the plant against pathogens. We therefore tested antimicrobial activity of PINA and PINB, and a putative synergism between these proteins. The results showed that the two polypeptides can in vitro inhibit growth of all the bacteria tested; furthermore when combined together they are able to enhance each other's toxicity. In view of their antimicrobial activity and of their natural presence in Triticum aestivum wheat flour, puroindolines look promising antibacterial agents and thus deserve further studies aimed at establishing their possible future applications in fields of food and health care. Since PINs were still detectable in bakery products, these proteins may be promising tools in investigating natural ways of food preservation.
引用
收藏
页码:857 / 867
页数:11
相关论文
共 23 条
[11]  
Dixon R A, 1990, Adv Genet, V28, P165
[12]   Spatial and temporal distribution of the major isoforms of puroindolines (puroindoline-a and puroindoline-b) and non specific lipid transfer protein (ns-LTPle1) of Triticum aestivum seeds.: Relationships with their in vitro antifungal properties [J].
Dubreil, L ;
Gaborit, T ;
Bouchet, B ;
Gallant, DJ ;
Broekaert, WF ;
Quillien, L ;
Marion, D .
PLANT SCIENCE, 1998, 138 (02) :121-135
[13]  
García-Olmedo F, 1998, BIOPOLYMERS, V47, P479, DOI 10.1002/(SICI)1097-0282(1998)47:6<479::AID-BIP6>3.0.CO
[14]  
2-K
[15]  
GARCIAOLMEDO F, 1989, PLANT MOL CELL BIOL, V6, P31
[16]   Cationic peptides: a new source of antibiotics [J].
Hancock, REW ;
Lehrer, R .
TRENDS IN BIOTECHNOLOGY, 1998, 16 (02) :82-88
[17]   How to optimize the drop plate method for enumerating bacteria [J].
Herigstad, B ;
Hamilton, M ;
Heersink, J .
JOURNAL OF MICROBIOLOGICAL METHODS, 2001, 44 (02) :121-129
[18]   Conformation of a bactericidal domain of puroindoline a: Structure and mechanism of action of a 13-residue antimicrobial peptide [J].
Jing, WG ;
Demcoe, AR ;
Vogel, HJ .
JOURNAL OF BACTERIOLOGY, 2003, 185 (16) :4938-4947
[19]   Expression of wheat puroindoline genes in transgenic rice enhances grain softness [J].
Krishnamurthy, K ;
Giroux, MJ .
NATURE BIOTECHNOLOGY, 2001, 19 (02) :162-166
[20]   Wheat puroindolines enhance fungal disease resistance in transgenic rice [J].
Krishnamurthy, K ;
Balconi, C ;
Sherwood, JE ;
Giroux, MJ .
MOLECULAR PLANT-MICROBE INTERACTIONS, 2001, 14 (10) :1255-1260