CN111440814A - Insect-resistant fusion gene mCry1AbVip3A, expression vector and application thereof - Google Patents
Insect-resistant fusion gene mCry1AbVip3A, expression vector and application thereof Download PDFInfo
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
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- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
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- C12N2800/80—Vectors containing sites for inducing double-stranded breaks, e.g. meganuclease restriction sites
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Abstract
The invention discloses an insect-resistant fusion gene mCry1AbVip3A, wherein the nucleotide sequence of the gene mCry1AbVip3A is shown as (a), (b) or (c): (a) SEQ ID NO: 1; or (b), encodes SEQ ID NO: 2; or (c), and SEQ ID NO: 1 under stringent hybridization conditions, and the protein encoded by the nucleotide has the function of the transcription factor of mCry1AbVip 3A. In vitro toxicity test proves that the modified and synthesized fusion gene toxigenin has obvious insecticidal effect on corn borer and spodoptera littoralis, can be stably and efficiently expressed in monocotyledons, and is further used for producing insect-resistant transgenic plants.
Description
Technical Field
The invention relates to the field of genetic engineering and biological control, in particular to an insect-resistant fusion gene, an expression vector and application thereof
Background
Pests cause losses of about 80 billion dollars per year to global agricultural production. The prevention and control of pests mainly depend on the use of chemical pesticides at present, but pesticide residues bring harm to human health. Therefore, transgenic crops capable of producing insecticidal toxins are successfully selected for insect resistance, and the transgenic insect-resistant corn and cotton are planted in large quantities at present.
Substances having strong insecticidal activity against pests such as cutworm (Agrotis ipsilon), Spodoptera exigua (Spodoptera exigua), Spodoptera frugiperda (Spodoptera rugerida) and the like are found in the fermentation supernatant of strain Bt AB88, and are named vegetative insecticidal proteins (Vip) (escherichia, 1996) in view of their expression from the middle to the spore phase of logarithmic growth. Bt genes from Bacillus thuringiensis (Bacillus thuringiensis) can also encode insecticidal protein crystals, which produce-insecticidal parasporal crystal proteins of endotoxins during spore formation, which have high insecticidal activity. The principle of action is that this insect-resistant protein is solubilized by alkaline intestinal fluid and hydrolyzed to smaller active toxin fragments, the core fragments (Hofte and Whiteley, 1989). The active fragment is resistant to further hydrolysis by proteases, and the activated protein binds to brush vesicles on the insect gut, causing perforation to affect osmotic balance, cell swelling and lysis, and target organisms stop feeding and eventually die. Studies have shown that intestinal epithelial cells of many target pests have high affinity binding sites for Bt proteins (Hofte and Whiteley, 1989). Compared with Cry proteins, the research on the insecticidal mechanism of Vip3 proteins just starts, and the initial mechanism research finds that the epithelial columnar cells expand into spherical shapes after the sensitive insect cutworm is fed with Vip3A toxin for 24 hours, the morphology of goblet cells is slightly changed, and the cell damage at the stage is not obvious; after 48h, the columnar cells continuously deteriorate, the intestinal cavity is filled with fragments of collapsed cells, the goblet cells are obviously damaged, but the goblet cells are still connected with the basement membrane; after 72h the epithelium was completely detached and the insect died, but no significant cell damage occurred in the foregut and hindgut. Ingestion of Vip3A by sensitive insects causes symptoms similar to endotoxin, but delayed in time. Meanwhile, in vivo immunolocalization experiments showed that Vip3A bound specifically to the apical microvilli and was mostly concentrated in the columnar cells, with no detectable signal in the goblet cells. The columnar cells in the midgut tissue mainly play the roles of secreting digestive enzymes and absorbing digestive products, and Vip3A is activated by protease in intestinal fluid, and is absorbed by the columnar cells, perhaps the combination of the columnar cells with certain receptor proteins on cell membranes leads to cell membrane perforation or initiates a certain signal path, and finally the insect body dies (Yu C G and Mullins M A et al, 1997).
In recent years, many studies on vegetative insecticidal proteins Vip have been carried out, and Vip-like proteins have been found to be mainly classified into 4 classes, namely Vip1, Vip2, Vip3 and Vip 4. Vip1/Vip2, which constitute binary toxins and mainly act on coleopteran and hemipteran insects, and relatively few studies have been carried out (Ellis R T and Stamp L, 2002). the university of agriculture in huazhong finds 1 Vip 4-like gene, and there are no reports on insecticidal action mode, target specificity and the like.
Saraswalk et al constructed a chimeric protein of Vip3Aa14 and Cry1Ac, which mainly existed in the form of inclusion body and has better stability to trypsin, but only maintained the insecticidal activity of Cry1Ac and showed no synergistic effect. Furthermore, the C-terminus of Cry1C significantly enhanced the synthesis of Vip3Aa7 and helped it form inclusion bodies in BMB171, but the biological activity was significantly reduced compared to protoxin Vip3Aa7 (Song R et al, 2008). The reduced virulence of the above fusion proteins may be due to the failure of the fusion protein to fold correctly. However, the fusion protein constructed by Dong et al fuses Vip3Aa7 and the N end of Cry9Ca to achieve 4.79 of the synergistic effect factor of diamondback moth, which is much higher than the synergistic effect of mixing 2 prototoxins. Yu et al co-express Vip3Aa29 and Cyt2Aa3, and the co-expressed protein has synergistic effect on spodoptera exigua and rice stem borer. The Vip3 and insecticidal toxins from different sources are fused or co-expressed, so that the toxicity of the Vip3 to target insects can be effectively enhanced, the insecticidal spectrum is expanded, and the generation of insect resistance is delayed. In addition, Vip3 can be integrated into the chromosome of insect virus, so that Vip3A can be effectively transmitted, and the insecticidal toxicity of the virus can be improved.
Compared with the independent Cry1Ab or VIP3A gene, the insect-resistant fusion gene can resist corn borer and spodoptera frugiperda.
Disclosure of Invention
The invention aims to provide an insect-resistant fusion gene capable of being stably and efficiently expressed in plants and an expression vector thereof.
The invention also aims to provide application of the insect-resistant fusion gene in improving insect resistance of transgenic plants.
The object of the invention can be further achieved by the following technical measures:
under the condition of keeping the amino acid composition of the Vip3A translation protein of the sequence unchanged, carrying out base substitution by using codons preferred by monocotyledons to obtain a modified DNA sequence preliminarily; eliminating AT-rich sequences and common restriction enzyme cutting sites (SacI) which are present in DNA sequences and cause unstable plant transcription, and then correcting and eliminating the AT-rich sequences by a method of replacing codons; then removing a terminator from the Cry1Ab-Ma sequence and placing the sequence at the N end of the synthesized Vip 3A; determining and chemically synthesizing the modified fusion gene mCry1AbVip3A, wherein the nucleotide sequence of the fusion gene mCry1AbVip3A is shown as SEQ ID No. 1; restriction enzyme recognition site sequences are added at two ends of the sequence according to cloning requirements and are constructed on corresponding expression vectors.
The fusion gene is operably connected with a prokaryotic expression vector, so that the toxicity of Bt gene expression products synthesized by the invention on corn borers and spodoptera littoralis can be rapidly and preliminarily detected. The fusion gene is operably connected with a plant expression vector, the expression vector is introduced into corresponding agrobacterium, and genetic transformation is carried out through an agrobacterium-mediated method to cultivate insect-resistant transgenic corn. Also can be used for genetic transformation of other crops or fruit trees and the like to ensure that the crops or fruit trees have insect-resistant activity.
The gene of the invention can be transformed into bacteria or fungi by the technicians in the field, the fusion insect-resistant protein is produced by large-scale fermentation, and the fusion insect-resistant protein is prepared into pesticides for controlling crop pests.
In order to achieve the purpose of the invention, the invention firstly provides an insect-resistant fusion gene mCry1AbVip3A, wherein the nucleotide sequence of the gene mCry1AbVip3A is shown as (a), (b) or (c):
(a) SEQ ID NO: 1; or
(b) Encoding SEQ ID NO: 2; or
(c) And SEQ ID NO: 1 under stringent hybridization conditions, and the protein encoded by the nucleotide has the function of the transcription factor of mCry1AbVip 3A.
Furthermore, the invention also provides an amino acid sequence coded by the insect-resistant fusion gene mCry1AbVip3A as shown in SEQ ID NO: 2, respectively.
Further, the invention also provides a vector containing the insect-resistant fusion gene, preferably a bivalent vector.
Further, the present invention also provides a host cell, preferably EHA105, containing the above vector.
Further, the invention also provides a transformed plant cell containing the insect-resistant fusion gene.
Furthermore, the invention also provides application of the insect-resistant fusion gene in improving insect resistance of transgenic plants. Preferably, the plant is a crop, a fruit tree or a vegetable, such as corn, rice, potato, cotton, and the like.
The invention has at least the following advantages and beneficial effects:
compared with independent Cry1Ab-Ma and Vip3A, the insect-resistant fusion protein provided by the invention has an insecticidal effect, and can be compatible with the corn borer resistance of Cry1Ab-Ma and the Spodoptera frugiperda resistance of Vip 3A.
After the insect-resistant fusion gene is introduced into corn, a transformant with stable inheritance can be obtained. In addition, the gene can also transform crops such as cotton, rice, vegetables and the like, so that the crops have corresponding insect-resistant activity, the use amount of pesticides is reduced, the environmental pollution is reduced, and the gene has important economic value and wide application prospect.
Drawings
FIG. 1 shows a plant expression vector containing a fragment of the mCry1AbVip3A gene.
FIG. 2 shows the detection result of the transgenic maize mCry1AbVip3A colloidal gold test strip, wherein the upper part of the test strip color development band is a quality control line, and the lower part of the test strip color development band is a target protein detection line; left 1 is a negative control, others are transgenic maize samples.
Detailed Description
The following examples are intended to illustrate the invention but are not intended to limit the scope of the invention. Unless otherwise specified, the technical means used in the examples are conventional means well known to those skilled in the art.
Example 1 Synthesis of an insect-resistant fusion Gene
According to the original nucleotide sequence (gene ID DQ539888.1) of Vip3A gene, under the condition of keeping the amino acid composition of the protein of the gene unchanged, base substitution is carried out by using codons preferred by monocotyledons, and a modified DNA sequence is obtained preliminarily; eliminating AT-rich sequences (such as ATTTA, AATGAA, etc.) which cause plant transcription instability and common restriction enzyme cutting sites (SacI) existing in the DNA sequence, and then correcting and eliminating by a method of replacing codons; and adding a Cry1Ab-Ma sequence at the 5' end; determining and chemically synthesizing a modified insect-resistant fusion gene mCry1AbVip3A, wherein the nucleotide sequence of the insect-resistant fusion gene mCry1AbVip3A is shown as SEQ ID No. 1; restriction enzyme recognition site sequences are added at two ends of the sequence according to cloning requirements and are constructed on corresponding expression vectors.
Example 2 expression of insect-resistant fusion genes in prokaryotic systems and toxicity testing of the products
In order to detect the in vitro expression of the modified insect-resistant gene and the toxicity to corn borer, a prokaryotic expression vector pET-mCry1AbVip3A is constructed.
Primer sequences are designed (upstream primer F1: shown as SEQ ID No.3, 5'-GACGACGACAAGGCCATGGATGGACAACAACCCG-3'; F2: shown as SEQ ID No.4, 5'-ACGACGACAAGGCCATGGATGAACAAGAACAAC-3'; downstream primer R1: 5'-GGTGGTGGTGGTGCTCGAGCTTGATGCTCACGTC-3', shown as SEQ ID No. 5; R2: shown as SEQ ID No.6, 5'-GGTGGTGGTGGTGCTCGAGGTACTCCGCCTCGAA-3').
The constructed pTF101.1-mCry1AbVip3A plant expression plasmid (figure 1) is used as a template, F1 and R1 are used as primers, an insect-resistant fusion gene is amplified, and a gel recovery kit (Tiangen Biochemical technology (Beijing) Co., Ltd., DP209) is used for recovering and purifying the insect-resistant gene fragment. pET30a + was digested with restriction enzymes NcoI and XhoI, and the 4.2kb fragment was recovered and purified by gel recovery kit. The recovered fragment and the digested pET30a + fragment are subjected to ligation reaction, and the constructed prokaryotic expression plasmid is named pET-mCry1AbVip 3A. And (3) carrying out enzyme digestion identification by using different restriction enzymes, which shows that the vector construction is correct.
The constructed prokaryotic vector pET-mCry1AbVip3A is converted into B L21 (DE3) competent cells, the infected Escherichia coli B L21 bacterial liquid is induced by IPTG, Bt protein is extracted, and the corn borer and spodoptera frugiperda are used for insect test.
① Escherichia coli B L21 single colony was inoculated in 5ml of L B (containing kanamycin) liquid medium and cultured overnight at 37 ℃.
② the bacterial liquid was inoculated into 500ml of L B (containing kanamycin) liquid medium and cultured until OD ≈ 0.5.
③ IPTG was added to a final concentration of 0.5mM and shaking induction was continued for 4 hours.
④ 4000 centrifuging at 4000rpm for 10min, and collecting thallus.
⑤ 36ml lysis buffer (2mM Tris-HCl; 0.2mM CaCl) was added2(ii) a pH 8.0), the cells were resuspended, lysozyme was added to a final concentration of 1mg/ml and placed on ice for 30 min.
⑥ ultrasonic crushing thallus (crushing parameter: working for 10s, interval 5s, 40 times, ice bath crushing), centrifuging at 4000rpm for 10min, and collecting supernatant.
⑦ the collected supernatant is added to feed for feeding corn borer and spodoptera littoralis.
The toxicity of the corn borer is measured, 5g of Asiatic corn borer artificial feed is weighed and placed in a culture dish, the feed is cut into 1-2mm slices, 1ml of protein liquid (50ng/ul) is evenly coated on the surface of the feed, 10 corn borer larvae incubated for 24 hours are inoculated in each culture dish after 2 h.2h of soaking, the test is controlled by distilled water with the same volume, 5 times of treatment is set for each treatment, the feed is placed in an artificial climate incubator with the temperature of 28 ℃, the light cycle of 16h:8h (L: D) and the relative humidity of 80 percent for culture, and the number of the survival larvae is investigated and recorded every other day.
The toxicity of spodoptera frugiperda is measured by weighing 5g of artificial feed, placing the feed in a spodoptera frugiperda box, cutting the feed into 1-2mm slices, uniformly coating 1ml of protein liquid (50ng/ul) on the surface of the feed, soaking the feed for 2 h.2h, then inoculating 1 spodoptera frugiperda larva hatched for 24h into each spodoptera frugiperda box, using the same volume of distilled water as a control in the test, setting 30 times of repetition in each treatment, placing the box in an artificial climate incubator with the temperature of 26 ℃, the light period of 16h:8h (L: D) and the relative humidity of 60% for culture, and investigating and recording the number of the survival larva every day.
And (3) data analysis: performing preliminary arrangement on the data by using excel 2007, and calculating the survival rates of larvae of ostrinia nubilalis and spodoptera exigua at different feeding times; analysis of variance and significance of differences were performed on the data from the corn borer survey using the sps 23. The result shows that no larvae of corn borer and spodoptera littoralis fed with the protein mCry1AbVip3A survive on day 6 (Table 1 and Table 2), and the test result shows that the mCry1AbVip3A has strong insecticidal activity.
Table 1: toxicity to corn borer larvae
Table 2: toxicity to Spodoptera frugiperda larvae
Example 3 expression of the mCry1AbVip3A Gene in transgenic maize
An agrobacterium-mediated transformation method (strain EHA105) is adopted to introduce an insertion sequence of pTF101.1-mCry1AbVip3A (shown in figure 1) into a callus of a receptor corn, and the transgenic corn is obtained after screening by herbicide bialaphos. Detection of target protein mCry1AbVip3A (Bt-Cry1Ab/1Ac colloidal gold immunological detection):
① is about 1cm in length2Left and right fresh young leaves were placed in a 1.5ml Eppendorf tube, to which 500ul of SEB4 sample extraction buffer was added and ground.
② the test strip (Beijing Zhennis Biotechnology Co., Ltd., Cat. No.: STX06200/0050) was removed and the top of the test strip was held in the hand and the end of the label was inserted into the centrifuge tube and a quality control line appeared within 3-5 minutes, and if the sample was positive, a test line appeared.
The expression of mCry1AbVip3A in 6 transgenic plant leaves was determined by a colloidal gold test strip assay. The results showed that mCry1 abbip 3A protein was expressed in transgenic maize leaf tissue (fig. 2).
Although the invention has been described in detail hereinabove with respect to a general description and specific embodiments thereof, it will be apparent to those skilled in the art that modifications or improvements may be made thereto based on the invention. Accordingly, such modifications and improvements are intended to be within the scope of the invention as claimed.
Sequence listing
<110> Jilin province academy of agricultural sciences of the institute of crop science of the academy of agricultural sciences of China
<120> insect-resistant fusion gene mCry1AbVip3A, and expression vector and application thereof
<130>P200143
<141>2020-04-15
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gaggggctct ccaacttgta ccagatctac gcggaatcct tccgggaatg ggaggcggac 360
ccgacgaatc cggcgttgag ggaagagatg aggatccagt tcaacgacat gaactccgcg 420
ctcacgacgg cgatcccgct cttcgcggtc cagaactatc aggtcccgct actctcggtc 480
tatgtccagg cggcgaacct ccatttgtcg gtcctccggg acgtgtcggt cttcggtcag 540
cgctgggggt tcgacgcggc gacgatcaac tcgcggtaca atgacctcac gcgcctcatc 600
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ccggactcca gggactggat ccgctacaac caattccgtc gggagcttac gttgacggtc 720
ctcgatatcg tcagcttgtt ccctaactac gattcgagga cgtatccgat ccggacggtc 780
tcgcagctca cgagggagat ttacacgaac ccggtcctcg agaacttcga tgggtccttc 840
cgggggtccg cgcaggggat cgaggggtcg atccgctccc cgcacctcat ggatatcctc 900
aactcgatca cgatctacac ggacgcgcac cggggggagt actattggtc cgggcaccag 960
atcatggcgt cgccggtggg cttctcgggc ccggagttca cgttcccgct gtacgggacg 1020
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acgctcagca gcacgctcta ccgccgcccg ttcaacatcg ggatcaacaa ccaacagctc 1140
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taccggaagt cagggacggt cgactcgctc gatgagatcc cgccgcagaa caataacgtc 1260
ccgccgcggc aggggttctc gcaccggctc tcgcacgtct cgatgttccg gtcggggttc 1320
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ggcttcgagt tctacctgaa caccttccac gacgtgatgg tgggcaacaa cctgttcggc 2580
cgcagcgccc tgaagaccgc cagcgagctg atcaccaagg agaacgtgaa gaccagcggc 2640
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ttcctgaccc tgaccacctg ccgcaagctg ctgggcctgg ccgacatcga ctacaccagc 2760
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agcaccggcg agatcgacct gaacaagaag aaggtggaga gcagcgaggc cgagtaccgc 3240
accctgagcg cgaacgacga cggcgtctac atgccactgggcgtgatcag cgagaccttc 3300
ctgaccccga tcaacggctt cggcctgcag gccgacgaga acagccgcct gatcaccctg 3360
acctgtaaga gctacctgcg cgagctgctg ctagccaccg acctgagcaa caaggagacc 3420
aagctgatcg tgccaccgag cggcttcatc agcaacatcg tggagaacgg cagcatcgag 3480
gaggacaacc tggagccgtg gaaggccaac aacaagaacg cctacgtcga ccacaccggc 3540
ggcgtgaacg gcaccaaggc cctgtacgtg cacaaggacg gcggcatcag ccagttcatc 3600
ggcgacaagc tgaagccgaa gaccgagtac gtgatccagt acaccgtgaa gggcaagcca 3660
tcgatccacc tgaaggacga gaacaccggc tacatccact acgaggacac caacaacaac 3720
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tacctgatcc tgaagagcca gaacggcgac gaggcctggg gcgacaactt catcatcctg 3840
gagatcagcc cgagcgagaa gctgctgagc ccggagctga tcaacaccaa caactggacc 3900
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Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln Phe Leu Leu Ser
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Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu Val Asp Ile Ile
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100 105 110
Ser Phe Arg Glu Trp Glu Ala Asp Pro Thr Asn Pro Ala Leu Arg Glu
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Glu Met Arg Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala
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Ile Arg Thr Val Ser Gln Leu Thr Arg Glu Ile Tyr Thr Asn Pro Val
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Leu Glu Asn Phe Asp Gly Ser Phe Arg Gly Ser Ala Gln Gly Ile Glu
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Gly Ser Ile Arg Ser Pro His Leu Met Asp Ile Leu Asn Ser Ile Thr
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Ile Tyr Thr Asp Ala His Arg Gly Glu Tyr Tyr Trp Ser Gly His Gln
305 310315 320
Ile Met Ala Ser Pro Val Gly Phe Ser Gly Pro Glu Phe Thr Phe Pro
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Leu Tyr Gly Thr Met Gly Asn Ala Ala Pro Gln Gln Arg Ile Val Ala
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Arg Pro Phe Asn Ile Gly Ile Asn Asn Gln Gln Leu Ser Val Leu Asp
370 375 380
Gly Thr Glu Phe Ala Tyr Gly Thr Ser Ser Asn Leu Pro Ser Ala Val
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Tyr Arg Lys Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln
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Asn Asn Asn Val Pro Pro Arg Gln Gly Phe Ser His Arg Leu Ser His
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Val Ser Met Phe Arg Ser Gly Phe Ser Asn Ser Ser Val Ser Ile Ile
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Ile Ile Pro Ser Ser Gln Ile Thr Gln Ile Pro Leu Thr Lys Ser Thr
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Asn Leu Gly Ser Gly Thr Ser Val Val Lys Gly Pro Gly Phe Thr Gly
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Val Asn Ile Thr Ala Pro Leu Ser Gln Arg Tyr Arg Val Arg Ile Arg
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Tyr Ala Ser Thr Thr Asn Leu Gln Phe His Thr Ser Ile Asp Gly Arg
530 535 540
Pro Ile Asn Gln Gly Asn Phe Ser Ala Thr Met Ser Ser Gly Ser Asn
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Leu Gln Ser Gly Ser Phe Arg Thr Val Gly Phe Thr Thr Pro Phe Asn
565 570 575
Phe Ser Asn Gly Ser Ser Val Phe Thr Leu Ser Ala His Val Phe Asn
580 585 590
Ser Gly Asn Glu Val Tyr Ile Asp Arg Ile Glu Phe Val Pro Ala Glu
595 600 605
Val Thr Phe Glu Ala Glu Tyr Met Asn Lys Asn Asn Thr Lys Leu Ser
610 615 620
Thr Arg Ala Leu Pro Ser Phe Ile Asp Tyr Phe Asn Gly Ile Tyr Gly
625 630635 640
Phe Ala Thr Gly Ile Lys Asp Ile Met Asn Met Ile Phe Lys Thr Asp
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Thr Gly Gly Asp Leu Thr Leu Asp Glu Ile Leu Lys Asn Gln Gln Leu
660 665 670
Leu Asn Asp Ile Ser Gly Lys Leu Asp Gly Val Asn Gly Ser Leu Asn
675 680 685
Asp Leu Ile Ala Gln Gly Asn Leu Asn Thr Glu Leu Ser Lys Glu Ile
690 695 700
Leu Lys Ile Ala Asn Glu Gln Asn Gln Val Leu Asn Asp Val Asn Asn
705 710 715 720
Lys Leu Asp Ala Ile Asn Thr Met Leu Arg Val Tyr Leu Pro Lys Ile
725 730 735
Thr Ser Met Leu Ser Asp Val Ile Lys Gln Asn Tyr Ala Leu Ser Leu
740 745 750
Gln Ile Glu Tyr Leu Ser Lys Gln Leu Gln Glu Ile Ser Asp Lys Leu
755 760 765
Asp Ile Ile Asn Val Asn Val Leu Ile Asn Ser Thr Leu Thr Glu Ile
770 775 780
Thr Pro Ala Tyr Gln Arg Ile Lys Tyr Val Asn Glu Lys Phe Glu Glu
785 790 795800
Leu Thr Phe Ala Thr Glu Thr Ser Ser Lys Val Lys Lys Asp Gly Ser
805 810 815
Pro Ala Asp Ile Leu Asp Glu Leu Thr Glu Leu Thr Glu Leu Ala Lys
820 825 830
Ser Val Thr Lys Asn Asp Val Asp Gly Phe Glu Phe Tyr Leu Asn Thr
835 840 845
Phe His Asp Val Met Val Gly Asn Asn Leu Phe Gly Arg Ser Ala Leu
850 855 860
Lys Thr Ala Ser Glu Leu Ile Thr Lys Glu Asn Val Lys Thr Ser Gly
865 870 875 880
Ser Glu Val Gly Asn Val Tyr Asn Phe Leu Ile Val Leu Thr Ala Leu
885 890 895
Gln Ala Gln Ala Phe Leu Thr Leu Thr Thr Cys Arg Lys Leu Leu Gly
900 905 910
Leu Ala Asp Ile Asp Tyr Thr Ser Ile Met Asn Glu His Leu Asn Lys
915 920 925
Glu Lys Glu Glu Phe Arg Val Asn Ile Leu Pro Thr Leu Ser Asn Thr
930 935 940
Phe Ser Asn Pro Asn Tyr Ala Lys Val Lys Gly Ser Asp Glu Asp Ala
945 950 955960
Lys Met Ile Val Glu Ala Lys Pro Gly His Ala Leu Ile Gly Phe Glu
965 970 975
Ile Ser Asn Asp Ser Ile Thr Val Leu Lys Val Tyr Glu Ala Lys Leu
980 985 990
Lys Gln Asn Tyr Gln Val Asp Lys Asp Ser Leu Ser Glu Val Ile Tyr
995 1000 1005
Gly Asp Met Asp Lys Leu Leu Cys Pro Asp Gln Ser Glu Gln Ile Tyr
1010 1015 1020
Tyr Thr Asn Asn Ile Val Phe Pro Asn Glu Tyr Val Ile Thr Lys Ile
1025 1030 1035 1040
Asp Phe Thr Lys Lys Met Lys Thr Leu Arg Tyr Glu Val Thr Ala Asn
1045 1050 1055
Phe Tyr Asp Ser Ser Thr Gly Glu Ile Asp Leu Asn Lys Lys Lys Val
1060 1065 1070
Glu Ser Ser Glu Ala Glu Tyr Arg Thr Leu Ser Ala Asn Asp Asp Gly
1075 1080 1085
Val Tyr Met Pro Leu Gly Val Ile Ser Glu Thr Phe Leu Thr Pro Ile
1090 1095 1100
Asn Gly Phe Gly Leu Gln Ala Asp Glu Asn Ser Arg Leu Ile Thr Leu
1105 1110 11151120
Thr Cys Lys Ser Tyr Leu Arg Glu Leu Leu Leu Ala Thr Asp Leu Ser
1125 1130 1135
Asn Lys Glu Thr Lys Leu Ile Val Pro Pro Ser Gly Phe Ile Ser Asn
1140 1145 1150
Ile Val Glu Asn Gly Ser Ile Glu Glu Asp Asn Leu Glu Pro Trp Lys
1155 1160 1165
Ala Asn Asn Lys Asn Ala Tyr Val Asp His Thr Gly Gly Val Asn Gly
1170 1175 1180
Thr Lys Ala Leu Tyr Val His Lys Asp Gly Gly Ile Ser Gln Phe Ile
1185 1190 1195 1200
Gly Asp Lys Leu Lys Pro Lys Thr Glu Tyr Val Ile Gln Tyr Thr Val
1205 1210 1215
Lys Gly Lys Pro Ser Ile His Leu Lys Asp Glu Asn Thr Gly Tyr Ile
1220 1225 1230
His Tyr Glu Asp Thr Asn Asn Asn Leu Glu Asp Tyr Gln Thr Ile Asn
1235 1240 1245
Lys Arg Phe Thr Thr Gly Thr Asp Leu Lys Gly Val Tyr Leu Ile Leu
1250 1255 1260
Lys Ser Gln Asn Gly Asp Glu Ala Trp Gly Asp Asn Phe Ile Ile Leu
1265 1270 12751280
Glu Ile Ser Pro Ser Glu Lys Leu Leu Ser Pro Glu Leu Ile Asn Thr
1285 1290 1295
Asn Asn Trp Thr Ser Thr Gly Ser Thr Asn Ile Ser Gly Asn Thr Leu
1300 1305 1310
Thr Leu Tyr Gln Gly Gly Arg Gly Ile Leu Lys Gln Asn Leu Gln Leu
1315 1320 1325
Asp Ser Phe Ser Thr Tyr Arg Val Tyr Phe Ser Val Ser Gly Asp Ala
1330 1335 1340
Asn Val Arg Ile Arg Asn Ser Arg Glu Val Leu Phe Glu Lys Arg Tyr
1345 1350 1355 1360
Met Ser Gly Ala Lys Asp Val Ser Glu Met Phe Thr Thr Lys Phe Glu
1365 1370 1375
Lys Asp Asn Phe Tyr Ile Glu Leu Ser Gln Gly Asn Asn Leu Tyr Gly
1380 1385 1390
Gly Pro Ile Val His Phe Tyr Asp Val Ser Ile Lys
1395 1400
<210>3
<211>34
<212>DNA
<213> Artificial sequence (Artificial sequence)
<400>3
gacgacgaca aggccatgga tggacaacaa cccg 34
<210>4
<211>33
<212>DNA
<213> Artificial sequence (Artificial sequence)
<400>4
acgacgacaa ggccatggat gaacaagaac aac 33
<210>5
<211>34
<212>DNA
<213> Artificial sequence (Artificial sequence)
<400>5
ggtggtggtg gtgctcgagc ttgatgctca cgtc 34
<210>6
<211>34
<212>DNA
<213> Artificial sequence (Artificial sequence)
<400>6
ggtggtggtg gtgctcgagg tactccgcct cgaa 34
Claims (10)
1. An insect-resistant fusion gene mCry1AbVip3A, wherein the nucleotide sequence of the gene mCry1AbVip3A is shown as (a), (b) or (c):
(a) SEQ ID NO: 1; or
(b) Encoding SEQ ID NO: 2; or
(c) And SEQ ID NO: 1 under stringent hybridization conditions, and the protein encoded by the nucleotide has the function of the transcription factor of mCry1AbVip 3A.
2. The insect-resistant fusion gene mCry1AbVip3A of claim 1, wherein the insect-resistant fusion gene mCry1AbVip3A encodes an amino acid sequence as set forth in SEQ ID NO: 2, respectively.
3. A vector comprising the gene of claim 1.
4. The vector of claim 3, which is a bivalent vector.
5. A host cell comprising the vector of claim 4.
6. The host cell of claim 5, which is EHA 105.
7. A transformed plant cell comprising the gene of claim 1.
8. Use of the gene of claim 1 to increase insect resistance in transgenic plants.
9. The use of claim 8, wherein the plant is a crop, a fruit tree or a vegetable.
10. The use of claim 9, wherein the plant is corn, rice, potato, cotton.
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Cited By (1)
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