Stability of puroindoline peptides and effects on wheat rust
| Autor: | Joe Panozzo, Harbans Bariana, Rebecca L. Alfred, Mrinal Bhave, Enzo A. Palombo |
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| Rok vydání: | 2013 |
| Předmět: |
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Hot Temperature Physiology Antimicrobial peptides Molecular Sequence Data Biology Applied Microbiology and Biotechnology Rust Wheat Rust Botany Amino Acid Sequence Triticum Plant Diseases Plant Proteins Basidiomycota Tryptophan food and beverages General Medicine Hydrogen-Ion Concentration Spores Fungal Spore Horticulture Germination Puccinia striiformis Biotechnology Antimicrobial Cationic Peptides |
| Zdroj: | World journal of microbiologybiotechnology. 29(8) |
| ISSN: | 1573-0972 |
| Popis: | Peptides modelled on the tryptophan rich domain of puroindolines and the related grain softness protein-1 have a broad range of antibacterial and antifungal activities. With the aims of further investigating the activities of these antimicrobial peptides we studied their activity against wheat rust diseases and environmental stability. PINA-based peptides were found to have high pH and thermal stability in addition to being stable over long periods at room temperature. These properties could make them excellent candidates as preservatives in food. PuroA, Pina-R39G and PuroB peptides adversely affected the morphology of the stripe rust spores (Puccinia striiformis f. sp. tritici), while PuroA and PuroB showed moderate inhibition of their germination. Additionally, GSP-5D reduced the germination of leaf rust spores (P. triticina). PuroA and PuroB sprayed onto stripe rust infected plants effected a moderate reduction in the number of stripe rust uredinia on wheat seedlings, as did PuroB sprayed onto the seedlings and allowed to coat the leaves for 5 day prior to spore infection. The results suggest that the presence of the PIN-based peptides may lower frequency of initial infection foci. |
| Databáze: | OpenAIRE |
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