CN115720906B - Application of glycoside hydrolase BvGH18 in preventing and controlling plant mites - Google Patents
Application of glycoside hydrolase BvGH18 in preventing and controlling plant mites Download PDFInfo
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- CN115720906B CN115720906B CN202211295304.6A CN202211295304A CN115720906B CN 115720906 B CN115720906 B CN 115720906B CN 202211295304 A CN202211295304 A CN 202211295304A CN 115720906 B CN115720906 B CN 115720906B
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- 102000005744 Glycoside Hydrolases Human genes 0.000 title claims abstract description 31
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- Agricultural Chemicals And Associated Chemicals (AREA)
Abstract
The invention belongs to the technical field of agricultural microbiology, and particularly relates to application of glycoside hydrolase BvGH18 in controlling plant mites. The gene of the glycoside hydrolase BvGH18 is constructed on a cold shock vector pColdII through a genetic engineering means and expressed in escherichia coli BL21 (DE 3) to obtain recombinant protein BvGH18, and the glycoside hydrolase BvGH18 belongs to the GH18 glycoside hydrolase family through protein sequence comparison analysis. Experiments prove that the BvGH18 protein has a certain chitinase activity: 0.299 U/mg, namely, the half-lethal concentration of tetranychus urticae is 4.826 mug/mL, the half-lethal concentration of tetranychus cinnabarinus is 24. h is 8.483 mug/mL, and the half-lethal concentration of tetranychus citri is 17.421 mug/mL. The invention provides a new selectivity for the biological control of plant mites.
Description
Technical Field
The invention belongs to the technical field of agricultural microbiology, and particularly relates to application of glycoside hydrolase BvGH18 in controlling plant mites.
Background
Tetranychus (Tetranychus) belongs to the arachnidae, acarina, europe order, tetranychidae. As phytophagous mites, a large variety of spider mites seriously affect grain crops, commercial crops and ornamental plants, including famous spider mites (Tetranychus urticae), spider mites (Tetranychus cinnabarinus) and Panonychus citri (Panonechus citri), and seriously jeopardize the yield and quality of commercial crops such as fruits, vegetables, cotton, tea and the like in China. The spider mites have tiny body shapes, are usually eaten by the back surfaces of the leaves, are not easy to be perceived, and do not show obvious harmful symptoms in the early stage of crop damage, so the damage is easy to be ignored. In addition, the spider mites have the characteristics of high breeding speed, strong adaptability, wide hosts, easiness in generating drug resistance and the like, and are extremely easy to cause disasters once eruption.
At present, the traditional chemical control method is mostly adopted for prevention, control and treatment of the spider mites, and along with abuse of chemical acaricides, the drug resistance of the spider mites is greatly increased, so that the mite injury is more serious, and the environmental protection and sustainable development of agricultural environments are not facilitated. Most of the acaricides on the market are poorly water-soluble chemical substances or antibiotics, and compared with the prior art, small molecular substances such as proteins are less reported. Therefore, the development of a green and efficient She Mansheng anti-preparation by using a new means is a problem to be solved urgently by the person skilled in the art, and has very important practical significance.
Disclosure of Invention
The invention aims to provide an application of glycoside hydrolase BvGH18 or a fermentation product containing the glycoside hydrolase BvGH18 in controlling plant mites, wherein the glycoside hydrolase BvGH18 is shown as SEQ ID NO. 2.
Another object of the invention is to provide the use of the glycoside hydrolase BvGH18 in the preparation of spider mite acaricides.
In order to achieve the above purpose, the present invention adopts the following technical scheme:
use of a glycoside hydrolase BvGH18 or a fermentation product comprising a glycoside hydrolase BvGH18 for controlling plant mites, said glycoside hydrolase BvGH18 being represented by SEQ ID No.2 or being the protein of SEQ ID No.2 to which the remaining gene expression elements are added, said elements comprising: enhancers, purification tags, and the like;
the purification tag includes: affinity purification tags, fluorescent tags, thioredoxin and other fusion protein tags.
The application process comprises the step of using glycoside hydrolase BvGH18 as one of the active ingredients or the only active ingredient for killing plant mites, wherein the killing mode is contact killing;
the application of the glycoside hydrolase BvGH18 or the fermentation product containing the glycoside hydrolase BvGH18 in preparing the preparation for killing the spider mites comprises the step of preparing the spider mite killing agent by taking the protein shown as SEQ ID NO.2 as one of the active ingredients or the only active ingredient.
In the above application, preferably, the spider mite is Tetranychus urticae or Tetranychus cinnabarinus, and Panonychus citri.
Compared with the prior art, the invention has the following advantages:
the invention reports that the 18-family glycoside hydrolase has acaricidal activity for the first time, and provides a new enzyme source for the preparation of novel acaricide.
The acaricide containing the glycoside hydrolase BvGH18 has the characteristics of high efficiency, low toxicity and environmental friendliness, and has good application prospect in the aspect of biological control of spider mites.
Drawings
FIG. 1 shows an SDS-PAGE analysis of purified glycoside hydrolase BvGH18.
FIG. 2 is a graph showing the effect of glycoside hydrolase BvGH18 on Tetranychus urticae.
FIG. 3 is a glycoside hydrolase BvGH18 chitinase activity assay.
Detailed Description
The experimental methods in the examples below, unless otherwise specified, are all reported microbiological routine procedures. The reagents or materials are conventional in the art unless specifically indicated.
The BvGH18 protein referred to in the invention may be obtained in a manner conventional in the art, such as prokaryotic expression, commercial synthesis, etc. The invention takes prokaryotic expression BvGH18 protein as an example to describe the mite-inhibiting activity, and the protein obtained by other modes can also perform the same function.
Example 1:
acquisition of acaricidal BvGH18 protein
(1) Constructing a recombinant plasmid:
according to the sequence shown in SEQ ID NO.1 (encoding the protein shown in SEQ ID NO. 2), a BvGH18 protein gene fragment BvGH18 (Beijing engine biotechnology Co., ltd.) is artificially synthesized and connected to an escherichia coli cold shock protein expression vector pColdII to obtain a recombinant expression plasmid pColdII-BvGH18.
(2) Expression and purification of acaricidal BvGH18 protein gene in escherichia coli
The recombinant plasmid pColdII-bvgh18 was introduced into E.coli BL21 (DE 3) to obtain recombinant strain BL21 (DE 3)/pColdII-bvgh 18. Selecting recombinant strain monoclonal, inoculating into 50mL LB liquid medium (containing ampicillin with final concentration of 100 μg/mL), shake culturing at 37deg.C and 200rpm/min to OD 600 To reach 0.8, isopropyl-B-D thiogalactoside (i.e. IPTG) with a final concentration of 1.0mmol/L was added for induction culture at 20℃for 12h. The 50mL recombinant BL21 (DE 3)/pColdII-bvgh 18 IPTG induction culture was centrifuged at 8,000rpm for 5min to collect the cells, then 10mL 10mmol/L PBS buffer was used to resuspend the cells, the cells were sonicated on ice (ultrasonic power 300W, disruption 10s, intermittent 10s, treatment 10 min), and the supernatant of the bacterial lysate was collected by centrifugation at 12,000rpm for 15min, then the impurities were filtered with a filter membrane with a pore size of 0.22. Mu.m, and the target protein was purified by using a His tag protein purification column.
The recombinant protein sequence expressed by the escherichia coli is respectively a translation enhancer, a His tag and a target protein BvGH18 sequence from the N-terminal to the C-terminal (a protein sequence shown by SEQ ID NO.2, and the theoretical molecular weight of the protein sequence is about 48.3 kDa), and the theoretical protein molecular weight of the protein sequence is about 49.7kDa. SDS-PAGE electrophoresis detection is carried out on the purified recombinant protein solution, and the result is shown in figure 1 and is basically consistent with the expected molecular weight of the recombinant protein, so that the BvGH18 protein of the invention is proved to be successfully expressed in escherichia coli.
Example 2:
1) Spider mite killing activity of BvGH18 protein:
reference is made to the tetranychus slide dipping method, a standard method recommended by FAO (national grain and agricultural organization). Cutting the double-sided adhesive tape into square with length of 2-3cm, attaching to one end of the glass slide, removing paper sheet on the adhesive tape, selecting female adult mites with consistent size, bright body color and active action by using a number 0 writing brush, and attaching the back of the female adult mites to the double-sided adhesive tape (note: not to adhere to mite feet, mite beards and mouthparts). Placing in biochemical incubator with temperature 25deg.C and relative humidity of 85% for 2-3 hr, and removing dead, injured and inactive individuals by binocular microscopy. Diluting the reagent to be tested (the supernatant of the bacterial lysate before BvGH18 protein in example 1 is subjected to column purification) with 10mmol/L PBS buffer solution for 5-7 concentration gradients on the basis of pre-test, immersing one end of the mite-carrying slide in the liquid medicine for 5s, taking out the mite-carrying slide after gentle shaking, rapidly sucking away the excessive liquid medicine around the mite body, then placing the mite-carrying slide in the biochemical incubator, and observing the test result by using binoculars after 24 hours. The writing brush is used for dabbing mites, and the people with the mite and the foot are dead. Each treatment was repeated 3 times with an additional 10mmol/L PBS buffer as a blank. The bioassay experiment shows that the BvGH18 protein crude enzyme solution before purification shows good acaricidal activity.
The results of the biological assay of BvGH18 protein suspension (purified BvGH18 protein prepared in example 1) against Tetranychus urticae (Tetranychus urticae) are shown in Table 1, following the above experimental procedure. The probability unit model equation of the BvGH18 insecticidal protein is PROBIT (P) = -1.312+1.920X (variable X is converted by using the logarithm with the base of 10) which is obtained by calculation by using SPSS 26.0 data processing software, and the Pearson model fitting goodness test X 2 =0.490, p=0.921, indicating a good model fit. LC treatment of spider mites (Tetranychus urticae) with BvGH18 protein suspensions for 24h by observing confidence intervals (see table 2) 50 ＝4.826μg/mL。
TABLE 1 determination of acaricidal Activity of BvGH18 protein against Tetranychus urticae
TABLE 2 concentration and 95% confidence interval for different death probabilities
According to the experimental steps, the results of the biological measurement of BvGH18 protein suspension on tetranychus cinnabarinus (Tetranychus cinnabarinus) and Panonychus citri (Panoneichus citri) are counted and calculated by using SPSS 26.0 data processing softwareLC of BvGH18 protein suspension under 24h treatment of Tetranychus cinnabarinus (Tetranychus cinnabarinus) and Panonychus citri (Pannychus citri) 50 The values were 8.483. Mu.g/mL and 17.421. Mu.g/mL, respectively.
(2) Chitinase Activity assay of BvGH18 protein:
the chitinase activity of the recombinant protein BvGH18 is determined by adopting a salicylic acid method which is commonly used at present:
preparing colloid chitin: 1g of chitin is weighed into a triangular flask, 20mL of concentrated hydrochloric acid is added, the mixture is stirred by a magnetic stirrer for 12h until the chitin is completely dissolved, then the solution is added into 200mL of pre-cooled sterile water, and the mixture is kept stand at 4 ℃ for 12h. And centrifuging to collect precipitate, re-suspending with sterile water, centrifuging again, repeatedly washing with water and centrifuging until the pH value of the solution is neutral to obtain colloidal chitin, and finally adjusting the concentration of the colloidal chitin to 1.0% with 20mmol/L PBS buffer. 100uL of protein solution to be tested and 100uL of 1.0% colloidal chitin solution are uniformly mixed, and are placed in a constant-temperature water bath kettle at 37 ℃ for incubation for 1h, and then are subjected to boiling water bath for 5min. After cooling, centrifuging at 8,000rpm at normal temperature for 10min, taking 160 mu L of supernatant, uniformly mixing with 40 mu L of 3, 5-dinitrosalicylic acid (DNS) reagent, reacting in boiling water bath for 10min, immediately placing on ice, and cooling to room temperature. The supernatant was measured in a 96-well plate to have an absorbance at 540nm of 0.0047.+ -. 0.0005. In the enzyme activity measurement process, N-acetylglucosamine (NAG) is used as a control of the DNS color reaction, and a standard curve is drawn as shown in FIG. 3. Definition of enzyme activity: the amount of enzyme that produces 1. Mu. Mol NAG per mg of chitin per hour at 37℃is one enzyme activity unit. The chitin activity of BvGH18 protein is calculated to be 0.299+/-0.011U/mg.
Claims (7)
1. Use of a glycoside hydrolase BvGH18 or a fermentation product containing the glycoside hydrolase BvGH18 in controlling plant mites, wherein the glycoside hydrolase BvGH18 is shown as SEQ ID No.2 or is a protein of SEQ ID No.2 to which a gene expression element is added, and the gene expression element comprises: enhancer, purification tag, plant mite is caused by Tetranychus urticae, tetranychus cinnabarinus and Panonychus citri.
2. The use according to claim 1, wherein the purification tag is: affinity purification tags, fluorescent tags, thioredoxin.
3. The use according to claim 1, wherein the glycoside hydrolase BvGH18 or the fermentation product containing the glycoside hydrolase BvGH18 is used as one or only effective component for killing plant mites.
4. The use according to claim 1, wherein the killing means during use is contact killing.
5. Use of glycoside hydrolase BvGH18 or a fermentation product comprising glycoside hydrolase BvGH18 in the preparation of a spider mite-killing formulation.
6. The use according to claim 5, wherein the tetranychus killing agent is prepared by using glycoside hydrolase BvGH18 or a fermentation product containing glycoside hydrolase BvGH18 as one of the active ingredients, or the only active ingredient.
7. The use according to claim 5, wherein the spider mite is Tetranychus urticae, tetranychus cinnabarinus or Tetranychus cinnabarinus.
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| CN117481145B (en) * | 2023-10-26 | 2024-05-10 | 湖北省生物农药工程研究中心 | Chitin binding protein BvCBP and application of compound thereof in preparation of plant mite-killing agent |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0254442A1 (en) * | 1986-07-07 | 1988-01-27 | North Carolina State University | Method of controlling plant feeding mites with the fungus neozygites floridana |
| CN101613685A (en) * | 2009-05-20 | 2009-12-30 | 广东省昆虫研究所 | Have the active combined chitinase of Di Siwa mite and the application thereof of killing |
| AU2020102670A4 (en) * | 2020-10-12 | 2020-12-03 | Shihezi University | Applications of ABC Transport Proteins in Agricultural Spider Mite Control and Bt Resistance Management |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0254442A1 (en) * | 1986-07-07 | 1988-01-27 | North Carolina State University | Method of controlling plant feeding mites with the fungus neozygites floridana |
| CN101613685A (en) * | 2009-05-20 | 2009-12-30 | 广东省昆虫研究所 | Have the active combined chitinase of Di Siwa mite and the application thereof of killing |
| AU2020102670A4 (en) * | 2020-10-12 | 2020-12-03 | Shihezi University | Applications of ABC Transport Proteins in Agricultural Spider Mite Control and Bt Resistance Management |
Non-Patent Citations (1)
| Title |
|---|
| NCBI.MULTISPECIES:glycoside hydrolase family 18 protein[Bacillus].Genbank:wp032872147.1.2020,1. * |
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