2014, Number 3
<< Back
Biotecnol Apl 2014; 31 (3)
The inhibition of pathogen-associated molecular patterns confers high protection against fungi and oomycetes in plants
Hernandez-Estévez I, Portieles-Alvarez R, Silva Y, Pujol-Ferrer M, Oliva-Borbón O, Borrás-Hidalgo O
Language: English
References: 18
Page: 254-257
PDF size: 411.75 Kb.
ABSTRACT
Crops of agricultural interest are highly affected by fungi- and oomycetes-caused diseases in Cuba and worldwide. The search for alternatives for its control continues, as a major challenge with the use of biotechnological techniques. In nature, plants are exposed to biotic stress and develop resistance against pathogenic infection through the fast activation of the innate immune system. Such an effective resistance response requires the detection and fast inhibition of the evolutionary conserved pathogen-associated molecular patterns (PAMPs). These PAMPs comprise, among others, proteases and polygalacturonases, which mediate the initial pathogenicity mechanisms during infection that counteract the initial plant defensive responses. In this work, inhibitors of pathogen’s proteases and polygalacturonases were developed to generate plant resistance against a wide spectrum of fungi- and oomycetes-caused diseases. Tobacco plants expressing a polygalacturonase inhibitor conferred, for the first time, high levels of resistance against this type of pathogens under field conditions. Additionally, a novel protease inhibitor effective against pathogens’ proteases was identified and characterized, which also provided resistance against pathogenic oomycetes in plants. This research granted the 2013 Award of the Cuban National Academy of Sciences.
REFERENCES
Jones JD, Dangl JL. The plant immune system. Nature. 2006;444(7117):323-9.
De Lorenzo G, D'Ovidio R, Cervone F. The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu Rev Phytopathol. 2001;39:313-35.
Casasoli M, Federici L, Spinelli F, Di Matteo A, Vella N, Scaloni F, et al. Integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein. Proc Natl Acad Sci USA. 2009;106(18):7666-71.
Brutus A, Sicilia F, Macone A, Cervone F, De Lorenzo G. A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides. Proc Natl Acad Sci USA. 2010;107(20):9452-7.
Powell AL, van Kan J, ten Have A, Visser J, Greve LC, Bennett AB, et al. Transgenic expression of pear PGIP in tomato limits fungal colonization. Mol Plant-Microbe Interact. 2000;13(9):942-50.
Ferrari S, Vairo D, Ausubel FM, Cervone F, De Lorenzo G. Tandemly duplicated Arabidopsis genes that encode polygalacturonase- inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection. Plant Cell. 2003;15(1):93-106.
Aguero CB, Uratsu SL, Greve C, Powell AL, Labavitch JM, Meredith CP, et al. Evaluation of tolerance to Pierce's disease and Botrytis in transgenic plants of Vitis vinifera L. expressing the pear PGIP gene. Mol Plant Pathol. 2005;6(1):43-51.
Manfredini C, Sicilia F, Ferrari S, Pontiggia D, Salvi G, Caprari C, et al. Polygalacturonaseinhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection. Physiol Mol Plant Pathol. 2005;67(2):108-15.
Janni M, Sella L, Favaron F, Blechl AE, De Lorenzo G, D'Ovidio R. The expression of a bean PGIP in transgenic wheat confers increased resistance to the fungal pathogen Bipolaris sorokiniana. Mol Plant Microbe Interact. 2008;21(2):171-7.
Ferrari S, Sella L, Janni M, De Lorenzo G, Favaron F, D'Ovidio R. Transgenic expression of polygalacturonase-inhibiting proteins in Arabidopsis and wheat increases resistance to the flower pathogen Fusarium graminearum. Plant Biol. 2012;14 Suppl 1:31-8.
Haq SK, Atif SM, Khan RH. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Arch Biochem Biophys. 2004;431(1):145-59.
Kim JY, Park SC, Hwang I, Cheong H, Nah JW, Hahm KS, et al. Protease inhibitors from plants with antimicrobial activity. Int J Mol Sci. 2009;10(6):2860-72.
Lorito M, Broadway RM, Hayes CK, Woo SL, Noviello C, Williams DL et al. Proteinase inhibitors from plants as a novel class of fungicides. Mol Plant-Microbe Interact. 1994;7(4):525-7.
Mosolov VV, Loginova MD, Fedurkina NV, Benken II. The biological significance of proteinase inhibitors in plants. Plant Sci Lett. 1976;7(2):77-80.
Ryan CA. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu Rev Phytopathol. 1990;28:425-49.
Woloshuk CP, Meulenhoff JS, Sela-Buurlage M, van den Elzen PJ, Cornelissen BJ. Pathogeninduced proteins with inhibitory activity toward Phytophthora infestans. Plant Cell. 1991;3(6):619-28.
Valueva TA, Revina TA, Gvozdeva EL, Gerasimova NG, Ozeretskovskaia OL. [Role of proteinase inhibitors in potato protection]. Bioorg Khim. 2003;29(5):499-504.
Valueva TA, Revina TA, Kladnitskaya GV, Mosolov VV. Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers. FEBS Lett. 1998;426(1):131-4.