CN108642029A - Green muscardine fungus protease P r1C and its gene and application - Google Patents
Green muscardine fungus protease P r1C and its gene and application Download PDFInfo
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- CN108642029A CN108642029A CN201810599450.5A CN201810599450A CN108642029A CN 108642029 A CN108642029 A CN 108642029A CN 201810599450 A CN201810599450 A CN 201810599450A CN 108642029 A CN108642029 A CN 108642029A
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- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
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- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
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Abstract
The invention belongs to agricultural biological technical fields, and in particular to green muscardine fungus protease P r1C and its gene and application.The present invention has obtained green muscardine fungus extracellular protease Pr1C genes by gene clone technology, and it expresses and obtains Pr1C albumen, functional verification has been carried out to the albumen by the method for artificial feeding locust, it was found that protease P r1C can obviously increase green muscardine fungus virulence, green muscardine fungus is promoted to kill the efficiency of locust.
Description
Technical field
The invention belongs to agricultural biological technical fields, and in particular to green muscardine fungus protease P r1C and its gene and application.
Background technology
Locust is the main agricultural pests in China, it has the characteristics that type is more, harm is serious and population outbreak often,
Heavy losses are often resulted in Chinese national economy, especially agricultural production.In recent years, as global warming trend increases,
High density locust swarm occurs now and then, and risk of migrating at a distance aggravation seriously threatens the grain-production of China agricultural main producing region.Existing disease
Pest control excessively relies on chemical pesticide mostly based on emergence control and chemical prevention to the prevention and control of plant diseases, pest control, causes to pollute environment,
Thus there is an urgent need for develop novel green non-environmental pollution control pest method.
Invention content
In order to overcome the problems, such as to rely on chemical pesticide present in existing locust pest control method, cannot prevent in advance,
The present invention provides a kind of green muscardine fungus protease P r1C, can dramatically increase the virulence of green muscardine fungus, improve green muscardine fungus and kill locust
The efficiency of worm.
The purpose of the present invention is to provide a kind of green muscardine fungus protease P r1C.
It is still another object of the present invention to provide the genes for encoding above-mentioned green muscardine fungus protease P r1C.
Another object of the present invention is to provide the recombinant expression containing the gene for encoding above-mentioned green muscardine fungus protease P r1C and carries
Body.
Another object of the present invention is to provide the recombinant bacterial strain containing the gene for encoding above-mentioned green muscardine fungus protease P r1C.
Another object of the present invention is to provide the preparation method of green muscardine fungus protease P r1C.
Another object of the present invention is to provide the purposes of green muscardine fungus protease P r1C.
Specific implementation mode according to the present invention, the amino acid sequence such as SEQ ID of green muscardine fungus protease P r1C of the invention
NO：Shown in 1：
The amino acid sum of above-mentioned green muscardine fungus protease P r1C is 708, weight average molecular weight 75036.
Specific implementation mode according to the present invention encodes the nucleotide sequence of the gene of above-mentioned green muscardine fungus protease P r1C such as
Such as SEQ ID NO：Shown in 2：
Specific implementation mode according to the present invention, the present invention are provided comprising the gene for encoding above-mentioned green muscardine fungus protease P r1C
Recombinant expression carrier, preferably this carrier be pET-Pr1C plasmids.
Specific implementation mode according to the present invention, the present invention are provided comprising the gene for encoding above-mentioned green muscardine fungus protease P r1C
Recombinant bacterial strain, which is preferably Escherichia coli.
Specific implementation mode according to the present invention, the method for preparing green muscardine fungus protease P r1C, includes the following steps：
(1) will include to encode above-mentioned green muscardine fungus protease P r1C genes to be inserted into expression vector；
(2) host cell is converted with the recombinant expression carrier comprising coding green muscardine fungus protease P r1C genes；
(3) host cell, the r1C expression of induction green muscardine fungus protease P are cultivated.
Green muscardine fungus (Metarhizium anisopliae) is a kind of insect pathogenic fungus being widely present, it can be parasitic
It invades in host insects body in various pests and by body surface, is constantly proliferated in pest body, consumption nutrition, mechanical penetration, production
Raw toxin, and constantly propagated in pest population, keep pest lethal.Green muscardine fungus has certain specificity, to person poultry harmless, together
When also have many advantages, such as that free from environmental pollution, pest will not develop immunity to drugs and develop microbial insecticide preparation using it there is good hair
Exhibition foreground.However, in the practical application of green muscardine fungus, responding time is long, affected by environment big.
Green muscardine fungus extracellular protease Pr1C according to the present invention can act on aspartic acid and paddy ammonia in insect cuticle
The carboxyl of acid, protein degradation matter generate synergistic effect, improve green muscardine fungus and kill by combining artificial feeding locust with green muscardine fungus
The efficiency of locust can obviously increase green muscardine fungus virulence.
Description of the drawings
The protein expression situation of the stiff mycoproteinase Pr1C of Fig. 1 displays；
Fig. 2 is locust survival rate line chart.
Specific implementation mode
1. selected insect source
Experiment migratory locusts purified population used is artificial feeding population.Migratory locusts locust egg is hatched in artificial climate incubator, is incubated
Change condition is：30 ± 2 DEG C of temperature, humidity 60%, light application time:Interlunation=16h:8h.The size that the same time is hatched
The consistent nymph of a locust is transferred in insect cage (60cm × 50cm × 60cm), is raised with fresh wheat seeding, until adult.Raising
Condition：Light application time:Interlunation=16h:8h, 30 ± 2 DEG C of temperature, relative humidity 60%.
2. strains tested
Raw survey has Asiatic migrotory locust very high virulence to green muscardine fungus IPPM202 indoors.
Under the conditions of 28 DEG C, with PDAY culture mediums (potato 200g, agar 20g, sucrose 20g, yeast powder 5g, water 1000m
L 15d) is cultivated, is preserved in 4 DEG C after scraping conidium drying.Spore content and measurement are calculated under blood counting chamber using preceding
Spore germination rate is handled according to effective spore content.
Embodiment 1 clones green muscardine fungus Pr1C genes
The extraction of green muscardine fungus total serum IgE is usedSeparation agent extracts the RNA of green muscardine fungus tissue sample, reverse transcription
Kit carries out reverse transcription, clones Pr1C genes, and specific primer is shown in Table 1, obtains nucleotide sequence as shown in SEQ ID No.2
Green muscardine fungus protease P r1C genes.
Table 1 clones the specific primer of Pr1C genes
By green muscardine fungus protease P r1C gene digestions, digestion products are inserted into pET-21b expression vectors, obtain plasmid pET-
Pr1C。
Connection product is converted into escherichia coli DH5a bacterial strain, is screened according to the mark (anti-Amp) of recombinant vector, picking list
Spot, alkaline lysis extract plasmid, double digestion Preliminary Identification in a small amount.Plasmid pET-Pr1C is transformed into BL21 (DE3) competent bacteria
In.SDS-PAGE electrophoresis is carried out, testing goal protein expression situation, the results are shown in Figure 1.
Embodiment 2 measures locust survival rate after feeding green muscardine fungus PR1C albumen
It selects the consistent locust 3 age nymph of growth conditions to be tested, 3 processing groups and 2 control groups, processing is set altogether
Group is：The processing of PR1C+ Metarhizium Strains 202, PR1C processing, the processing of Metarhizium Strains 202；Control group is：Induction bacterium, blank
Group.Each processing group and control group are equipped with 5 repetitions, each to repeat have 30 locusts.
The locust selected is put into constant incubator, 28 DEG C, light and dark ratio 16h:8h is cultivated, after Nature enemy 12h,
Man-made feeds are fed, fresh wheat seeding is replaced afterwards for 24 hours, records daily death toll, locust survival rate the results are shown in Table 2 and Fig. 2：
The 2 locust survival rate table of comparisons of table
According to experimental result, the crude survival rate of the blank control group of untreated locust declines from initial 84.7%
To 77.3%, natural mortality rate 7.5%；In feed individually plus after PR1C, the survival rate of locust drops to from 78.7%
71.3%, the death rate 7.4% does not change compared with blank group；But it is fed jointly with Metarhizium Strains with PR1C
After locust, drop to 36.7% from 71.3% in the survival rate of locust 5 days, survival rate only has initial half, at the 10th day
Locust survival rate only has 28%.
The protease P r1C of the present invention can act on the carboxyl of aspartic acid and glutamic acid in insect cuticle, egg of degrading
White matter, protease P R1C generate synergistic effect with green muscardine fungus, are obviously improved for green muscardine fungus virulence, in stiff bacterium to entomopathogenic power
Aspect plays an important role.
Sequence table
<110>Plant Protection institute, Chinese Academy of Agricultral Sciences
<120>Green muscardine fungus protease P r1C and its gene and application
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 708
<212> PRT
<213>Green muscardine fungus IPPM202 (Metarhizium anisopliae IPPM202)
<400> 1
Met Asp Cys Asn Gly His Gly Thr Asn Ala Ala Gly Ile Ile Gly Thr
1 5 10 15
Arg Pro Asn Ala Met Gly Phe Thr Gly Ala Ala Pro Gly Ala Gln Leu
20 25 30
Gly Met Tyr Arg Ile Thr Cys Ser Gly Glu Phe Pro Thr Asp Val Met
35 40 45
Val Asp Ala Ile Tyr Arg Ala Leu Ala Asp Gly Val Asp Ile Ile Ser
50 55 60
Ser Ser Ala Gly Leu Pro Gly Gly Trp Pro Asp Ser Leu Leu Ser Ser
65 70 75 80
Ala Ala Thr Arg Ala Val Glu Ser Gly Val Val Phe Val Gln Gly Ala
85 90 95
Gly Asn Asp Gly Thr Leu Gly Leu Phe Ser His Leu Asp Pro Ala Val
100 105 110
Gly Asn Gly Val Ile Ser Val Gly Ser Val Asn Ser Arg Val Tyr Pro
115 120 125
Gln Leu Ile Asn Glu Ala Lys Tyr Thr Ile Gly Asn Gly Ser Glu Val
130 135 140
Pro Phe His Phe Phe Pro Thr Leu Pro Ser Asp Asn Phe Thr Gly Thr
145 150 155 160
Pro Met Glu Val Tyr Ala Leu Pro Val Asn Gly Ser Gly Ala Gly Asn
165 170 175
Asp Thr Arg Ala Cys Asp Pro Leu Pro Ser Asp Thr Pro Asp Leu Ser
180 185 190
Asn Lys Leu Val Leu Leu Asn Phe Arg Ser Gly Arg Gly Asp Cys Ser
195 200 205
Leu Arg Asn Arg Thr Lys Ala Val His Glu Lys Gly Ala Ala Arg Ile
210 215 220
Leu Ala Tyr Val Ala Asp Glu Asp Trp Leu Pro Asp Ile Tyr Tyr Val
225 230 235 240
Asp Asn Leu Pro Glu Gly Val Leu Ala Leu Gly Met Leu Gly Phe Asp
245 250 255
Thr Ala Thr Glu Met Leu Lys Ala Leu Gln Ser Gly Arg Lys Val Leu
260 265 270
Ala Thr Val Phe Pro Tyr Asn Asp Ala Pro Arg Val Tyr Ile Glu Glu
275 280 285
Pro Asn Asp Glu Ile Ala Gly Ser Val Ser Asp Phe Ser Ser Trp Gly
290 295 300
Pro Ser Trp Asn Leu Gly Leu Lys Pro Ser Leu Thr Ala Val Gly Gly
305 310 315 320
Glu Ile Ile Ser Thr Asp Phe Arg Glu Thr Asn Pro Ser Gly Tyr Thr
325 330 335
Ile Thr Arg Gly Thr Ser Phe Ser Gly Pro Leu Ile Ala Ala Leu Val
340 345 350
Ala Leu Ile Gly Glu Ala Arg Gly Ser Leu Asp Pro Ala Thr Val Glu
355 360 365
Ser Leu Leu Val Ser His Ser Asn Pro Gln Leu Tyr His Asp Gly Glu
370 375 380
Lys Phe Leu Pro Tyr Leu Ala Pro Val Ala Gln Gln Gly Gly Gly Leu
385 390 395 400
Ala Arg Ala Tyr Asp Ala Ala Tyr Ala Thr Thr Leu Val Gln Pro Ala
405 410 415
Gly Leu Asn Phe Asn Asp Thr Glu His Met Ala Ala Ser Leu Asn Phe
420 425 430
Thr Ile Lys Asn Val Gly Gln Gly Ala Ile Thr Tyr Arg Leu Ser His
435 440 445
Val Pro Ala Val Thr Val Tyr Thr Phe Thr Glu Asn Gly Thr Val Ser
450 455 460
Ser Tyr Pro Asn Lys Leu Glu Ala Val Glu Thr Pro Ala Ala Ile Thr
465 470 475 480
Leu Ser Asp Thr Ser Val Thr Val Asp Pro Gly Asn Ser Val Asn Ile
485 490 495
Arg Val Ser Ala Ser Ile Pro Glu Gly Leu Asp Ala Ser Arg Met Pro
500 505 510
Leu Trp Ser Gly Trp Ile Ala Ile Asn Gly Ser Asp Ser Thr Ser Leu
515 520 525
Ser Val Pro Tyr Gln Gly Phe Ser Gly Ser Ile Arg Lys His Gln Val
530 535 540
Leu Arg Pro Asp Gly Ala Ser Leu Thr Tyr Arg Asn Ala Ser Val Thr
545 550 555 560
Glu Gly Thr Thr Val Val Leu Pro Ala Pro Gly Ser Ile Thr Pro Ser
565 570 575
Gln Leu Val Leu Asn Ile Asn Ala Thr Met Gly Ile Pro Leu Val Arg
580 585 590
Ala Glu Val Val Pro Ala Asn Gly Thr Ala Asn Ala Thr Asp Ile Thr
595 600 605
Thr Ser Ile Gly Gln Val Gln Gly Phe Pro Val Gln Trp Arg Pro Arg
610 615 620
Asn Leu Gln Gln Asp Ser Asn Ser Pro Asp Leu Leu Gln Phe Thr Gln
625 630 635 640
Phe Lys Trp Asn Gly Gln Leu Asp Thr Gly Ser Asn Val Pro Glu Gly
645 650 655
Tyr Tyr Lys Leu Val Val Arg Ala Leu Arg Ile Phe Gly Asn Pro Ser
660 665 670
Asn Asp Glu Asp Trp Asp Val Ser Glu Ser Pro Arg Phe Gln Ile Thr
675 680 685
Tyr Cys Gln Lys Gly Asn Ser Ser Ser Thr Ile Arg Arg Arg Val Glu
690 695 700
Arg Gly His Asn
705
<210> 2
<211> 2124
<212> DNA
<213>Green muscardine fungus IPPM202 (Metarhizium anisopliae IPPM202)
<400> 2
atggactgca acggtcacgg aaccaatgcc gccggcatca ttggcacacg accaaacgcg 60
atgggcttta ccggcgcggc ccctggcgcc cagctaggca tgtaccgcat aacctgcagc 120
ggtgagtttc ccaccgacgt catggtggac gcaatttacc gcgccctcgc cgacggcgtg 180
gatatcatct cgtcgtcggc cgggcttccg ggcgggtggc cggatagtct cttgtcgtcg 240
gccgcgacgc gggctgtcga gagcggcgtc gtcttcgtcc agggcgcagg caacgacggc 300
actctcggtc tcttttcgca cttggacccg gccgtcggca atggcgttat tagtgttgga 360
tcggtgaata gccgtgtcta tccccagctc atcaatgagg ccaagtacac catcggcaac 420
ggatccgaag tccccttcca ctttttcccg acattaccct cggataactt caccggcacc 480
ccgatggagg tctatgccct gcccgtgaat ggatctggtg caggcaacga tactcgtgcc 540
tgtgacccgc tcccttctga cacgccggac ttgagcaaca agctagtcct gctgaatttc 600
cgtagtggca gaggggactg tagcttgagg aataggacca aagcggtcca tgaaaagggg 660
gcagcgcgta ttcttgccta cgttgctgat gaagactggc ttcctgatat ctattacgtg 720
gataacttgc ccgagggggt tctcgccctc ggaatgctag ggtttgatac cgcgacggag 780
atgctcaagg cgctccaatc tggccgcaaa gtcctcgcca cagtcttccc ctacaatgat 840
gcaccccgag tttatattga ggagcccaat gacgagattg caggatctgt ttctgatttc 900
agttcctggg gcccttcgtg gaatctcggt ctcaagcctt ccctgactgc ggttggcgga 960
gaaatcatct cgacggattt tagagagacg aatccttctg gctacacgat tacacgagga 1020
acttccttct caggtcccct gattgctgcc ctcgttgcac tgattggcga ggctcgcggc 1080
tctctggatc cagctaccgt cgagagcctt ctcgtttcgc actcaaatcc gcagctctac 1140
cacgacggag agaaattctt gccctacctt gcccctgttg cccagcaggg cggcggtctg 1200
gcgcgtgcct atgacgctgc ctatgctaca actcttgtcc aaccggcagg cctcaacttc 1260
aacgacactg aacacatggc ggcctcgctc aactttacca tcaagaatgt gggccaaggt 1320
gctatcacgt accgtctttc tcacgttccc gccgtcaccg tgtatacctt tacggaaaat 1380
ggcaccgttt cctcgtatcc caataagctt gaggcagttg agactccagc cgcgattact 1440
ctcagtgaca caagtgtcac cgtagaccct gggaattccg tcaacatccg tgtatcagcg 1500
tcgattcctg agggccttga cgccagtcga atgcccctgt ggtctggctg gattgcgatc 1560
aacgggtctg acagcacttc actctctgtt ccttatcagg ggttttccgg ctcaatccgc 1620
aaacaccagg tcctgcgacc cgacggcgcc tcgctcacct atcgaaatgc ctctgtcact 1680
gagggcacca ctgttgtcct gccagcacca ggctccatca cgccatctca acttgtgttg 1740
aatatcaacg caacaatggg aatccctctc gtgcgtgctg aggtggtgcc cgcgaatggc 1800
acagccaatg ccaccgatat tactacatcg attggtcagg ttcaaggatt ccccgtgcag 1860
tggcgcccga ggaacttgca gcaggattcg aattcgccag acttgcttca attcacccag 1920
ttcaaatgga atggccagct cgacacaggt agcaatgtgc ccgagggcta ctacaaactc 1980
gtcgtgcggg ccctgaggat tttcggcaac cctagcaatg acgaggactg ggatgttagt 2040
gagtcgccgc gattccagat tacatactgc caaaaaggaa attcatctag cacgatccgt 2100
cgccgagtcg aaaggggaca caat 2124
Claims (10)
1. a kind of green muscardine fungus protease P r1C, which is characterized in that its amino acid sequence such as SEQ ID NO：Shown in 1.
2. green muscardine fungus protease P r1C genes, which is characterized in that encode green muscardine fungus protease P r1C described in claim 1.
3. green muscardine fungus protease P r1C genes according to claim 2, which is characterized in that the green muscardine fungus protease P r1C
The sequence of gene such as SEQ ID NO：Shown in 2.
4. including the recombinant expression carrier of the green muscardine fungus protease P r1C genes described in claim 2.
5. including the recombinant bacterial strain of the green muscardine fungus protease P r1C genes described in claim 2.
6. a kind of method preparing green muscardine fungus protease P r1C described in claim 1, which is characterized in that include the following steps：
(1) gene comprising green muscardine fungus protease P r1C described in coding claim 1 is inserted into expression vector, is recombinantly expressed
Carrier；
(2) recombinant expression carrier that step (1) obtains is used to convert host cell；
(3) host cell, induced expression green muscardine fungus protease P r1C are cultivated.
7. the purposes of green muscardine fungus protease P r1C described in claim 1.
8. purposes of the green muscardine fungus protease P r1C described in claim 1 in terms of preventing locust disease.
9. the purposes of green muscardine fungus protease P r1C according to claim 7, which is characterized in that the green muscardine fungus protease
Pr1C is used in combination with green muscardine fungus.
10. a kind of method of prevention locust, which is characterized in that the method includes green muscardine fungus described in claim 1 is administered in combination
Protease P r1C and the step of green muscardine fungus, with lethal locust.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110876387A (en) * | 2019-12-05 | 2020-03-13 | 中国农业科学院植物保护研究所 | Compound bait for preventing and controlling locust and application thereof |
| CN112970783A (en) * | 2021-03-02 | 2021-06-18 | 中国农业科学院植物保护研究所 | Composite bait agent of artemisia sieversiana crude extract and metarhizium anisopliae for preventing and treating locusts asiaticus and application of composite bait agent |
| CN117209574A (en) * | 2023-07-28 | 2023-12-12 | 中国科学院动物研究所 | High-toxicity destruxin for transformation of locust pests, and preparation method and application thereof |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1800378A (en) * | 2005-12-09 | 2006-07-12 | 重庆大学 | Thermostable tyrosine phosphatase , and its separation and purification method |
| US20070122876A1 (en) * | 2004-12-08 | 2007-05-31 | Chang Margaret D | Nucleic acids for enhancing gene expression and use thereof |
| CN104862326A (en) * | 2015-06-02 | 2015-08-26 | 中国农业科学院生物技术研究所 | Metarhizium anisopliae o-methyltransferase and application thereof |
-
2018
- 2018-06-12 CN CN201810599450.5A patent/CN108642029B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070122876A1 (en) * | 2004-12-08 | 2007-05-31 | Chang Margaret D | Nucleic acids for enhancing gene expression and use thereof |
| CN1800378A (en) * | 2005-12-09 | 2006-07-12 | 重庆大学 | Thermostable tyrosine phosphatase , and its separation and purification method |
| CN104862326A (en) * | 2015-06-02 | 2015-08-26 | 中国农业科学院生物技术研究所 | Metarhizium anisopliae o-methyltransferase and application thereof |
Non-Patent Citations (4)
| Title |
|---|
| HU,X等: "Metarhizium brunneum ARSEF 3297 subtilisin-like serine protease PR1C partial mRNA", 《GENEBANK ONLINE：XM_014684945.1》 * |
| ST LEGER R等: "Isoforms of the cuticle-degrading PR1 protease and production of a metalloprotease by Metarhizium anisopliae", 《ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS》 * |
| STAATS C. C.等: "subtilisin-like serine protease PR1C [Metarhizium anisopliae]", 《GENEBANK ONLINE：KFG78468.1》 * |
| 张伟: "绿僵菌和蝗虫中具有降解昆虫体壁功能蛋白酶基因的分离、克隆及功能研究", 《中国博士学位论文全文数据库 农业科技辑》 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110876387A (en) * | 2019-12-05 | 2020-03-13 | 中国农业科学院植物保护研究所 | Compound bait for preventing and controlling locust and application thereof |
| CN112970783A (en) * | 2021-03-02 | 2021-06-18 | 中国农业科学院植物保护研究所 | Composite bait agent of artemisia sieversiana crude extract and metarhizium anisopliae for preventing and treating locusts asiaticus and application of composite bait agent |
| CN117209574A (en) * | 2023-07-28 | 2023-12-12 | 中国科学院动物研究所 | High-toxicity destruxin for transformation of locust pests, and preparation method and application thereof |
| CN117209574B (en) * | 2023-07-28 | 2024-03-29 | 中国科学院动物研究所 | High-toxicity destruxin for transformation of locust pests, and preparation method and application thereof |
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