Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen
The disease-specific (dsp) gene dspA/E of Erwinia amylovora encodes an essential pathogenicity effector of 198 kDa, which is critical to the development of the devastating plant disease fire blight. A yeast two-hybrid assay and in vitro protein pull-down assay demonstrated that DspA/E interacts phys...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
2006-01-01
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| Series: | Molecular Plant-Microbe Interactions |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0053 |
| _version_ | 1811291415290839040 |
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| author | Xiangdong Meng Jean M. Bonasera Jihyun F. Kim Riitta M. Nissinen Steven V. Beer |
| author_facet | Xiangdong Meng Jean M. Bonasera Jihyun F. Kim Riitta M. Nissinen Steven V. Beer |
| author_sort | Xiangdong Meng |
| collection | DOAJ |
| description | The disease-specific (dsp) gene dspA/E of Erwinia amylovora encodes an essential pathogenicity effector of 198 kDa, which is critical to the development of the devastating plant disease fire blight. A yeast two-hybrid assay and in vitro protein pull-down assay demonstrated that DspA/E interacts physically and specifically with four similar putative leucine-rich repeat (LRR) receptor-like serine/threonine kinases (RLK) from apple, an important host of E. amylovora. The genes encoding these four DspA/E-interacting proteins of Malus ×domestica (DIPM1 to 4) are conserved in all genera of hosts of E. amylovora tested. They also are conserved in all cultivars of apple tested that range in susceptibility to fire blight from highly susceptible to highly resistant. The four DIPMs have been characterized, and they are expressed constitutively in host plants. In silico analysis indicated that the DIPMs have similar sequence structure and resemble LRR RLKs from other organisms. Evidence is presented for direct physical interaction between DspA/E and the apple proteins encoded by the four identified clones, which may act as susceptibility factors and be essential to disease development. Knowledge of DIPMs and the interaction with DspA/E thus may facilitate understanding of fire blight development and lead to new approaches to control of disease. |
| first_indexed | 2024-04-13T04:28:07Z |
| format | Article |
| id | doaj.art-e0f46d3dd5de487d9962963da9b8a21a |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-13T04:28:07Z |
| publishDate | 2006-01-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-e0f46d3dd5de487d9962963da9b8a21a2022-12-22T03:02:25ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062006-01-01191536110.1094/MPMI-19-0053Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight PathogenXiangdong MengJean M. BonaseraJihyun F. KimRiitta M. NissinenSteven V. BeerThe disease-specific (dsp) gene dspA/E of Erwinia amylovora encodes an essential pathogenicity effector of 198 kDa, which is critical to the development of the devastating plant disease fire blight. A yeast two-hybrid assay and in vitro protein pull-down assay demonstrated that DspA/E interacts physically and specifically with four similar putative leucine-rich repeat (LRR) receptor-like serine/threonine kinases (RLK) from apple, an important host of E. amylovora. The genes encoding these four DspA/E-interacting proteins of Malus ×domestica (DIPM1 to 4) are conserved in all genera of hosts of E. amylovora tested. They also are conserved in all cultivars of apple tested that range in susceptibility to fire blight from highly susceptible to highly resistant. The four DIPMs have been characterized, and they are expressed constitutively in host plants. In silico analysis indicated that the DIPMs have similar sequence structure and resemble LRR RLKs from other organisms. Evidence is presented for direct physical interaction between DspA/E and the apple proteins encoded by the four identified clones, which may act as susceptibility factors and be essential to disease development. Knowledge of DIPMs and the interaction with DspA/E thus may facilitate understanding of fire blight development and lead to new approaches to control of disease.https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0053 |
| spellingShingle | Xiangdong Meng Jean M. Bonasera Jihyun F. Kim Riitta M. Nissinen Steven V. Beer Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen Molecular Plant-Microbe Interactions |
| title | Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen |
| title_full | Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen |
| title_fullStr | Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen |
| title_full_unstemmed | Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen |
| title_short | Apple Proteins that Interact with DspA/E, a Pathogenicity Effector of Erwinia amylovora, the Fire Blight Pathogen |
| title_sort | apple proteins that interact with dspa e a pathogenicity effector of erwinia amylovora the fire blight pathogen |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0053 |
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