CN115804377B - Application of glycine/glutamine enrichment sequence in inducing plant disease resistance - Google Patents
Application of glycine/glutamine enrichment sequence in inducing plant disease resistance Download PDFInfo
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- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 4
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- Agricultural Chemicals And Associated Chemicals (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
The invention discloses application of glycine/glutamine enrichment sequence in inducing plant disease resistance. The application of the glycine/glutamine enrichment sequence shown in SEQ ID NO.1 in preparing a virulence factor BCG1 recombinant protein for inducing the disease resistance of plants to fusarium graminearum and phytophthora capsici. The GQ/-motif which is respectively fused into one fusarium graminearum at the C end of MoBCG1 and AfBCG1 proteins which do not contain G/Q-rich motif shows that the MoBCG1+ FgG/Q, afBCG + FgG/Q proteins obviously enhance the disease resistance to the fusarium graminearum and phytophthora capsici. The G/Q-rich motif can be used as an enhancer to obviously enhance the capability of protein to induce plant disease resistance.
Description
Technical Field
The invention belongs to the field of plant protection, and relates to application of glycine/glutamine enrichment sequences in inducing plant disease resistance.
Background
Elicitors (elicators) are a specific class of compounds that activate the immune response of a host plant. The excitons are classified into polysaccharides, glycoproteins, polypeptides, etc. in terms of chemical composition. Many protein and polypeptide elicitors have been found in plant-pathogenic bacterial interaction systems, including the elicitors (elicitins) produced by Phytophthora (Phytophthora), the Harpin proteins of bacteria, xylanases, protein elicitors of plant viruses, and avirulence genes, among others. The most common exciton is flg22, which is a small peptide containing 22 amino acids conserved at the N-terminus of flagellin, and is commonly used in plant immunity research. The virulence factor BCG1 of the plant pathogenic fungus fusarium graminearum (Fusarium graminearum) contains a glycine/glutamine enrichment sequence (G/Q-rich motif) with an unknown function consisting of 54 amino acids at the C end, and the specific function of the glycine/glutamine enrichment sequence is not reported at present.
Disclosure of Invention
The object of the present invention is to address the above-mentioned deficiencies of the prior art and to provide the use of glycine/glutamine enrichment sequences (G/Q-rich motif) for inducing disease resistance in plants.
The aim of the invention can be achieved by the following technical scheme:
use of a recombinant BCG1 protein comprising a glycine/glutamine enrichment sequence (G/Q-rich) as shown in SEQ ID No.1 for inducing disease resistance of a plant against fusarium graminearum (f.graminearum), phytophthora capsici (Phytophthora capsica).
The application of the glycine/glutamine enrichment sequence shown in SEQ ID NO.1 in preparing recombinant BCG1 protein for inducing plant disease resistance to fusarium graminearum and phytophthora capsici. .
As a preferable mode of the invention, the recombinant protein obtained by merging the glycine/glutamine enrichment sequence shown in SEQ ID NO.1 into the C end of the BCG1 protein without the glycine/glutamine enrichment sequence can induce the disease resistance of plants to fusarium graminearum and phytophthora capsici.
The virulence factor FgBCG1 and homologous proteins thereof in fusarium graminearum (F.granatum) and FvBCG1 from fusarium oxysporum (F.oxysporum) and fusarium verticillium (F.verticillides) obviously enhance the disease resistance to fusarium graminearum (F.graminearum) and phytophthora capsici (P.capsica). Truncated protein FgBCG1 deleted of G/Q-rich motif ΔGQ 、FoBCG1 ΔGQ 、FvBCG1 ΔGQ And the ability of BCG1 homologous proteins not containing G/Q-rich motif (moccg 1 of rice blast fungus (Magnaporthe oryzae), afBCG1 of aspergillus flavus (Aspergillus flavus), respectively) to induce plant disease resistance was significantly reduced. It was demonstrated that the G/Q-rich motif-deleted BCG1 protein was unable to induce disease resistance against Fusarium graminearum (F.graminearum), phytophthora capsici (P.capsica).
Next, we fused G/Q-motif in one fusarium graminearum at the C-terminus of the mocbg 1 and AfBCG1 proteins without G/Q-rich motif, respectively, and the results show that the mocbg1+ FgG/Q, afBCG + FgG/Q proteins significantly enhance disease resistance against fusarium graminearum (f.graminearum) and phytophthora capsici (p.capsica). The G/Q-rich motif can be used as an enhancer to obviously enhance the capability of protein to induce plant disease resistance. Subsequently, we describe in detail the molecular mechanism of G/Q-rich motif affecting infection by phytopathogenic fungi (Fusarium graminearum, P.capsica). The experimental results show that G/Q-rich motif influences the induction of plant Reactive Oxygen Species (ROS) bursts by affecting the protein, and thus the induction of plant disease resistance. Thus, it was further demonstrated that the inhibition of F.graminearum, P.capsici, by G/Q-rich motif on the pathogenicity of Fusarium graminearum was achieved by inducing an immune response in plants. The findings indicate that the G/Q-rich motif has great application prospect in inducing plant disease resistance in agricultural production.
Drawings
The G/Q-rich motif of BCG1 of FIG. 1 is highly conserved only in Fusarium (A) the sequence features of the BCG1 protein; (B) constructing a phylogenetic tree based on RPB 2; (C) Weblogo 3 shows the G/Q-rich motif sequence.
FIG. 2 is a schematic diagram showing that the G/Q-rich motif-deleted BCG1 protein cannot induce disease resistance against Fusarium graminearum F.graminearum
FIG. 3 is a schematic diagram showing that the G/Q-rich motif-deleted BCG1 protein cannot induce disease resistance against P.capsica of Phytophthora capsici
FIG. 4G/Q-rich motif enhances wheat disease resistance to Fusarium graminearum F.graminearum
FIG. 5G/Q-rich motif enhances disease resistance of plants against P.capsica
FIG. 6G/Q-rich motif deletion results in a significant protein-induced reduction of reactive oxygen species
FIG. 7G/Q-rich motif protein enhancement of reactive oxygen species
The specific embodiment is as follows:
example 1G/Q-rich motif of BCG1 is highly conserved only in Fusarium
The experimental method comprises the following steps:
the proteins were aligned using ClustalW and the results of the alignment were visualized via the ENDscript/ESPript 3.0 website.
Experimental results: fusarium graminearum BCG1 contains a novel G/Q-rich motif. We constructed phylogenetic trees based on RPB2 protein sequences, studying the phylogenetic distribution of BCG1 in different organisms. As a result, the G/Q-rich motif sequence was found to be highly conserved, widely found in Fusarium, but homologous proteins containing G/Q-rich motif were not found in other organisms (FIG. 1).
Example 2 loss of G/Q-rich motif BCG1 protein was unable to induce disease resistance against Fusarium graminearum
The experimental method comprises the following steps:
protein expression and purification: the protein NCBI accession number (https:// www.ncbi.nlm.nih.gov /) of Table 1 was issued to Nanjing's tripod Biotechnology Co., ltd, and was commissioned for protein expression and purification.
Disease resistance experiment: after spraying 1. Mu.M of the successfully purified proteins of Table 1 on wheat ears during the flowering phase for 24h, fresh conidium suspensions of F.graminearum PH-1 strain (10 5 mu.L of 10% sterilized water was injected onto the flowers of the wheat ears, and 10. Mu.L of sterilized water was used as a control. 15 days after inoculation, the number of morbid ears per inoculated ear was recorded and photographed.
Experimental results: experimental results show that after the wheat ears are respectively pretreated by FgBCG1, foBCG1 and FvBCG1 proteins with G/Q-rich motif, disease symptoms caused by fusarium graminearum PH-1 can be obviously weakened (figure 2), and after the wheat ears are pretreated by the MoBCG1 and AfBCG1 proteins without G/Q-rich motif, the toxicity of PH-1 on wheat is not influenced. Truncated protein FgBCG1 deleted of G/Q-rich motif ΔGQ 、FoBCG1 ΔGQ 、FvBCG1 ΔGQ The protein has no influence on the toxicity of PH-1 on wheat. Taken together, our results indicate that the deletion of G/Q-rich motif results in the protein not being able to induce disease resistance against Fusarium graminearum. Example 3 BCG1 protein deleted for G/Q-rich motif was unable to induce disease resistance assay method against p.capsica of phytophthora capsici: after each protein in Table 1 was injected into leaf pieces of Benshi tobacco for 24 hours, the leaf pieces were moisturized with cottonPlacing in a square dish, inoculating Phytophthora capsici (P.capsica) bacteria dish at the center of the leaf, performing moisture culture at 25deg.C for 36 hr, photographing with hand-held ultraviolet lamp in darkness, counting the diameter of the disease spot, and repeating the experiment three times.
Experimental results: experimental results show that after the FgBCG1, the FoBCG1 and the FvBCG1 containing the G/Q-rich motif respectively pretreat wheat ears, disease symptoms caused by phytophthora capsici (P.capsica) can be remarkably weakened (figure 3), and after the wheat ears are pretreated by the MoBCG1 and the AfBCG1 containing the G/Q-rich motif, the toxicity of the phytophthora capsici (P.capsica) on the N.benthamiana is not influenced. Truncated protein FgBCG1 deleted of G/Q-rich motif ΔGQ 、FoBCG1 ΔGQ 、FvBCG1 ΔGQ The protein has no influence on the virulence of phytophthora capsici (P.capsica) on the cigarette. Taken together, our results indicate that the deletion of G/Q-rich motif results in the protein not being able to induce disease resistance against Phytophthora capsici.
Example 4G/Q-rich motif as enhancer to induce plant disease resistance to Fusarium graminearum (F.graminearum)
The experimental method comprises the following steps:
protein expression and purification: the Nanjing tripod biotechnology limited company is entrusted to express and purify the two proteins after the C end of the MoBCG1 without G/Q-rich motif and the C end of the AfBCG1 protein are respectively fused with the G/Q-motif sequence of FgBCG1 (namely, the last 54 amino acids of the FgBCG1 sequence).
Disease resistance experimental method: after spraying 1. Mu.M MoBCG1+ FgG/Q, afBCG1+ FgG/Q protein on the wheat ears during the flowering phase for 24 hours, fresh conidium suspensions of F.graminearum PH-1 strain (10 5 mu.L of 10% sterilized water was injected onto the flowers of the wheat ears, and 10. Mu.L of sterilized water was used as a control. 15 days after inoculation, the number of susceptible ears per inoculated ear was recorded and photographed.
Experimental results: G/Q-rich motif, which does not contain G/Q-rich motif, was incorporated into F.graminearum, and after pretreatment of wheat ears, disease symptoms caused by F.graminearum could be significantly reduced (FIG. 4). It is shown that G/Q-rich motif can act as an enhancer to enhance protein-induced disease resistance against Fusarium graminearum (F.graminearum).
Example 5G/Q-rich motif as enhancer, method of disease resistance experiment to induce plants against Phytophthora capsici (P.capsica): after 1 mu M MoBCG1+ FgG/Q, afBCG + FgG/Q protein is respectively injected into the leaf pieces of Benshi tobacco for 24 hours, the leaf pieces are put into a square dish by cotton moisturizing, phytophthora capsici (P.capsica) fungus dishes are inoculated at the center of the leaf pieces, the leaf pieces are subjected to moisturizing culture for 36 hours at 25 ℃, then the leaf pieces are photographed by a hand-held ultraviolet lamp in the dark, the diameter of the disease spots is counted, and the experiment is repeated three times.
Experimental results: the C-terminal of the protein without G/Q-rich motif was incorporated into G/Q-rich motif in Fusarium graminearum, and after pretreatment of wheat ears, disease symptoms caused by P.capsica (FIG. 5) were significantly reduced. It is shown that G/Q-rich motif can be used as an enhancer to enhance protein-induced disease resistance against Phytophthora capsici (P.capsica).
Example 6G/Q-rich motif deletion results in protein-induced reactive oxygen species reduction
The experimental method comprises the following steps: luminol chemiluminescence method detects Reactive Oxygen Species (ROS), and the leaf discs of benthamia were harvested for 5 weeks and floated in 200 μl of sterile water in 96-well plates overnight. Sterile water was discarded and ROS-buffer (10. Mu.g/mL peroxidase, 35.4. Mu.g/mL luminol, 1. Mu.M purified each BCG1 protein of Table 1) was added. Luminescence was measured using a GLOMAX 96-well plate photometer (Promega, madison, wis., USA).
Experimental results: to investigate the molecular mechanisms of G/Q-rich motif affecting plant infection with phytopathogenic fungi (Fusarium graminearum, P.capsica). Reactive Oxygen Species (ROS) are signaling molecules that play a role in the multilayer immune system of plants. We therefore examined the protein-induced accumulation of active oxygen in nicotiana benthamiana. Experimental results show that FgBCG1, foBCG1 and FvBCG1 proteins containing G/Q-rich motif can induce the accumulation of a large amount of Reactive Oxygen Species (ROS) in Nicotiana benthamiana, and that MoBCG1 and AfBCG1 proteins without G/Q-rich motif can only induce a small amount of ROS accumulation. Truncated protein FgBCG1 deleted of G/Q-rich motif ΔGQ 、FoBCG1 ΔGQ 、FvBCG1 ΔGQ Only small amounts of ROS were induced (fig. 6). Taken together, our results indicate that G/Q-rich motif affects protein-induced plant active oxygen bursts, thereby affecting disease resistance against Fusarium graminearum (F. Graminearum), P. Capsica).
Example 7G/Q-rich motif as enhancer to enhance protein-induced reactive oxygen species accumulation
The experimental method comprises the following steps: luminol chemiluminescence method detects Reactive Oxygen Species (ROS), and the leaf discs of benthamia were harvested for 5 weeks and floated in 200 μl of sterile water in 96-well plates overnight. Sterile water was discarded and ROS-buffer (10. Mu.g/mL peroxidase, 35.4. Mu.g/mL luminol, 1. Mu.M purified each BCG1 protein of Table 1) was added. Luminescence was measured using a GLOMAX 96-well plate photometer (Promega, madison, wis., USA).
Experimental results: experimental results show that the C-terminal of the G/Q-rich motif protein is not incorporated into G/Q-rich motif in Fusarium graminearum, which can significantly enhance the protein-induced active oxygen content (FIG. 7). Taken together, our results indicate that G/Q-rich motif can act as an enhancer to induce the active oxygen bursts in plants, thereby affecting the disease resistance against Fusarium graminearum (F. Graminearum) and Phytophthora capsici (P. Capsica). The G/Q-rich motif is shown to enhance disease resistance of the protein by enhancing the immune response of the plant.
Claims (3)
1. Recombinant BCG1 protein containing glycine/glutamine enrichment sequence shown in SEQ ID NO.1 for inducing fusarium graminearum in plants、Application of phytophthora capsici in disease resistance is provided.
2. Glycine/glutamine enrichment sequence shown in SEQ ID NO.1 for preparing induced plant fusarium graminearum、Application of phytophthora capsici disease resistance recombinant BCG1 protein is provided.
3. Use according to claim 2, characterized in that the recombinant BCG1 protein obtained by incorporating the glycine/glutamine enrichment sequence shown in SEQ ID No.1 at the C-terminus of the recombinant protein without glycine/glutamine enrichment sequence is capable of inducing plants to fusarium graminearum、Disease resistance of phytophthora capsici.
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| CN110922457A (en) * | 2019-11-14 | 2020-03-27 | 南京农业大学 | Plant immune induced resistance protein FgPII1 secreted by fusarium graminearum and application thereof |
| CN113150087A (en) * | 2021-03-09 | 2021-07-23 | 南京农业大学 | Plant immune activator protein Fg62 secreted by fusarium graminearum and application thereof |
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| CN110922457A (en) * | 2019-11-14 | 2020-03-27 | 南京农业大学 | Plant immune induced resistance protein FgPII1 secreted by fusarium graminearum and application thereof |
| CN113150087A (en) * | 2021-03-09 | 2021-07-23 | 南京农业大学 | Plant immune activator protein Fg62 secreted by fusarium graminearum and application thereof |
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| 丝状真菌G蛋白信号途径的研究进展;李利;陈莎;毛涛;陈福生;;微生物学通报(第08期);全文 * |
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