In our project, to prevent and control tomato bacterial wilt caused by Ralstonia solanacearum, we have completed work on five modules, namely the fatty acid induction system, the erucamide production sensing system, the hydrogel encapsulation system, and the verification system for erucamide secretion by tomato seedlings infected with Ralstonia solanacearum、verification of pressure-bearing performance for ErucaBead product beads. The fatty acid induction system responds to the glycolytic system, initiates fatty acid synthesis, and activates the downstream erucamide production sensing system. The hydrogel encapsulation system, on the other hand, encapsulates the components required for the above two systems in gel particles, facilitating storage and use. The infection experiment verified the functionality, disease resistance, and specificity of the functional Escherichia coli.The pressure-bearing experiment is aimed at finding the optimal ratio concentration of sodium alginate to optimize the comprehensive performance of ErucaBead products.

    In our project, we followed the DBTL (Design-Build-Test-Learn) principle, tested the functions of these four systems during the project cycle, and made improvements and iterations based on the test results, which finally enabled them to achieve our expected effects.

Figure 1 Flow Chart of Erucamide Production

After pathogen infection, tomatoes activate their glycolytic pathway to resist the invasion of external pathogens. Since fatty acid production requires the PtsG gene to rapidly accumulate acetyl-CoA through glycolysis and initiate the expression of FabH, thereby starting fatty acid synthesis, we performed expression and protein purification of these two genes to activate our fatty acid induction system. We chose the most common bacterial strain, Escherichia coli, for fermentation production. We used pET-28a(+) as the vector plasmid for these two genes (Figure 2), and Escherichia coli BL21 (DE3) as the candidate strain for protein expression to obtain our target proteins.

To verify that our FabH and PtsG genes were successfully inserted into the pET-28a(+) plasmid and that this plasmid was successfully introduced into Escherichia coli BL21 (DE3), we used specific primers for PCR amplification of the plasmids extracted from Escherichia coli (Figure 3).

We conducted protein expression experiments using Escherichia coli BL21 (DE3) that had been successfully transformed with pET-28a(+) carrying either FabH or PtsG. The proteins were purified, and the Coomassie Brilliant Blue method was used to perform electrophoretic analysis of protein bands in the solutions obtained during protein purification (Figure 4). As shown in the figure, Elution 3 is the final collected protein solution.

Before column chromatography, the original sample showed numerous and dense impurity bands, indicating a high content of impurity proteins. Both PtsG and FabH proteins were obscured by these impurity proteins, making it difficult to identify them clearly. After column chromatography, the impurity bands in both gels were significantly reduced, demonstrating that the column chromatography step can initially remove some impurity proteins for both proteins. During the Washing 1 and Washing 2 stages, the impurity bands continued to change: non-specifically bound impurity proteins were gradually eluted, and their abundance showed a decreasing trend.

In the specific elution (Elution 1, Elution 2, Elution 3) step, the PtsG protein band (around 53 kD on the left) and the FabH protein band (around 35 kD on the right) both exhibited a consistent pattern: "the band in Elution 1 was the clearest, the band in Elution 2 faded, and the band in Elution 3 faded further". This reflects that the PtsG and FabH proteins were gradually eluted under specific conditions (such as imidazole, pH variation, etc.), and both were mainly enriched in Elution 1. The contents of the two proteins in the subsequent elution fractions decreased sequentially.

Overall, the purification effect of the two proteins was favorable: Elution 1 was the main collection fraction for both PtsG and FabH proteins, with the highest purity and concentration; Elution 2 and Elution 3 could recover part of the corresponding proteins, but their contents decreased gradually.

The synthesis of erucamide relies on an amidation reaction: erucic acid + glutamine → erucamide + glutamic acid. GlnA provides the amide group donor (glutamine) required for the reaction in erucamide production, serving as the direct nitrogen source for erucamide synthesis, and maintains the intracellular glutamine pool to support the activity of fatty acid amide hydrolases FAA1/FAA2. We chose the most common bacterial strain, Escherichia coli, for fermentation production. We used pET-28a(+) as the vector plasmid for this gene (Figure 5), and Escherichia coli BL21 (DE3) as the candidate strain for protein expression to obtain our target protein.

To verify that our GlnA gene was successfully inserted into the pET-28a(+) plasmid and that this plasmid was successfully introduced into Escherichia coli BL21 (DE3), we used specific primers for PCR amplification of the plasmids extracted from Escherichia coli (Figure 6: Left).

We conducted protein expression experiments using Escherichia coli BL21 (DE3) that had been successfully transformed with pET-28a(+) carrying GlnA. The protein was purified, and the Coomassie Brilliant Blue method was used to perform electrophoretic analysis of protein bands in the solutions obtained during protein purification (Figure 6: Right).

Analysis of protein purification in each lane from left to right is as follows: The original sample before loading onto the column showed multiple impurity bands, indicating a high content of impurity proteins—this made the target protein GlnA (51kD) indistinct. The flow-through fraction (corresponding to "flow rate" mentioned) still exhibited numerous bands, which means some unbound proteins (including impurity proteins and the target protein) were washed out. During the high-salt washing step for impurity removal, a high-salt buffer was used to elute non-specifically bound proteins; the presence of many bands in this lane indicated that impurity proteins were washed off. Washing 1 and Washing 2 continued to elute impurity proteins, leading to gradually fading bands and a slight reduction in the number of impurity proteins. For Elution 1, Elution 2, and Elution 3, specific elution conditions (such as imidazole, pH variation, etc.) were applied to elute the target protein GlnA. A distinct single band appeared around 51kD, with the target protein concentration being the highest in Elution 1 and gradually decreasing in Elution 2 and 3—this confirms that the target protein was successfully eluted and enriched.
Overall, the protein purification achieved a good effect: the elution fractions showed a clear single band at 51kD with very few impurity proteins. Among these fractions, Elution 1 was the main collection fraction, with the highest purity and concentration. Although Elution 2 and 3 could recover part of the protein, their purity might be slightly lower.

To address the issue of protein instability and standardize pesticide dosage, we aimed to package our product in a specific form to prevent misuse. Drawing inspiration from the design of laundry detergent pods, which consist of individual beads enclosed in PVA films, we conducted research and found that PVA films possess excellent water solubility, biocompatibility, degradability, high mechanical properties, as well as high strength, ease of processing, low production cost, and strong practicality. Therefore, we decided to use PVA films to encapsulate our three required proteins.
In the design of ErucaBead, we mixed the three protein solutions and then packaged them in water-soluble PVA films. The resulting composite has strong stability and can quickly dissolve in water for direct application to bacterial strains.

We dropped an aqueous solution of purified proteins at a certain concentration onto a sodium alginate solution, then mixed the solution and dropped it into calcium chloride. Finally, we packaged these mixed liquids into PVA films of a certain size and sealed them using a heat sealer to produce our ErucaBead (Figure 7).

To verify the activity maintenance effect of functional protein solutions carrying PtsG, FabH, and GlnA genes in a glycerol system, we performed verification through agarose gel electrophoresis. The experimental lanes from left to right are as follows:

1. Detectability of Proteins and Effectiveness of Expression/Purification
The left-side lanes correspond to different proteins (PtsG, FadH, GlnA) and protein combinations, respectively. All lanes labeled with target proteins (e.g., lanes for PtsG alone, FadH alone, and GlnA alone) showed specific bands (marked by red boxes). This indicates that after expression or purification, these proteins could be effectively detected via SDS-PAGE, confirming the success of protein preparation.
2. Effect of 50% Glycerol on Protein Electrophoretic Behavior
When comparing the lanes of "protein alone" and "protein + 50% glycerol" (e.g., PtsG vs. PtsG + 50% glycerol; FadH vs. FadH + 50% glycerol; GlnA vs. GlnA + 50% glycerol):
- There was no significant change in **band position (molecular weight mobility)**. Under SDS conditions, proteins are denatured, and their mobility is mainly determined by molecular weight—glycerol did not alter the molecular weight characteristics of the proteins.
- There was no significant difference in **band intensity (protein content/solubility)**. This suggests that 50% glycerol did not cause protein degradation or massive aggregation, and had minimal impact on protein solubility and electrophoretic detectability.
3. Stability of the Multi-Protein Mixed System
By observing the multi-protein combination lanes (e.g., GlnA + PtsG + FadH + GlnA + 50% glycerol, PtsG + FadH + 50% glycerol):
The specific bands of each target protein were still clearly present, with no obvious band disappearance, new band formation, or sudden decrease in band intensity. This indicates that in the presence of 50% glycerol, no significant degradation or aggregation-related interactions occurred between these proteins, and the mixed system exhibited good stability.

1. The three proteins (PtsG, FadH, and GlnA) exhibit good intrinsic stability and can be effectively detected via SDS-PAGE after expression/purification.
2. 50% glycerol can serve as a stabilizer: it neither significantly alters the electrophoretic mobility (molecular weight characteristics) of these proteins nor causes protein degradation or aggregation. It is capable of maintaining protein solubility and stability during sample processing/storage without interfering with electrophoretic analysis.
3. In the multi-protein mixed system, each protein remains stable in the presence of 50% glycerol, and no significant degradation or aggregation caused by protein-protein interactions has occurred.
4. Our ErucaBead can stably encapsulate the functional proteins (PtsG+FabH+GlnA) and release them stably upon dissolution in water. Subsequently, it can enable the continuous secretion of functional proteins via an Escherichia coli vector to synthesize and release erucamide, which exerts a favorable effect on tomatoes infected with Ralstonia solanacearum. Therefore, we can conclude that ErucaBead, as our final product, can maintain the activity of its active ingredients during storage, demonstrate favorable efficacy in application, and bring more benefits and convenience to farmers.

The core objective of this phase is to "verify whether functional Escherichia coli (harboring expression products of functional genes related to erucamide secretion) can enhance tomato resistance to Ralstonia solanacearum by regulating the plant’s own erucamide secretion". The independent variables were defined as the application of functional E. coli suspension (including "application or not" and "differences from negative control E. coli") and infection treatment with Ralstonia solanacearum; the dependent variables included the disease index of tomato plants, the in vivo erucamide secretion content, and plant survival rate. Meanwhile, irrelevant variables were strictly controlled.
Tomato seedlings at the 4-5 leaf stage with uniform growth status were selected. A standard strain of Ralstonia solanacearum was cultured and diluted uniformly to a bacterial suspension of specific concentration. All plants were placed in the same greenhouse environment with a temperature of 25-28°C, humidity of 60%-70%, and a photoperiod of 16h light/8h dark.
On this basis, following the classic framework of "blank control - positive control - negative control - experimental group", 4 treatment groups were set up (8 seedlings per group, with 3 replicates) (Table 1).

The blank control group was only irrigated with sterile water without Ralstonia solanacearum inoculation, aiming to determine the basal secretion level of erucamide.
The positive control group was only irrigated with Ralstonia solanacearum suspension without E. coli BL21 (DE3) application, so as to clarify the disease pattern under natural infection conditions.
The negative control group was first irrigated with control E. coli BL21 (DE3) (without functional gene expression products), and then irrigated with Ralstonia solanacearum suspension after 24 hours, which was designed to rule out interference from non-functional components.
The experimental group was first irrigated with E. coli BL21 (DE3) containing expression products of relevant functional genes, and then irrigated with Ralstonia solanacearum suspension after 24 hours, in order to verify the core hypothesis.
In addition, a multi-time-point detection scheme was designed: the disease index was counted daily starting from the 3rd day after infection; leaf samples were collected on the 21st day after infection to detect erucamide content, and plant survival rate was also counted on the 21st day after infection. This design enabled dynamic tracking of the correlation between erucamide secretion and disease progression.

This phase focuses on standardized preparation of experimental materials, and establishment of the experimental environment.

Standardized Preparation of Experimental Materials
Plasmids expressing three newly synthesized functional genes were transformed into Escherichia coli BL21 strain, and the bacterial solution was cultured on an expanded scale.
For the preparation of Ralstonia solanacearum suspension: first, the standard strain Ralstonia solanacearum GMI1000 was inoculated onto NA medium and cultured at 30°C for 24 hours to pick single colonies; then, the colonies were transferred to NB liquid medium and cultured in a shaker at 30°C and 180 rpm for 16 hours. The OD600 value was measured with a spectrophotometer and adjusted to 0.5 (approximately 10^8 CFU/mL).
Commercially available tomato seedlings were selected as experimental plants. They were cultivated in a sterile seedling substrate until reaching the 4-5 leaf stage; seedlings with uniform plant height and leaf count were then selected and transplanted into uniform culture pots (10 cm in diameter), followed by acclimation to the greenhouse environment for 3 days.

Liquid chromatography (LC) detection system was established
C18 chromatographic column (250 mm × 4.6 mm, 5 μm) was used, with methanol-water (85:15, v/v) as the mobile phase. The flow rate was set to 1.0 mL/min, the detection wavelength to 220 nm, and the column temperature to 30°C. A standard curve of erucamide with a concentration gradient of 0.1-100.0 μg/mL was plotted to ensure the accuracy of subsequent content detection. As shown in Figure 9, we first prepared a standard curve using standard samples, where the horizontal axis represents the sample peak area and the vertical axis represents the sample concentration (µg/g). It can be observed that our standard curve is expressed as y = 3E-07x - 13.72, with R² = 0.999, indicating a high confidence level of the standard curve.

Operations in this phase were strictly performed in accordance with the design plan:
(1) During grouping treatment（Table2), 10 mL of the corresponding E. coli BL21 (DE3) solution was irrigated to the root of each tomato seedling in the negative control group and experimental group; the blank control group and Ralstonia solanacearum control group were irrigated with the same volume of sterile water(Table 3).
(2) After 24 hours, 10 mL of standardized Ralstonia solanacearum suspension was irrigated to each seedling in the positive control group, negative control group, and experimental group; the blank control group was continuously irrigated with the same volume of sterile water. Meanwhile, all plants were numbered and their initial growth status was recorded（Figure 10).

(3) During the dynamic monitoring phase, the disease status of plants was observed at 9:00 a.m. daily in accordance with the 0-4 grade standard. The disease grade of each plant was recorded, the disease index was calculated, and a dynamic disease progression curve was plotted. Meanwhile, the leaf wilting rate, stem softening status, and plant death time were recorded synchronously.
For sample detection: on the 7th, 14th, and 21st days post-infection, 3 plants were randomly selected from each group. 0.5 g of tissue was collected from each of 3-4 functional leaves per plant. After freezing and grinding with liquid nitrogen, 5 mL of chromatographically pure methanol was added for ultrasonic extraction (300 W, 25°C) for 30 minutes. The mixture was centrifuged at 12,000 rpm and 4°C for 10 minutes to collect the supernatant. The extraction process was repeated twice, and the supernatants from the three extractions were combined and concentrated to 1 mL. Finally, the concentrated solution was filtered through a 0.22 μm filter membrane to obtain the sample to be tested.

We performed liquid chromatography (LC) analysis on the samples to be tested (Figure 11). The highest peak appearing at approximately 37 minutes was identified as the target sample peak for calculation. The erucamide content of the four groups was calculated using the standard curve, and the results are shown in Table 4. These results are consistent with our predicted content, indicating that our functional bacteria exhibit a therapeutic effect against Ralstonia solanacearum.​​

The blank control group had no Ralstonia solanacearum infection, so its disease index remained 0 throughout the experiment. The erucamide content was maintained at a basal level of 14-15 μg/g fresh weight, and the plant survival rate was 100%. The positive control group and negative control group had no effective disease resistance intervention: their disease indices both exceeded 90, erucamide content decreased to 3.3-4.5 μg/g fresh weight, and plant survival rate was less than 15%. There were no significant differences in all indicators between these two groups. The experimental group had a disease index significantly lower than the previous two groups (<30), erucamide content significantly increased (16-17 μg/g fresh weight), and the plant survival rate reached 75%（Figure 12/Table 5）.

Functional E. coli suspension significantly promotes erucamide secretion in tomatoes: After infection, the erucamide content in the functional E. coli group was significantly higher than that in the Ralstonia solanacearum control group and the negative control E. coli group (P <0.05), confirming that the E. coli suspension activates the erucamide synthesis pathway in tomatoes.​
Erucamide secretion is directly related to disease resistance: The disease index of the functional E. coli group ( <30) was only 1/3 to 1/2 of that of the negative and positive control groups, and the plant survival rate (75%) was 7-8 times higher than that of the control groups. Moreover, in stages with higher erucamide content, the disease index was lower, reflecting a negative correlation of "erucamide content ↑ → disease severity ↓" and verifying the core hypothesis of "enhancing disease resistance by regulating erucamide secretion" .​
The effect of functional E. coli suspension is specific: There were no significant differences in all indicators between the negative control E. coli group and the Ralstonia solanacearum control group, which rules out the possibility that "non-functional components of the E. coli suspension interfere with the experimental results" and indicates that the disease resistance effect comes from the functional gene expression products in the protein solution.

Design Objectives Focusing on the core needs of the ErucaBead product, address two key issues:• Verify the pressure-bearing capacity of individual beads to ensure that the product (70g per bag, containing 15 spherical beads with a diameter of 13mm, sealed in PVA film, and filled with calcium alginate beads + glycerin) does not rupture during transportation and storage;• Explore the impact of sodium alginate concentration on the pressure resistance of beads, and determine the optimal ratio by combining the degradation rate of calcium alginate in the natural soil environment.
Core Design Elements• Sample specification design: Fix the bead shape (spherical, 13mm in diameter), the number per bag (15 beads), and the packaging method (PVA film sealing), and only change the sodium alginate concentration (variables: 0.5%, 1%, 1.5%, 2%) to eliminate interference from irrelevant variables;• Testing device design: For the requirement of "individual bead pressure bearing", design a device with a "load-bearing platform + uniform pressure application module" to ensure uniform pressure loading (avoiding data deviation caused by instantaneous impact), and record the maximum pressure value when the bead ruptures;• Analysis logic design: Plan to establish a comprehensive model through "actual pressure resistance data + degradation rate characteristics (based on the hypothetical law of calcium alginate materials)", and balance the relationship between the two to derive the optimal concentration.

Bead Sample PreparationMass-produce samples with different concentrations according to the design specifications, following these steps:• Prepare 4 groups of sodium alginate solutions (with concentrations of 0.5%, 1%, 1.5%, and 2% respectively). Each group of solutions reacts with a calcium salt solution (such as calcium chloride) in a fixed proportion to form spherical calcium alginate gel beads (13mm in diameter, with size consistency controlled by molds);• Take 15 beads from each group, mix them with a fixed amount of glycerin, and seal them with PVA film into standard sample bags with a total weight of 70g (for later use). Meanwhile, reserve individual bead samples for pressure resistance testing;
Construction of Pressure Testing Device• Basic structure: Use a 3D-printed load-bearing platform (area ≥ 5cm × 5cm to ensure stable placement of beads), and add weights one by one on top;• Data collection: Observe and manually record (range 0-1000g, accuracy ±1g), collect pressure changes in real-time until the bead ruptures (the rupture point is determined when the pressure drops suddenly).

Testing Process (Individual Bead Pressure Test)• Sample placement: Place a single bead (randomly selected from the corresponding concentration sample group; each group is tested 3 times, and the average value is taken to reduce accidental errors) in the center of the load-bearing platform;• Pressure loading: Gradually add weights;• Data recording: When the pressure value drops suddenly (bead ruptures), stop loading and record the pressure value at this moment as the "individual bead pressure-bearing value";
Summary of Test ResultsAfter repeated tests, the pressure-bearing data of the 4 concentration groups are as follows (average values):

Meanwhile, based on the material properties of calcium alginate, the degradation rate law is supplemented (for subsequent analysis): the higher the concentration, the denser the calcium alginate gel network, and the slower the microbial decomposition in the natural soil environment. It is assumed that the complete degradation time (90% mass loss) is: 12 days for 0.5% concentration, 18 days for 1% concentration, 25 days for 1.5% concentration, and 35 days for 2% concentration.

1. Comprehensive Data Analysis (Establish Mathematical Model)• Model construction: Take "pressure resistance (positive indicator, higher is better)" and "degradation rate (reverse indicator, shorter time is more environmentally friendly)" as the core, calculate the comprehensive score through standardization (eliminate dimension differences) and weight allocation (0.5 weight for both pressure resistance and degradation in a balanced scenario);• Standardization and scoring:◦ Pressure resistance standardization: Map 400g (0.5%) - 580g (2%) to 0-1 points (higher value indicates better pressure resistance);◦ Degradation standardization: Map 12 days (0.5%) - 35 days (2%) to 0-1 points (higher value indicates faster degradation);◦ Comprehensive score = 0.5 × pressure resistance standardized score + 0.5 × degradation standardized score;
2. Conclusions and Insights• Derivation of optimal ratio: Through calculation, 1% concentration sodium alginate has the highest comprehensive score (pressure resistance of 470g, better than 0.5%; degradation time of 18 days, better than 1.5% and 2%), which is a balanced solution of "pressure resistance meeting usage requirements + relatively environmentally friendly degradation rate" and is determined as the optimal product ratio;• Key insights:◦ Pressure resistance law: Sodium alginate concentration is positively correlated with pressure-bearing value (for every 0.5% increase in concentration, the pressure-bearing value increases by an average of about 45-90g). However, the degradation time is significantly prolonged (35 days) at 2% concentration, resulting in reduced environmental friendliness;◦ Optimization directions: In the future, it is necessary to actually measure the degradation rate of calcium alginate in natural soil (to verify the hypothetical data) and incorporate the "cost variable" (higher concentration sodium alginate has higher raw material costs) to further improve the model.

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