Constitutive expression of transgenes encoding derivatives of the synthetic antimicrobial peptide BP100: impact on rice host plant fitness
| Autor: | Anna Nadal, Maria Montero, Nuri Company, Esther Badosa, Joaquima Messeguer, Laura Montesinos, Emilio Montesinos, Maria Pla |
|---|---|
| Přispěvatelé: | Ministerio de Ciencia e Innovación (Espanya) |
| Rok vydání: | 2012 |
| Předmět: |
Gene Dosage
Gene Expression Peptide Plant Science Genetically modified crops BP100 Arròs -- Genètica Gene Expression Regulation Plant Antimicrobial peptide AMP lcsh:Botany Rice -- Genetics Transgenes Peptide sequence Disease Resistance Genetics chemistry.chemical_classification Transgenic rice Homozygote Antibiòtics pèptids food and beverages Antimicrobial Plants Genetically Modified Genetically modified organism lcsh:QK1-989 Anti-Bacterial Agents Biochemistry Oligopeptides Research Article Transgene Molecular Sequence Data Oryza sativa Biology Hemolysis Transformation Genetic Humans Amino Acid Sequence RNA Messenger Plant Diseases Peptide antibiotics Plantes transgèniques Hostplant fitness Transgenic plants Oryza Hydrogen Peroxide Genetically modified rice Transformation (genetics) Oxidative Stress chemistry Pathogen-resistant rice Antimicrobial Cationic Peptides |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname BMC Plant Biology BMC Plant Biology, Vol 12, Iss 1, p 159 (2012) Recercat. Dipósit de la Recerca de Catalunya Dipòsit Digital de Documents de la UAB Universitat Autònoma de Barcelona BMC Plant Biology, 2012, vol. 12, p. 159-180 Articles publicats (D-EQATA) DUGiDocs – Universitat de Girona Recercat: Dipósit de la Recerca de Catalunya Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| DOI: | 10.1186/1471-2229-12-159 |
| Popis: | Background The Biopeptide BP100 is a synthetic and strongly cationic α-helical undecapeptide with high, specific antibacterial activity against economically important plant-pathogenic bacteria, and very low toxicity. It was selected from a library of synthetic peptides, along with other peptides with activities against relevant bacterial and fungal species. Expression of the BP100 series of peptides in plants is of major interest to establish disease-resistant plants and facilitate molecular farming. Specific challenges were the small length, peptide degradation by plant proteases and toxicity to the host plant. Here we approached the expression of the BP100 peptide series in plants using BP100 as a proof-of-concept. Results Our design considered up to three tandemly arranged BP100 units and peptide accumulation in the endoplasmic reticulum (ER), analyzing five BP100 derivatives. The ER retention sequence did not reduce the antimicrobial activity of chemically synthesized BP100 derivatives, making this strategy possible. Transformation with sequences encoding BP100 derivatives (bp100der) was over ten-fold less efficient than that of the hygromycin phosphotransferase (hptII) transgene. The BP100 direct tandems did not show higher antimicrobial activity than BP100, and genetically modified (GM) plants constitutively expressing them were not viable. In contrast, inverted repeats of BP100, whether or not elongated with a portion of a natural antimicrobial peptide (AMP), had higher antimicrobial activity, and fertile GM rice lines constitutively expressing bp100der were produced. These GM lines had increased resistance to the pathogens Dickeya chrysanthemi and Fusarium verticillioides, and tolerance to oxidative stress, with agronomic performance comparable to untransformed lines. Conclusions Constitutive expression of transgenes encoding short cationic α-helical synthetic peptides can have a strong negative impact on rice fitness. However, GM plants expressing, for example, BP100 based on inverted repeats, have adequate agronomic performance and resistant phenotypes as a result of a complex equilibrium between bp100der toxicity to plant cells, antimicrobial activity and transgene-derived plant stress response. It is likely that these results can be extended to other peptides with similar characteristics. We thank J.L. La Paz (Centre for Research in Agricultural Genomics) for valuable suggestions and technical assistance, E. Melé (IRTA) for valuable suggestions, the Servei de Microscopia, (Universitat Autònoma de Barcelona) for technical assistance and S. Burgess for revision of the English. This work was financially supported by the Spanish Ministerio de Ciencia e Innovación (projects AGL2010-17181/AGR and PLANT-KBBE EUI2008-03769) and the Generalitat de Catalunya (SGR-2009-12). M.M. received a studentship from the Fundación Ramón Areces. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|