CN111995690A - Artificially synthesized insect-resistant protein mCry1Ia2, and preparation method and application thereof - Google Patents
Artificially synthesized insect-resistant protein mCry1Ia2, and preparation method and application thereof Download PDFInfo
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- CN111995690A CN111995690A CN202010915439.2A CN202010915439A CN111995690A CN 111995690 A CN111995690 A CN 111995690A CN 202010915439 A CN202010915439 A CN 202010915439A CN 111995690 A CN111995690 A CN 111995690A
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Abstract
The invention discloses an artificially synthesized insect-resistant protein mCry1Ia 2. The invention also discloses a nucleic acid molecule of the protein, and a recombinant vector, a host cell or a recombinant bacterium of the nucleic acid molecule. Also discloses applications of the protein, the nucleic acid molecule, a recombinant vector, a host cell or a recombinant bacterium of the protein in regulating and controlling plant insect resistance, killing insects or improving transgenic plant insect resistance and preparing insecticides or insect-resistant preparations. In vitro experiments prove that the modified and synthesized Bt gene toxigenic protein has higher insecticidal activity to corn borers and has obvious insecticidal effect to corn borer populations with resistance to Cry1Ab, Cry1F and Cry1Ie toxigenic proteins. The invention constructs a novel plant expression vector by using a constitutive promoter, and the insect-resistant gene mCry1Ia2 can be stably and efficiently expressed in monocotyledons, so that the insect-resistant gene mCry1Ia2 can be 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 artificially synthesized insect-resistant protein mCry1Ia2, and a preparation method and application thereof.
Background
The Bt gene codes insecticidal crystal protein, comes from Bacillus thuringiensis (Bacillus thuringiensis), is widely present in water, soil, desert, leaves and insect corpses, and is the biological insecticide with the largest yield and the most widely used nowadays. It can form Insecticidal Crystal Protein (ICP) when forming spores, also called endotoxin, and can produce specific insecticidal activity to agricultural pests of Lepidoptera and Coleoptera. The action process comprises the steps of swallowing protoxin by an insect body, performing enzymolysis and activation on the protoxin, enabling the toxin to pass through a peritrophic membrane, combining the toxin with a specific receptor, embedding toxin molecules into an epidermal cell membrane, forming an ion channel, and performing cell lysis after the ion imbalance of midgut cells. Over the past several decades, several tens of Bacillus thuringiensis strains and 130 or more of their encoded insecticidal crystal proteins have been identified.
The nucleotide sequence of the cry gene cloned from Bacillus thuringiensis was published by Whiteley and Schnepf in 1985. With the continuous discovery of new Bt strains and the cloning of Bt genes, members of the Bt family are increasing, and 975 insecticidal protein genes, including 789 Cry genes, 38 Cyt genes, and 142 Vip genes, have been identified and named in isolated Bt strains at present according to the latest updated data statistics of databases (www.lifesci.sussex.ac.uk). The cultivation of insect-resistant transgenic crops by introducing Bt genes into plants is the main application direction of Bt genes. According to data statistics of the international agricultural biotechnology application service organization (ISAAA) website, 345 transformation events by safety evaluation of Bt genes exist, wherein 255 maize transformant events pass approval.
The well-established trans Bt transgenic maize was obtained in 1990 by monsanto and dicaka. In 1993, Koziel et al developed cry1Ab transgenic maize, and Michael et al obtained by modifying cry1Ab gene showed higher resistance to corn borer. In 1996, transgenic insect-resistant maize began to be commercially grown in the united states. In 1997, 4 varieties of transgenic Bt maize were officially approved for sale in the United states, including mon810 by Monsanto, Bt176 and Bt11 by Syngenta, and DBT418 by Dicard, all of which are corn borers, and the insect-resistant transgenic maize was grown in a range of up to 320 kilohm2. Since cutworms, corn rootworms and other soil insects also affect corn yield, montelukast corporation has promoted the control of the soil insect "mon 863" (cry3Bb), and has obtained an insect-resistant corn "mon 863 × mon 810" which has control effects on both corn borers and soil insects. In 2007 and 2008, mr 604(cry3A) and mir162(Vip3Aa) for controlling lepidopteran pests and subterranean pests were introduced by the first zhengda company. Insect-resistant corns with a double gene of bt11 × GA21 × mir162 "and a triple gene of bt11 × mir162 × mir604 × GA 21" were introduced in 2011 and 2012 respectively.
The research of insect-resistant transgenic corn in China starts later, but great progress is made in recent years, and a plurality of transformants with stable heredity and good insect-resistant characters and transgenic hybrid combinations are obtained. Queen et al (1995) used a particle gun method to transfer pB48.415 plasmid into maize callus and obtained transgenic plants, which were identified to have a certain insect resistance. Zhang Li Nu et al (2003) modified Bt, SCK,The SCK and Bt bivalent insect-resistant gene is transferred into a maize inbred line R18 by a gene gun method to obtain a large number of transgenic plants. Zhang Yan Zhen et al (2004) adopt agrobacterium-mediated method to introduce Bt gene into corn inbred line 4112 and Dan 340, and molecular detection method proves that exogenous gene has been stably integrated on corn genome, and average transformation rate reaches 2.35%. Selfing line S of maize of plum fruit goodness et al (2005)1Transferring Bt and GNA genes into the strain to obtain a strain capable of simultaneously amplifying two target genes, and performing indoor insect resistance identification to discover the strain with stronger resistance. Xishu tree chapter and the like (2015) obtain the GmCry1F gene by a codon optimization method, and the gene is transferred into a corn material, so that a new material is provided for breeding insect-resistant varieties. Wangyang et al (2016) exchanged Cry1Ab domain and Cry1Ial domain, followed by codon optimization and transformation into maize, obtained genetically stable new germplasm for resisting corn borer. The Chinese agriculture university utilizes the insect-resistant gene mCry1Ac with the independent property right to culture an excellent transformant Bt-799, and the transgenic insect-resistant corn Bt-799 shows high resistance to Asiatic corn borers under the insect-grafting condition in the field heart-leaf stage. In 12 months of 2019, DBN9936 insect-resistant corn of Cry1Ab gene transferred by Beijing Dabei agricultural biotechnology limited and double-resistant 12-5 corn of Hangzhou Ruifeng biological technology limited and Cry1Ab/Cry2Aj transferred by Zhejiang university respectively obtain safety certificate examination and approval.
Cry1Ab is the most widely used transgenic crop, and is a parasporal crystal produced by bacillus thuringiensis and having a poisoning effect on lepidoptera pests, and has important application prospects in the field of biological control. The bacillus thuringiensis-endotoxin gene Cry1Ab is derived from microorganisms, but the transgenic plants thereof have the problems of low expression level, unstable expression products, poor insect resistance effect and the like. The expression level of GC content can be improved in transgenic plants by modifying a base sequence, so that the aim of killing pests is fulfilled (Koziel, 1993).
The generation of resistance by target pests seriously hinders the continuous application of Bt preparations and transgenic Bt insect-resistant corns, and a single transgenic insect-resistant plant is planted in a large area, so that the target pests can be caused to generate resistance. Current research has found that many insects have developed varying degrees of resistance to Bt toxic proteins indoors, and that resistance to Bt preparations or Bt crops has also been reported in field or greenhouse conditions. Pesticide cross-resistance refers to the phenomenon that a plant pest or pathogenic microorganism develops resistance to one insecticidal (bacterial) agent and also to another agent that has never been used but has a similar mechanism of action. The current research also finds that many pesticides generate cross resistance when applied, so that overcoming the problem of cross resistance is also an important subject in the research of various crop disease and insect resistance at present.
It is believed that domain i of Bt proteins is involved in pore formation, domain ii determines specific binding of the toxin to the receptor, and domain iii primarily regulates toxin activity. Indoor studies show that Asian corn borer Cry1F resistant strains have moderate cross resistance to Cry1Ab and Cry1Ac insecticidal proteins, but have no cross resistance to Cry1h or Cry1Ie, and the superposition of Cry1F and Cry1h or Cry1Ie can be used as a strategy for delaying the generation of resistance to Bt proteins by Asian corn borer (Wang et al, 2016). Further studies have shown that Cry1Ie has no cross-resistance with Cry1Ab, Cry1Ac, Cry1F and Cry1h, and can be stacked with these proteins to delay the development of resistance by Bt proteins (Wang et al, 2017).
Corn is an important grain crop and also an important feed and industrial raw material, and the current corn insect pest (mainly corn borer) is serious, so that the yield of the corn is greatly reduced, and therefore, the method has important significance for improving the corn yield and increasing the income of farmers by adopting effective measures to control the harm of the corn. Due to the lack of suitable insect-resistant varieties, the current main solution to insect damage is to spray chemical insecticides during growth; however, chemical pesticides kill both pests and their natural enemies, causing ecological imbalance and environmental pollution. By the transgenic technology, the insect-resistant gene can be introduced into a corn variety, so that the insect resistance of the transgenic corn is improved, the use amount of pesticides is reduced, and manpower, material resources and social resources are saved. The use of a single insect-resistant gene can cause the corn borer to generate resistance to Bt protein. Therefore, the application of new insect-resistant gene combinations, the improvement of the expression level of insecticidal proteins and the cultivation of novel insect-resistant transgenic corn are one of the most effective approaches to solve the problems.
Disclosure of Invention
In order to cultivate novel insect-resistant crops, the invention aims to provide an artificially synthesized insect-resistant protein mCry1Ia 2.
Another object of the present invention is to provide a nucleic acid molecule encoding the above protein.
Another object of the present invention is to provide a recombinant vector, host cell or recombinant bacterium containing the above gene.
Another object of the present invention is to provide the use of the above protein for controlling plant insect resistance, killing insects or improving insect resistance of transgenic plants.
It is a further object of the present invention to provide the use of the above-mentioned proteins in the preparation of insecticides or pest control formulations.
It is a further object of the present invention to provide a method for increasing the insect resistance of a plant.
It is a further object of the present invention to provide a method for breeding a transgenic plant with improved insect resistance.
It is a further object of the present invention to provide a method of slowing the population of Bt resistant corn borers.
In order to achieve the purpose of the invention, the invention provides the following scheme: an insect-resistant gene mCry1Ia2 is prepared by artificially optimizing, modifying and synthesizing three cry1Ab, cry1F and cry1Ie genes with high toxicity to lepidoptera pests to obtain a new DNA sequence, so that the codon sequence preferred by plants is utilized to improve the conversion power of the insect-resistant gene in the transgenic process, simultaneously improve the expression quantity and the stable expression characteristic in transgenic plants, and delay the generation of Bt protein resistance of Asiatic corn borer and improve the insecticidal activity of the gene by the combined application of three genes and six structural domains
Firstly, the artificially synthesized insect-resistant protein mCry1Ia2 provided by the invention is any one of the following proteins (a) to (d):
(a) the amino acid sequence of the polypeptide comprises an amino acid sequence shown in a sequence 2 in a sequence table;
(b) the amino acid sequence of the polypeptide consists of amino acid residues shown in a sequence 2 in a sequence table;
(c) protein which is obtained by substituting and/or deleting and/or adding one or more amino acid residues in the amino acid sequence of (a) or (b) and has an insect-resistant function and is derived from (a) or (b);
(d) a protein having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% homology with the protein defined in (a) or (b) and having an anti-insect function.
The sequence 2 is an amino acid sequence shown in SEQ ID No. 2.
The protein mCry1Ia2 in (b) above can be obtained by synthesizing its coding gene (SEQ ID NO: 1) and then performing biological expression. The gene encoding the protein mCry1Ia2 in (b) above can be obtained by deleting one or several codons for amino acid residues from the DNA sequence represented by nucleotides 1 to 4002 in sequence No.1 and/or by performing missense mutation of one or several base pairs.
The invention also provides a nucleic acid molecule for coding the protein, which is named as gene mCry1Ia 2.
The nucleic acid molecule is any one of the following nucleic acid molecules 1) to 4):
1) the coding region comprises a nucleic acid molecule shown as a sequence 1 in a sequence table;
2) the coding region consists of nucleic acid molecules shown in a sequence 1 in a sequence table;
3) nucleic acid molecules which hybridize with the nucleic acid sequences defined in 1) or 2) and which code for proteins having a function against insects;
4) a nucleic acid molecule having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% homology to a nucleic acid sequence defined in 1) or 2) and encoding a protein having an anti-insect function.
The nucleotide sequence of the nucleic acid molecule of the sequence 1 is shown as SEQ ID No. 1.
The nucleic acid molecule of the insect-resistant gene provided by the invention is formed by splicing a first functional domain 1392bp and a second functional domain 1392bp of Cry1Ab which are optimized by codons, a third functional domain 453bp of Cry1F and a fragment of three functional domains of Cry1Ie which are 2157bp in length to form a new nucleotide sequence of six domains and is named as mCry1Ia 2.
The invention also provides a vector containing the insect-resistant gene mCry1Ia2, preferably a bivalent vector pTF101, wherein the vector contains a screening gene bar gene, which is favorable for screening transformants and reducing the workload of later detection on one hand; on the other hand, in the case of a transformant, it can be further clarified that the gene of interest has been transferred into a recipient plant by detecting the bar gene.
Further, the present invention also provides a host cell, preferably LBA4404, containing the above vector.
The invention also provides a transformed plant cell or recombinant bacterium containing the insect-resistant gene mCry1Ia 2.
Furthermore, the invention also provides application of the protein, the nucleic acid molecule, the recombinant vector, the host cell or the recombinant bacterium in regulation and control of plant insect resistance;
or, the use of said protein, said nucleic acid molecule, recombinant vector, host cell or recombinant bacterium in pest control;
or, the protein, the nucleic acid molecule, the recombinant vector, the host cell or the recombinant bacterium is used for improving the insect resistance of the transgenic plant;
or the protein, the nucleic acid molecule, the recombinant vector, the host cell or the recombinant bacterium are applied to the preparation of pesticides or insect-resistant preparations.
The plant is preferably a crop, fruit tree or vegetable, such as corn, rice, potato, cotton, and the like.
Still further, the present invention provides an insecticide or a pest control formulation.
The active ingredients of the pesticide or the insect-resistant preparation provided by the invention are the protein, the DNA molecule or the recombinant vector, the host cell or the recombinant bacterium.
Further, the present invention provides a method for breeding a transgenic plant having improved insect resistance or a method for improving insect resistance of a plant.
The method provided by the invention comprises the following steps: and (3) increasing the expression quantity or activity of DNA molecules encoding the protein in the plant to obtain a transgenic plant, wherein the insect resistance of the transgenic plant is higher than that of the target plant.
In the above method, the expression level or activity of the DNA molecule encoding the protein is increased by introducing the DNA molecule encoding the protein into a target plant.
Still further, the present invention provides a method for solving Bt protein cross-resistance, comprising the steps of: effectively poisoning Cry1Ab, Cry1F and Cry1Ie poison protein resistant corn borer populations to obtain transgenic plants, wherein the transgenic plants effectively delay the output of the Bt protein resistant corn borers; the transgenic plant comprises an artificially synthesized insect-resistant protein mCry1Ia 2.
The gene mCry1Ia2 of the invention is operably connected with a prokaryotic expression vector, so that the toxicity of the Bt gene expression product synthesized by the invention to corn borers can be rapidly and preliminarily detected. The gene mCry1Ia2 is operably connected with a plant expression vector, the expression vector is introduced into corresponding agrobacterium, and genetic transformation is carried out by 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 skilled person can also transform the gene of the invention into bacteria or fungi, produce Bt protein by large-scale fermentation, and prepare the Bt protein into pesticide for controlling crop pests.
The invention has at least the following advantages and beneficial effects:
compared with the original Cry1Ab, Cry1F and Cry1Ie sequences, the artificially synthesized insect-resistant gene mCry1Ia2 sequence greatly enhances the expression of the insect-resistant gene mCry1Ia2 in plants and delays the generation of Bt protein resistance of the ostrinia nubilalis. Through NCBI database (https:// NCBI. nlm. nih. gov) comparison analysis, the similarity of the modified mCry1Ia2 gene and the CACL gene (gene sequence number, KY421715.1) in the priority ratio of 1-1605bp is 89.65%, and the similarity of the modified mCry1Ia2 gene and the Cry1Ie gene (gene sequence number, KX650634.1) in the priority ratio of 1846-4002bp is 82.00%. Alignment analysis of the encoded amino acid sequences showed that the engineered mCry1Ia2 encoded protein was 81.60% similar to the preferential ratio protein Cry1 accy 1I (AGS 47767.1). The insect-resistant gene mCry1Ia2 can be efficiently and stably expressed in plant cells.
After introducing the insect-resistant gene mCry1Ia2 into maize, a stably inherited mCry1Ia2 transformant 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.
In vitro experiments prove that the modified and synthesized Bt gene toxigenic protein has higher insecticidal activity to corn borers and has obvious insecticidal effect to corn borer populations with resistance to Cry1Ab, Cry1F and Cry1Ie toxigenic proteins. The invention constructs a novel plant expression vector by using a constitutive promoter, and the insect-resistant gene mCry1Ia2 can be stably and efficiently expressed in monocotyledons, so that the insect-resistant gene mCry1Ia2 can be further used for producing insect-resistant transgenic plants.
Drawings
FIG. 1 is T0Carrying out immunological detection on a target protein mCry1Ia2 of a generation transformant, wherein CK is a negative control of a non-transgenic seedling; the number of transgenic positive seedlings is 1 to 5. The upper band is the quality control line, and the lower band is the detection line indicating the detected protein. The result shows that the target protein expressed by the insect-resistant gene mCry1Ia2 is efficiently expressed in the transgenic corn.
FIG. 2 is T1Detecting the insecticidal property of the ostrinia nubilalis of the filigree of the generation transformant, wherein CK is negative control of the filigree of the non-transgenic seedling; the number of transgenic positive seedling filaments is 1 to 5. The result shows that the target protein expressed by the insect-resistant gene mCry1Ia2 is high-efficiency insecticidal in the transgenic corn.
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 mCry1Ia2 Gene
Cry1Ab, Cry1F and Cry1Ie were synthesized by codon optimization (the synthesis was done by Kinzhi, Suzhou, Inc.), and the first and second functional domains of Cry1Ab, the third functional domain of Cry1F and the three domain fragments of Cry1Ie were spliced together by the SOE method (1992, Chua 26104) to form a new six-domain mCry1Ia2 DNA sequence, the nucleotide sequence of which is shown in SEQ ID No. 1. It is generally believed that: the Bt protein is composed of three structural domains, wherein the structural domain I comprises 250-300 amino acids at the N terminal of the active insecticidal protein and consists of 7 alpha-helices, one alpha-helix has stronger hydrophobicity and is positioned at the center of the structural domain I, and the other 6 alpha-helices surround the periphery. It has been shown to be associated with the toxicity of insecticidal proteins, the hydrophobic alpha-helix having the ability to insert into and form channels in the midgut cell membranes of sensitive insects; the structure domain II is formed by three anti-phase parallel beta folds into a triangular structure, and each fold is connected through a small ring structure. There are two beta sheets that are highly homologous, each consisting of four anti-parallel peptide chains with beta conformation. The other beta sheet consists of three beta conformational peptide chains and a small alpha helix. This domain consists of the middle about 200 amino acids. The structural domain II is mainly involved in recognition and combination of target cells of the alimentary canal epidermis of a target insect and is a main factor for determining specificity of insecticidal protein. Domain III is highly entangled by two anti-parallel peptide chains with beta conformation to form a beta-three-splint structure, whose main function is to maintain the protein structure stable against degradation by insect proteases (Li et al, 1991; Grochilski et al, 1995). In addition, the domain may also serve to ensure stable binding of the toxic protein to the receptor. Through NCBI database (https:// NCBI. nlm. nih. gov) comparison analysis, the similarity of the modified mCry1Ia2 gene and the CACL gene (gene sequence number, KY421715.1) in the priority ratio of 1-1605bp is 89.65%, and the similarity of the modified mCry1Ia2 gene and the Cry1Ie gene (gene sequence number, KX650634.1) in the priority ratio of 1846-4002bp is 82.00%. Alignment analysis of the encoded amino acid sequences showed that the engineered mCry1Ia2 encoded protein was 81.60% similar to the preferential ratio protein Cry1 accy 1I (AGS 47767.1). The amino acid sequence of the code mCry1Ia2 is shown in SEQ ID NO. 2.
Example 2 expression of mCry1Ia2 Gene in prokaryotic System and toxicity testing of the product
In order to detect the in vitro expression of the modified mCry1Ia2 gene and the toxicity to corn borer, a Bt prokaryotic expression vector is constructed. According to the needAn NdeI endonuclease recognition site sequence AAGGAGATATACATA is added at the 5' end of the primer sequence, and is shown as SEQ ID NO. 3; the 3' end is added with XhoI endonuclease recognition site sequence GGTGGTGGTGCTCGAG which is shown in SEQ ID NO. 4. Designing a primer sequence as follows: f:AAGGAGATATACATATGGACAACAACCCCAAC, as shown in SEQ ID NO. 5; r:GGTGGTGGTGCTCGAGCATGTCCCGCTGCTCGAT, as shown in SEQ ID NO. 6. And amplifying the mCry1Ia2 gene by using the spliced DNA as a template and a primer added with a joint, and recovering and purifying the mCry1Ia2 gene fragment by using a gel recovery kit. pET30a was digested with restriction enzymes NdeI and XhoI, and recovered and purified. The two fragments were ligated to each other, and the resulting prokaryotic expression plasmid was designated as pET30a-mCry1Ia 2. PCR detection and sequencing show that the vector is constructed correctly. BL21(DE3) competent cells were transformed with pET30a-mCry1Ia 2.
After IPTG induction is carried out on Escherichia coli BL21 bacterial liquid containing pET30a-mCry1Ia2, Bt protein is extracted, and insect test is carried out on the corn borer by taking clear water and the Escherichia coli BL21 bacterial liquid containing an empty carrier pET30a as a control. The method comprises the following specific steps:
inoculating Escherichia coli BL21 single colony in 5ml LB liquid culture medium containing kanamycin, and culturing at 37 deg.C overnight.
② inoculating the bacterial liquid into 500ml LB (containing kanamycin) liquid culture medium, and culturing until OD is approximately equal to 0.5.
③ IPTG was added to a final concentration of 0.5mM and the induction was continued for 4 hours with shaking.
Fourthly, centrifuging for 10min at 4000rpm and collecting thalli.
Fifthly, 20ml of lysis buffer (2mM Tris-HCl; 0.2mM CaCl) is added2(ii) a pH 8.0), resuspending the cells, adding lysozyme to a final concentration of 1mg/ml, and standing on ice for 30 min.
Sixthly, crushing thalli by ultrasonic wave (crushing parameter: working for 3s, interval for 3s, 80 times, ice bath crushing), centrifuging for 10min at 4000rpm, and collecting supernatant.
Seventhly, adding the collected supernatant into a feed for feeding the corn borers. The bacterial liquid of Escherichia coli BL21 containing empty vector pET30a was used as negative control.
Placing a feed on a 24-hole plate, connecting each hole with the feed to 1-head corn borer of 2-3 years old, connecting each hole with 100 holes, and repeating for three times. Culturing in an environment with the temperature of 26-28 ℃ and the relative humidity of about 70%, and carrying out toxicity identification after 7 days: the result shows that the Bt protein encoded by the secreted and expressed mCry1Ia2 gene has a good insecticidal effect, the death rate of the ostrinia nubilalis reaches 100%, and the growth of the ostrinia nubilalis is obviously inhibited (Table 1).
TABLE 1 toxicity test results of prokaryotic expression product of mCry1Ia2 gene
Treatment (three replicates) | Number of tested insects | Average mortality (%) |
H2O (negative control) | 500 | 0 |
pET30a (negative control) | 500 | 0 |
Positive control | 500 | 100 |
mCry1Ia2 | 500 | 100 |
Example 3 expression of the mCry1Ia2 Gene in transgenic plants and toxicity testing of the expression product
SmaI endonuclease recognition site sequence CTCTAGAGGATCCCC is added at the 5 'end and the 3' end of the primer sequence respectively, and is shown as SEQ ID NO. 7; and TCGAGCTCGGTACCC, as shown in SEQ ID NO. 8. The design primer is: f: 5'CTCTAGAGG ATCCCCATGGACAACAACCCCAAC 3' as shown in SEQ ID NO. 9; r is 5'TCGAGCTCGGTACCCCTACTACTCGAGTGTGGCAGT 3', as shown in SEQ ID NO.10, using the synthesized mCry1Ia2 nucleotide sequence as a template, amplifying by using a primer with a joint, and recovering the target fragment by using a gel recovery purification kit. At the same time, Sma I is used for enzyme digestion of the plant expression vector pTF101, and the pTF101 fragment after enzyme digestion is recovered and purified. The two fragments were ligated (In-Fusion HD cloning kit, Clontech) to construct the eukaryotic expression plasmid pTF101-mCry1Ia2 (promoter CaMV35S, marker gene is herbicide-resistant gene Bar of Streptomyces hygroscopicus). PCR detection and sequencing show that the vector is constructed correctly.
Wherein, the pTF101(pTF101-35S-MCS-Bar) plasmid is a plasmid constructed on the basis of pCAMBIA1300 plasmid and contains a target gene insertion box and a herbicide-resistant gene Bar from streptomyces hygroscopicus. The vector can be used for genetic transformation of corn receptor material.
The insertion sequence is introduced into the stem tip tissue of a receptor plant by adopting an agrobacterium-mediated transformation method (strain LBA4404), and a transgenic plant is obtained after screening of herbicide bialaphos. When the transplanted survived transformed plant grows 7-8 leaves, taking the leaves to extract DNA, and detecting the exogenous gene by adopting a PCR technology.
Detection of target protein mCry1Ia2 (Cry1Ab immunological detection):
1. taking about 1cm2Left and right fresh young leaves were placed in a 1.5ml Eppendorf tube. The tube with the leaves is then inserted in an ice bin to maintain freshness.
2. Liquid nitrogen was taken, the material was snap frozen, ground to powder with a drill bit, and 500 μ L-lml SEB4 sample extraction buffer was quickly added to the tube.
3. The test strip (Shanghai Youlong Biotech Co., Ltd.) was taken out, and the top end of the test strip was held by hand to make a test mark. The protective film is not removed. The test strip is held upright and the labeled end is inserted into a centrifuge tube or extraction bag. The insertion portion does not exceed 0.5 cm. The inserted state is maintained throughout the detection process.
4. The control line appeared within 3-5 minutes, the maximum reaction time was 30 minutes, at which time the test strip was removed. The quality control line is used to ensure the accuracy of the test results. If the quality control line does not appear, the detection is invalid. The time at which the signal is generated varies due to the difference in fluidity of the sample. If the sample is positive, a test line will appear. If the sample is negative, the test line will not appear. If the test results are to be stored for a long period of time, the sample pad can be cut off and blotted dry with a paper towel, which will prevent the remaining liquid from interfering with the results. The depth of the detection line reflects the content of the protein to be detected (FIG. 1). Wherein CK is a negative control of a non-transgenic seedling; the number of transgenic positive seedlings is 1 to 5. The upper band is the quality control line, and the lower band is the detection line indicating the detected protein. The result shows that the target protein expressed by the insect-resistant gene mCry1Ia2 is efficiently expressed in the transgenic corn.
Indoor insect killing detection of insect-resistant corn filaments by transferring mCry1Ia2 gene:
place the cornsilk in petri dishes and 30 heads of corn borer larvae as one replicate per petri dish, with 5 replicates per treatment set up. Placing the strain in an artificial climate box for feeding, wherein the culture conditions are as follows: temperature 28 ℃, RH 80%, illumination period 16L: and 8D, timely supplementing the same tissue sample according to the situation that the corn silk is eaten by the corn borers. The survival number of the larvae of the ostrinia nubilalis is counted for 1 time every 48 hours from the inoculation, and the investigation is carried out for 7 days. The survival rate of the larvae of corn borer fed by different corn filaments was calculated according to the number of the larvae survived in each treatment (fig. 2). The indoor bioassay results of the silks show that the survival rate of the corn borers is remarkably reduced by less than 20% on day 3; after 7 days, the survival rate of the transgenic corn filament fed to the Asiatic corn borers is 0%, and the survival rate of the negative control fed to the Asiatic corn borers is close to 100%, which indicates that the transgenic mCry1Ia2 gene insect-resistant corn filament has good resistance to the Asiatic corn borers.
TABLE 2 toxicity test results of positive plantlet filaments transformed with mCry1Ia2 gene
Treatment (three replicates) | Number of tested insects | 7 balance average mortality (%) |
Negative control | 30 | 0 |
Transgenic |
30 | 100 |
Transgenic |
30 | 100 |
Transgenic |
30 | 100 |
Transgenic |
30 | 100 |
Transgenic positive seedling 5 | 30 | 100 |
Example 4 mCry1Ia2 protein insecticidal Activity and Cross-resistance assays
Asiatic corn borer sensitive strain (ACB-BtS) is collected from the population of Zhengzhou corn field in Henan, and is fed with agar-free semi-artificial feed under the conditions of 28 +/-1 ℃ and 16L/8D, RH 70-80% of photoperiod. The method adopts a feed mixing method to carry out indoor artificial jigging, namely Cry1Ab, Cry1F and Cry1Ie proteins are added into semi-artificial feed of the Asiatic corn borers to prepare jigging feed, and the artificial feeding is started by the jigging feed in a larval stage. Cry1Ab, Cry1F and Cry1Ie corn borer resistant populations (ACB-AbR, ACB-FR and ACB-IeR) of the rejected 20, 14 and 16 generations are obtained respectively under indoor conditions, and the resistance indexes are improved by 405.4, 248.6 and 320.2 times respectively. The biological assay of the toxicity of the mCry1Ia2 protein to the resistant species group of the three corn borers adopts a feed mixing method, namely, 9 concentration gradients of the Bt protein are prepared to prepare a raw assay feed, and distilled water is used as a control. And (3) putting 1 to-be-tested larvae of the ostrinia nubilalis into a 48-hole culture plate without holes, feeding the larvae with each concentration of 1 plate under the conditions of 28 +/-1 ℃ and a light cycle of 16L:8D, RH 70-80%, recording survival number of the larvae after 7 days, weighing and repeating for 3 times. LC50 and 95% confidence intervals of mCry1Ia2 protein on corn borer of each resistant strain are analyzed by Poloplus statistical software, and chi-square test is adopted for the analysis of difference significance. As shown in table 3, the results showed that the maize borer resistant populations culled with the Cry1Ab, Cry1F and Cry1Ie proteins did not have reduced sensitivity to the mCry1Ia2 protein, i.e. did not cause cross-resistance of 3 single Bt proteins.
Indoor bioassay for testing toxicity on 4 corn borer populations by utilizing mCry1Ia2, Cry1Ab, Cry1F and Cry1Ie respectively is carried out, and equivalent Bt protein is added into artificial feed, so that the results show that the mCry1Ia2 can completely poison 4 corn borer populations in 7 days, the Cry1Ab and Cry1F can only completely poison 2 corn borer populations, and the Cry1Ie can poison 3 corn borer populations (Table 4). The toxicity of an Asian corn borer sensitive line (ACB-BtS) is respectively tested by using mCry1Ia2, Cry1Ab, Cry1F and Cry1Ie, an equal amount of Bt protein is added into artificial feed, the mCry1Ia2 can completely poison corn borers in 5 days, and the Cry1Ab, Cry1F and Cry1Ie can completely poison corn borers in 7 days (table 5), and the results show that the insecticidal activity of the mCry1Ia2 protein for the corn borers is stronger.
TABLE 3 results of sensitivity analysis of mCry1Ia2 to different Asian corn borer populations
Corn borer population | LC50(95%FL)(ug/g) | χ2 |
ACB-BtS | 0.48(0.33-0.68) | |
ACB-AbR | 0.45(0.28-0.64) | 13.83 |
ACB-FR | 0.52(0.38-0.72) | 28.18 |
ACB-IeR | 0.50(0.35-0.70) | 26.49 |
TABLE 44 survival rate (%)
mCry1Ia2 | Cry1Ab | Cry1F | Cry1Ie | |
ACB-BtS | 0 | 0 | 0 | 0 |
ACB-AbR | 0 | 100 | 30.00±7.07 | 0 |
ACB-FR | 0 | 28.00±4.47 | 100 | 0 |
ACB-IeR | 0 | 0 | 0 | 100 |
TABLE 5 survival rate (%)
1 |
3 days | 5 days | 7 days | |
mCry1Ia2 | 72.00±10.95a | 18.00±8.37a | 0.00±0.00a | 0.00±0.00a |
Cry1Ab | 78.00±10.95a | 25.00±7.07b | 4.00±5.48b | 0.00±0.00a |
Cry1F | 82.00±8.37a | 30.00±10b | 8.00±4.47b | 0.00±0.00a |
Cry1Ie | 84.00±8.94a | 34.00±8.37b | 4.00±5.48b | 0.00±0.00a |
Note that the difference in letters in the same column indicates significant difference (P <0.05)
Indoor bioassay of different resistant populations of ostrinia nubilalis was performed using mCry1Ia2 transgenic maize obtained in example 3, the procedure was the same as above. The indoor bioassay results of the silks show that the survival rates of the corn borers of different resistant populations are remarkably reduced to be below 20% on day 3; after 7 days, the survival rate of the transgenic corn filaments fed with the Asiatic corn borers of different resistant populations is 0%, and the survival rate of the negative control fed with the Asiatic corn borer larvae is close to 100%, which shows that the transgenic mCry1Ia2 gene insect-resistant corn filaments have high-efficiency poisoning Cry1Ab, Cry1F and Cry1Ie insect-resistant corn borer populations, and the generation of cross resistance is avoided (Table 6).
TABLE 6 toxicity test results of mCry1Ia2 transgenic positive seedling filaments on different resistant populations of Asiatic corn borer
Treatment (three replicates) | Number of tested insects | 7 balance average survival rate (%) |
ACB-BtS | 100 | 0 |
ACB-AbR | 100 | 0 |
ACB-FR | 100 | 0 |
ACB-IeR | 100 | 0 |
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> Heilongjiang Roc agriculture Co Ltd
<120> artificially synthesized insect-resistant protein mCry1Ia2, and preparation method and application thereof
<130> P200256
<141> 2020-09-03
<160> 10
<170> SIPOSequenceListing 1.0
<210> 1
<211> 4002
<212> DNA
<213> Artificial sequence (artificial sequence)
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agcctgaccc agttcctcct gtccgagttc gtcccgggcg ccggcttcgt gctgggcctg 180
gtcgacatca tctggggcat cttcggcccc agccagtggg acgcgttcct cgtccagatc 240
gagcagctga tcaaccagcg catcgaggag ttcgcccgca accaggcgat cagccgcctg 300
gagggcctgt ccaacctgta ccagatctac gcggagtcct tccgcgagtg ggaggcggac 360
cccaccaacc ccgccctgag ggaggagatg cgcatccagt tcaacgacat gaactccgcg 420
ctgacgaccg ccatccccct gttcgccgtg cagaactacc aggtgcccct gctgagcgtc 480
tacgtgcagg ccgccaacct gcacctgtcg gtcctccgcg acgtcagcgt cttcggccag 540
cgctggggct tcgacgccgc cacgatcaac tcccgctaca acgacctgac ccgcctgatc 600
ggcaactaca ccgaccacgc cgtgcgctgg tacaacaccg ggctggagcg cgtgtggggg 660
cccgacagcc gcgactggat caggtacaac cagttccgcc gcgagctgac gctgaccgtg 720
ctcgacatcg tcagcctgtt ccccaactac gacagccgca cgtaccccat ccgcaccgtg 780
agccagctga cgcgcgagat ctacaccaac cccgtgctgg agaacttcga cggctccttc 840
cgcggcagcg cgcagggcat cgaggggagc atccgctccc cccacctgat ggacatcctc 900
aactcgatca ccatctacac ggacgcccac cgcggcgagt actactggag cggccaccag 960
atcatggcca gccccgtcgg cttctcgggc ccggagttca cgttccccct gtacggcacc 1020
atgggcaacg ccgcgccgca gcagcgcatc gtggcgcagc tgggccaggg cgtgtaccgc 1080
acgctcagca gcacgctgta ccggcggccg ttcaacatcg gcatcaacaa ccagcagctg 1140
agcgtgctgg acggcaccga gttcgcgtac ggcacgagca gcaacctgcc cagcgccgtg 1200
taccgcaagt cgggcacggt ggacagcctg gacgagatcc ccccgcagaa caacaacgtc 1260
ccgccgcgac agggcttcag ccaccggctg tcgcacgtca gcatgttccg cagcggcttc 1320
agcaactcca gcgtctcgat catccgggcg ccgatgttca gctggatcca ccgctcggcc 1380
gagttcaaca acaccatcga ccccgagagg atcacccaga tccccttggt gaaggcgcac 1440
acgctccagt cgggcaccac ggtcgtcagg gggccggggt tcacgggcgg cgacatcctc 1500
cgacgcacca gcggcggccc cttcgcgtac accatcgtca acatcaacgg gcagctcccc 1560
cagaggtacc gggccaggat ccgctacgcc tccaccacca acctgaggat ctacgtcacg 1620
gtcgcggggg agcggatctt cgccgggcag ttcaacaaga cgatggacac cggggacccc 1680
ctcacgttcc agtccttctc ctacgccacc atcaacaccg cgttcacctt ccccatgagc 1740
cagagcagct tcacggtcgg ggccgacacc ttcagctcgg gcaacgaggt gtacatcgac 1800
aggttcgagt tgatccccgt caccgccacg ctcgaggccg agtacaagct gaagaaccag 1860
gacaagcacc agagcttctc cagcaacgcg aaggtcgaca agatctccac ggactcgctg 1920
aagaacgaga cggacatcga gttgcagaac atcaaccacg aggactgctt gaagatgtcc 1980
gagtacgaga acgtcgagcc gttcgtcagc gcctcgacca tccagacggg catcgggatc 2040
gccggcaaga tcctcgggac cctgggggtc ccgttcgccg ggcagatcgc cagcctctac 2100
agcttcatct tgggcgagct ctggccgaag gggaagagcc agtgggagat cttcatggag 2160
cacgtcgagg agctcatcgc gcagaagatc tcgacctacg cgaggaacaa ggcgctcacg 2220
gacttgaagg gcttggggga cgccttggcg gtctaccacg agtcgctcga gagctggatc 2280
gagaaccgca acaacacgag ggccaggagc gtcgtcaaga gccagtacat ctcgctggag 2340
ctcatgttcg tccagaagtt gccgtccttc gcggtgtccg gggaggaggt cccgctgttg 2400
cccatctacg cccaggccgc gaacctgcac ttgttgctgt tgagggacgc gtccgtcttc 2460
ggcaaggagt ggggcttgtc gtcctcggag atctcgacgt tctacaaccg gcaggtcgag 2520
cgagcgggcg actactccga ccactgcgtg aagtggtaca gcacggggct gaacaacttg 2580
agggggacga acgccgagag ctgggtccgg tacaaccagt tccggaagga catgacgttg 2640
atggtcctgg acttgatcgc gttgttcccc agctacgaca cgctcgtcta ccccatcaag 2700
accacctccc agctcacgag ggaggtctac acggacgcga tcgggacggt ccaccccaac 2760
gcgagcttcg cgagcacgac ctggtacaac aacaacgcgc cgtcgttctc cgccatcgag 2820
tccgccgtcg tccgaaaccc gcacctgctc gacttcttgg agcaggtcac gatctacagc 2880
ttgttgagca ggtggagcaa cacccagtac atgaacatgt ggggcggcca caggctcgag 2940
ttccgaacga tcggcggcgt gttgaacacc tcgacgcagg ggtccacgaa cacctccatc 3000
aacccggtca cgttgccgtt cacgtcccga gacgtctaca ggaccgagtc gttggcgggg 3060
ctgaacctgt tcttgaccca gccggtcaac ggcgtcccga gggtcgactt ccactggaag 3120
ttcgccacgc tcccgatcgc gtccgacaac ttctactacc ccgggtacgc cggcatcggg 3180
acgcagttgc aggactcgga gaacgagttg ccgccggaga cgacggtcca gcccaactac 3240
gagtcgtaca gccacaggtt gtcccacatc ggcctcatct cggcgtcgca cgtgaaggcg 3300
ttggtctact cctggacgca ccggagcgcg gaccggacga acacgatcga gcccaacagc 3360
atcacgcaga tccccttggt caaggcgttc aacctgtcct cgggggccgc cgtcgtcagg 3420
ggcccgggct tcacgggggg cgacatcctc cgaaggacga acaccgggac gttcggggac 3480
atccgagtca acatcaaccc ccccttcgcg cagaggtacc gcgtcaggat ccggtacgcg 3540
tccaccacgg acttgcagtt ccacacgtcg atcaacggca gggccatcaa ccaggggaac 3600
ttctcggcga ccatgaacag gggcgaggac ttggagtaca ggaccttcag gaccgtcggc 3660
ttcaccaccc ccttcagctt ctcggacgtc cagagcacgt tcacgatcgg ggcctggaac 3720
ttctcctcgg ggaacgacgt ctacatcgac cgaatcgagt tcgtcccggt cgaggtcccc 3780
tacgaggagg agtacgactt cgagaaggtg caggaggcgg tcaccgcgct gttcacgtcc 3840
acgaacccca gggagttgaa gacggacgtc acggactacc acatcgacca ggtctcgaac 3900
ttggtcgagt ccctgtcgga cgagttctac ctcgacgaga agagggagtt gttcgagatc 3960
gtcaagtacg tcaagcagct caacatcgag cgggacatgt ag 4002
<210> 2
<211> 1333
<212> PRT
<213> Artificial sequence (artificial sequence)
<400> 2
Met Asp Asn Asn Pro Asn Ile Asn Glu Cys Ile Pro Tyr Asn Cys Leu
1 5 10 15
Ser Asn Pro Glu Val Glu Val Leu Gly Gly Glu Arg Ile Glu Thr Gly
20 25 30
Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln Phe Leu Leu Ser
35 40 45
Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu Val Asp Ile Ile
50 55 60
Trp Gly Ile Phe Gly Pro Ser Gln Trp Asp Ala Phe Leu Val Gln Ile
65 70 75 80
Glu Gln Leu Ile Asn Gln Arg Ile Glu Glu Phe Ala Arg Asn Gln Ala
85 90 95
Ile Ser Arg Leu Glu Gly Leu Ser Asn Leu Tyr Gln Ile Tyr Ala Glu
100 105 110
Ser Phe Arg Glu Trp Glu Ala Asp Pro Thr Asn Pro Ala Leu Arg Glu
115 120 125
Glu Met Arg Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala
130 135 140
Ile Pro Leu Phe Ala Val Gln Asn Tyr Gln Val Pro Leu Leu Ser Val
145 150 155 160
Tyr Val Gln Ala Ala Asn Leu His Leu Ser Val Leu Arg Asp Val Ser
165 170 175
Val Phe Gly Gln Arg Trp Gly Phe Asp Ala Ala Thr Ile Asn Ser Arg
180 185 190
Tyr Asn Asp Leu Thr Arg Leu Ile Gly Asn Tyr Thr Asp His Ala Val
195 200 205
Arg Trp Tyr Asn Thr Gly Leu Glu Arg Val Trp Gly Pro Asp Ser Arg
210 215 220
Asp Trp Ile Arg Tyr Asn Gln Phe Arg Arg Glu Leu Thr Leu Thr Val
225 230 235 240
Leu Asp Ile Val Ser Leu Phe Pro Asn Tyr Asp Ser Arg Thr Tyr Pro
245 250 255
Ile Arg Thr Val Ser Gln Leu Thr Arg Glu Ile Tyr Thr Asn Pro Val
260 265 270
Leu Glu Asn Phe Asp Gly Ser Phe Arg Gly Ser Ala Gln Gly Ile Glu
275 280 285
Gly Ser Ile Arg Ser Pro His Leu Met Asp Ile Leu Asn Ser Ile Thr
290 295 300
Ile Tyr Thr Asp Ala His Arg Gly Glu Tyr Tyr Trp Ser Gly His Gln
305 310 315 320
Ile Met Ala Ser Pro Val Gly Phe Ser Gly Pro Glu Phe Thr Phe Pro
325 330 335
Leu Tyr Gly Thr Met Gly Asn Ala Ala Pro Gln Gln Arg Ile Val Ala
340 345 350
Gln Leu Gly Gln Gly Val Tyr Arg Thr Leu Ser Ser Thr Leu Tyr Arg
355 360 365
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
385 390 395 400
Tyr Arg Lys Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln
405 410 415
Asn Asn Asn Val Pro Pro Arg Gln Gly Phe Ser His Arg Leu Ser His
420 425 430
Val Ser Met Phe Arg Ser Gly Phe Ser Asn Ser Ser Val Ser Ile Ile
435 440 445
Arg Ala Pro Met Phe Ser Trp Ile His Arg Ser Ala Glu Phe Asn Asn
450 455 460
Thr Ile Asp Pro Glu Arg Ile Thr Gln Ile Pro Leu Val Lys Ala His
465 470 475 480
Thr Leu Gln Ser Gly Thr Thr Val Val Arg Gly Pro Gly Phe Thr Gly
485 490 495
Gly Asp Ile Leu Arg Arg Thr Ser Gly Gly Pro Phe Ala Tyr Thr Ile
500 505 510
Val Asn Ile Asn Gly Gln Leu Pro Gln Arg Tyr Arg Ala Arg Ile Arg
515 520 525
Tyr Ala Ser Thr Thr Asn Leu Arg Ile Tyr Val Thr Val Ala Gly Glu
530 535 540
Arg Ile Phe Ala Gly Gln Phe Asn Lys Thr Met Asp Thr Gly Asp Pro
545 550 555 560
Leu Thr Phe Gln Ser Phe Ser Tyr Ala Thr Ile Asn Thr Ala Phe Thr
565 570 575
Phe Pro Met Ser Gln Ser Ser Phe Thr Val Gly Ala Asp Thr Phe Ser
580 585 590
Ser Gly Asn Glu Val Tyr Ile Asp Arg Phe Glu Leu Ile Pro Val Thr
595 600 605
Ala Thr Leu Glu Ala Glu Tyr Lys Leu Lys Asn Gln Asp Lys His Gln
610 615 620
Ser Phe Ser Ser Asn Ala Lys Val Asp Lys Ile Ser Thr Asp Ser Leu
625 630 635 640
Lys Asn Glu Thr Asp Ile Glu Leu Gln Asn Ile Asn His Glu Asp Cys
645 650 655
Leu Lys Met Ser Glu Tyr Glu Asn Val Glu Pro Phe Val Ser Ala Ser
660 665 670
Thr Ile Gln Thr Gly Ile Gly Ile Ala Gly Lys Ile Leu Gly Thr Leu
675 680 685
Gly Val Pro Phe Ala Gly Gln Ile Ala Ser Leu Tyr Ser Phe Ile Leu
690 695 700
Gly Glu Leu Trp Pro Lys Gly Lys Ser Gln Trp Glu Ile Phe Met Glu
705 710 715 720
His Val Glu Glu Leu Ile Ala Gln Lys Ile Ser Thr Tyr Ala Arg Asn
725 730 735
Lys Ala Leu Thr Asp Leu Lys Gly Leu Gly Asp Ala Leu Ala Val Tyr
740 745 750
His Glu Ser Leu Glu Ser Trp Ile Glu Asn Arg Asn Asn Thr Arg Ala
755 760 765
Arg Ser Val Val Lys Ser Gln Tyr Ile Ser Leu Glu Leu Met Phe Val
770 775 780
Gln Lys Leu Pro Ser Phe Ala Val Ser Gly Glu Glu Val Pro Leu Leu
785 790 795 800
Pro Ile Tyr Ala Gln Ala Ala Asn Leu His Leu Leu Leu Leu Arg Asp
805 810 815
Ala Ser Val Phe Gly Lys Glu Trp Gly Leu Ser Ser Ser Glu Ile Ser
820 825 830
Thr Phe Tyr Asn Arg Gln Val Glu Arg Ala Gly Asp Tyr Ser Asp His
835 840 845
Cys Val Lys Trp Tyr Ser Thr Gly Leu Asn Asn Leu Arg Gly Thr Asn
850 855 860
Ala Glu Ser Trp Val Arg Tyr Asn Gln Phe Arg Lys Asp Met Thr Leu
865 870 875 880
Met Val Leu Asp Leu Ile Ala Leu Phe Pro Ser Tyr Asp Thr Leu Val
885 890 895
Tyr Pro Ile Lys Thr Thr Ser Gln Leu Thr Arg Glu Val Tyr Thr Asp
900 905 910
Ala Ile Gly Thr Val His Pro Asn Ala Ser Phe Ala Ser Thr Thr Trp
915 920 925
Tyr Asn Asn Asn Ala Pro Ser Phe Ser Ala Ile Glu Ser Ala Val Val
930 935 940
Arg Asn Pro His Leu Leu Asp Phe Leu Glu Gln Val Thr Ile Tyr Ser
945 950 955 960
Leu Leu Ser Arg Trp Ser Asn Thr Gln Tyr Met Asn Met Trp Gly Gly
965 970 975
His Arg Leu Glu Phe Arg Thr Ile Gly Gly Val Leu Asn Thr Ser Thr
980 985 990
Gln Gly Ser Thr Asn Thr Ser Ile Asn Pro Val Thr Leu Pro Phe Thr
995 1000 1005
Ser Arg Asp Val Tyr Arg Thr Glu Ser Leu Ala Gly Leu Asn Leu Phe
1010 1015 1020
Leu Thr Gln Pro Val Asn Gly Val Pro Arg Val Asp Phe His Trp Lys
1025 1030 1035 1040
Phe Ala Thr Leu Pro Ile Ala Ser Asp Asn Phe Tyr Tyr Pro Gly Tyr
1045 1050 1055
Ala Gly Ile Gly Thr Gln Leu Gln Asp Ser Glu Asn Glu Leu Pro Pro
1060 1065 1070
Glu Thr Thr Val Gln Pro Asn Tyr Glu Ser Tyr Ser His Arg Leu Ser
1075 1080 1085
His Ile Gly Leu Ile Ser Ala Ser His Val Lys Ala Leu Val Tyr Ser
1090 1095 1100
Trp Thr His Arg Ser Ala Asp Arg Thr Asn Thr Ile Glu Pro Asn Ser
1105 1110 1115 1120
Ile Thr Gln Ile Pro Leu Val Lys Ala Phe Asn Leu Ser Ser Gly Ala
1125 1130 1135
Ala Val Val Arg Gly Pro Gly Phe Thr Gly Gly Asp Ile Leu Arg Arg
1140 1145 1150
Thr Asn Thr Gly Thr Phe Gly Asp Ile Arg Val Asn Ile Asn Pro Pro
1155 1160 1165
Phe Ala Gln Arg Tyr Arg Val Arg Ile Arg Tyr Ala Ser Thr Thr Asp
1170 1175 1180
Leu Gln Phe His Thr Ser Ile Asn Gly Arg Ala Ile Asn Gln Gly Asn
1185 1190 1195 1200
Phe Ser Ala Thr Met Asn Arg Gly Glu Asp Leu Glu Tyr Arg Thr Phe
1205 1210 1215
Arg Thr Val Gly Phe Thr Thr Pro Phe Ser Phe Ser Asp Val Gln Ser
1220 1225 1230
Thr Phe Thr Ile Gly Ala Trp Asn Phe Ser Ser Gly Asn Asp Val Tyr
1235 1240 1245
Ile Asp Arg Ile Glu Phe Val Pro Val Glu Val Pro Tyr Glu Glu Glu
1250 1255 1260
Tyr Asp Phe Glu Lys Val Gln Glu Ala Val Thr Ala Leu Phe Thr Ser
1265 1270 1275 1280
Thr Asn Pro Arg Glu Leu Lys Thr Asp Val Thr Asp Tyr His Ile Asp
1285 1290 1295
Gln Val Ser Asn Leu Val Glu Ser Leu Ser Asp Glu Phe Tyr Leu Asp
1300 1305 1310
Glu Lys Arg Glu Leu Phe Glu Ile Val Lys Tyr Val Lys Gln Leu Asn
1315 1320 1325
Ile Glu Arg Asp Met
1330
<210> 3
<211> 15
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 3
aaggagatat acata 15
<210> 4
<211> 16
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 4
ggtggtggtg ctcgag 16
<210> 5
<211> 32
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 5
aaggagatat acatatggac aacaacccca ac 32
<210> 6
<211> 34
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 6
ggtggtggtg ctcgagcatg tcccgctgct cgat 34
<210> 7
<211> 15
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 7
ctctagagga tcccc 15
<210> 8
<211> 15
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 8
tcgagctcgg taccc 15
<210> 9
<211> 33
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 9
ctctagagga tccccatgga caacaacccc aac 33
<210> 10
<211> 36
<212> DNA
<213> Artificial sequence (artificial sequence)
<400> 10
tcgagctcgg tacccctact actcgagtgt ggcagt 36
Claims (10)
1. An artificially synthesized insect-resistant protein mCry1Ia2, which is any one of the following proteins (a) to (d):
(a) the amino acid sequence of the polypeptide comprises an amino acid sequence shown in a sequence 2 in a sequence table;
(b) the amino acid sequence of the polypeptide consists of amino acid residues shown in a sequence 2 in a sequence table;
(c) protein which is obtained by substituting and/or deleting and/or adding one or more amino acid residues in the amino acid sequence of (a) or (b) and has an insect-resistant function and is derived from (a) or (b);
(d) a protein having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% homology with the protein defined in (a) or (b) and having an anti-insect function.
2. A nucleic acid molecule encoding the protein of claim 1.
3. The nucleic acid molecule according to claim 2, wherein the nucleic acid molecule is any one of the following 1) to 4):
1) the coding region comprises a nucleic acid molecule shown as a sequence 1 in a sequence table;
2) the coding region consists of nucleic acid molecules shown in a sequence 1 in a sequence table;
3) nucleic acid molecules which hybridize with the nucleic acid sequences defined in 1) or 2) and which code for proteins having a function against insects;
4) a nucleic acid molecule having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% homology to a nucleic acid sequence defined in 1) or 2) and encoding a protein having an anti-insect function.
4. The nucleic acid molecule according to claim 2, characterized in that it is a new nucleotide sequence of six domains formed by splicing together the codon optimized first and second functional domains 1392bp of Cry1Ab and the third functional domain 453bp of Cry1F and a fragment of three functional domains of Cry1Ie, which is 2157bp long, and named mCry1Ia 2.
5. A recombinant vector, host cell or recombinant bacterium comprising the nucleic acid molecule of any one of claims 2 to 4.
6. Use of the protein of claim 1, the nucleic acid molecule of any one of claims 2 to 4, or the recombinant vector, host cell, or recombinant bacterium of claim 5 for modulating insect resistance in a plant;
or, the use of a protein according to claim 1, a nucleic acid molecule according to any one of claims 2 to 4 or a recombinant vector, host cell or recombinant bacterium according to claim 5 for combating pests;
or, the use of a protein according to claim 1, a nucleic acid molecule according to any one of claims 2 to 4 or a recombinant vector, host cell or recombinant bacterium according to claim 5 for increasing the insect resistance of transgenic plants;
or the protein of claim 1, the nucleic acid molecule of any one of claims 2 to 4 or the recombinant vector, host cell or recombinant bacterium of claim 5 for use in the preparation of a pesticide or pest control formulation.
7. The use according to claim 6, wherein the plant is a crop, a fruit tree or a vegetable.
8. A pesticide or pest control agent, the active ingredient of which is a protein according to claim 1, a nucleic acid molecule according to any one of claims 2 to 4 or a recombinant vector, host cell or recombinant bacterium according to claim 5.
9. A method for improving insect resistance of a plant, comprising the steps of: increasing the expression or activity of a DNA molecule encoding the protein of claim 1 in a plant, to obtain a transgenic plant having a higher resistance to insects than said plant of interest.
10. A method of addressing Bt protein cross-resistance, comprising the steps of: effectively poisoning Cry1Ab, Cry1F and Cry1Ie poison protein resistant corn borer populations to obtain transgenic plants, wherein the transgenic plants effectively delay the generation of Bt protein resistant corn borers; the transgenic plant comprises an artificially synthesized insect-resistant protein mCry1Ia 2.
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CN113896786A (en) * | 2021-09-15 | 2022-01-07 | 中国农业科学院生物技术研究所 | Artificially synthesized material with biological activity and agricultural application thereof |
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