NL2027065B1 - Hybridoma cell strain secreting monoclonal antibody against tobacco ringspot virus, antibody therefrom and antibody preparation method thereof - Google Patents
Hybridoma cell strain secreting monoclonal antibody against tobacco ringspot virus, antibody therefrom and antibody preparation method thereof Download PDFInfo
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- NL2027065B1 NL2027065B1 NL2027065A NL2027065A NL2027065B1 NL 2027065 B1 NL2027065 B1 NL 2027065B1 NL 2027065 A NL2027065 A NL 2027065A NL 2027065 A NL2027065 A NL 2027065A NL 2027065 B1 NL2027065 B1 NL 2027065B1
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- monoclonal antibody
- variable region
- ser
- antibody
- ringspot virus
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
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- Medicinal Chemistry (AREA)
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Abstract
The present invention provides a hybridoma cell strain secreting monoclonal antibody against Tobacco ringspot virus as well as antibody therefrom and antibody preparation method thereof, wherein: BALB/c mice are immunized with the recombinant expression of full-length tobacco ringspot virus coat protein TRSV (523aa) to obtain a hybridoma cell strain, and the cell strain which can produce monoclonal antibody specifically recognize the Tobacco ringspot virus coat protein are screened, then monoclonal antibodies specifically recognizing Tobacco ringspot virus coat protein are obtained by ascites preparation method, the lengths of heavy chain variable region and light chain variable region of this monoclonal antibody are respectively 185 and 121 amino acids; the yield of monoclonal antibody is 500 ~ 5000 mg/l ascites, the purity is 85% ~ 99.5%. The monoclonal antibody of the present invention has a characteristic of specifically recognizing Tobacco ringspot virus coat protein, and it has a broad application prospect in terms of Tobacco ringspot virus entry-exit inspection and quarantine.
Description
TECHNICAL FIELD The present invention relates to a monoclonal antibody, particularly relates to a hybridoma cell strain secreting monoclonal antibody against Tobacco ringspot virus (TRSV) as well as antibody therefrom and antibody preparation method thereof.
BACKGROUND Tobacco ringspot virus (TRSV) is a member of virus Comoviridae, its virion is an icosahedron with equal diameter, the diameter is about 29 nm. TRSV can infect 300 types of crops such as soybean, apple, and tobacco. At present, international quarantine method for TRSV comprises SEM observation, biological method, serological test and molecular biology method. Because TRSV is a spherical virus with a diameter of 29 nm and virus content in the sample is low, it is difficult to be observed and identified under the electron microscope; inoculation and identification of the host require a special isolated greenhouse, and spend a long time, and masking of symptom of the virus tends to affect identification result. The serological method is necessary means for rapid detection of plant virus, and current virus detection at port rely on purchase of imported antiserum, being expensive, but in China there has being no reports on TRSV serum detection kit for imported plant seeding.
The present invention screens and obtains a monoclonal-antibody-secreting cell strain, by using TRSV coat protein as the detection target, via the complete gene fusion expression, isolation and purification of TRSV coat protein, as well as a series of steps such as cross-linked immunity of mouse, cell fusion, antibody activity detection. Sequence of antigen recognition region in antibody gene is obtained by RT-PCR method. Finally, monoclonal antibodies of which the sequence specifically recognizing target antigen being known is obtained a cell strain producing this antibody and corresponding antibody production method. Compared to the method for obtaining monoclonal antibody by immunizing mouse with purified virion, The present invention does not require the active virus sample, and can directly obtain the virus coat protein by the whole gene synthesis and fusion expression method, and the acquisition of antigen is not restricted by the source of carrying virus samples, nor does it violate the operation scope of imported inspection and quarantine objects. The variable region sequence of monoclonal antibody is clear, and does not repeat with the existing antibody sequence, and it has clear and easy to be recognized compared to the antibodies already on the market and related investigated and reported antibodies.
SUMMARY OF THE INVENTION The technical problem to be solved by the present invention is to provide a monoclonal antibody against TRSV, the monoclonal antibody has a reaction specificity that recognizes and binds with TRSV coat protein, and lack of binding specificity to other viruses and plant tissue, and lays a foundation for further research and development of TRSV serum detection kit.
The present invention firstly discloses a monoclonal antibody against TRSV, the sequence of heavy chain variable region of this antibody is as shown in SEQ ID NO:1, the sequence of light chain variable region is as shown in SEQ ID NO:2.
The lengths of the heavy chain variable region and the light chain variable region in this monoclonal antibody are respectively 185 and 121 amino acids.
As a preferred embodiment of the present invention, the nucleotide sequences encoding said heavy chain and light chain variable region are respectively as shown in SEQ ID NO:3 and SEQ ID NO:4.
Said monoclonal antibody is prepared by ascites inducing method, its yield is 500-5000 mg/l, and purity is 85%~99.5%.
The present invention also discloses a hybridoma cell strain secreting monoclonal antibody against TRSV, the hybridoma cell strain is collected at China General Microbiological Culture Collection, and the accession number is: CGMCC20795.
The present invention also discloses application of said monoclonal antibody against TRSV virus in preparation of TRSV detection reagent or kit.
Said monoclonal antibodies against TRSV are prepared by the steps as follows: Finding out the RNA sequence of TRSV coat protein from Genbank (sequence number: KP144328.1), the length of which was 1545bp; The recombinant gene sequence was obtained by sequence optimization and separation tag fusion, as shown in SEQ ID NO: 5, and the corresponding protein sequence was shown in SEQ ID NO: 6.
SEQ ID NO: 5 was inserted into PET28b vector and expressed in the strain of E. coli BL21(DE3). The induced expression conditions were LB liquid medium, with IPTG (Isopropyl- beta-D-thiogalactopyranoside) at 1mM, at 16 °C for 16h, and 200 rpm. The fusion protein TRSV was isolated and purified by Ni-ion affinity chromatography.
Immunizing mice with the fusion protein TRSV,; Preparing hybridoma cells and screening cell strain producing antibody specifically recognizing SEQ ID NO:8 protein; By RT-PCR method, cloning and determining the sequences of heavy chain and light chain variable regions of the monoclonal antibody in the monoclonal antibody cell strain; By using the ascites inducing method, preparing monoclonal antibodies which can recognize SEQ ID NO:6 protein and show positive reaction to the sample carrying TRSV,;
By using ammonium sulphate precipitation and protein G affinity chromatography method, purifying the monoclonal antibodies according to the present invention.
Preparation process of the monoclonal antibodies by ascites inducing method specifically comprises the steps as follows: 8 ~ 15 week old BALB/c mice are injected intraperitoneally with a sterilized paraffin at 0.1 ~ 0.5 ml/mouse; After 5 ~ 10 days, intraperitoneally inoculated with hybridoma cells suspended in PBS at 5x105- 5x 108/mouse; After 5 — 10 days, the ascites is collected 2 ~ 4 times; The ascites is centrifuged at 1000xg for 10 minutes, uppermost adipose tissue is sucked off, cell components and precipitate are removed, and supernatant was collected;\ 3 ml of ascites supernatant is taken, after centrifugation, precipitation, redissolution, and recentrifugation, it is concentrated to 5 ml; The concentrated solution is passed through a protein G purifying resin, eluted with 10 ~ 15 column volumes of pre-eluent, monoclonal antibodies are eluted with 5 ~ 10 column volumes of elution buffer, after concentration, to obtain the monoclonal antibodies of the present invention.
Preferably, the pre-eluant in said step (6) includes 0.1 ~ 0.15 M NaCl and 10 ~ 40 mM Na:HPO,, pH is 7.0; said elution buffer is 0.1 - 0.3 M glycine, and pH is 3.0.
The term “monoclonal antibody” as used in the present invention refers to an antibody obtained from a substantially homogenous cell population, namely individual antibodies included in this population are same, except for a few possible naturally occurring mutations. The monoclonal antibody is directed against a single antigen site with high specificity. The monoclonal antibody according to the present invention specifically recognizes the fusion protein shown in SEQ ID NO:6 derived from TRSV coat protein The present invention has the following beneficial effects: the monoclonal antibody against TRSV according to the present invention underwent antibody titre determination and ELISA, the results indicate that the monoclonal antibody recognizing the fusion protein shown in SEQ ID NO:6 has a reaction specificity with TRSV, and can be used as an antibody for TRSV detection, which can lay a good foundation for subsequent development of TRSV serum detection kit, and serve for work needs of entry-exit inspection and quarantine.
DETAILED DESCRIPTION The present invention is further explained by the following examples.
Example 1 (1) the RNA sequence of TRSV coat protein from Genbank (sequence number: KP144328.1), the length of which was 1545bp; (2) The recombinant gene sequence was obtained by sequence optimization and separation tag fusion, as shown in SEQ ID NO: 5, and the corresponding protein sequence was shown in SEQ ID NO: 6.
(3) SEQ ID NO: 5 was inserted into PET28b vector and expressed in the strain of E. coli BL21(DE3). The induced expression conditions were LB liquid medium, with IPTG (Isopropyl- beta-D-thiogalactopyranoside) at 1mM, at 16°C for 16h, and 200 rpm. The fusion protein TRSV was isolated and purified by Ni-ion affinity chromatography.
{4) Immunization of mice (5) Preparation of hybridoma cells (6) Cloning of hybridoma cells (by limited dilution method) (7) Preparation of monoclonal antibodies by ascites inducing method Example 2 The steps (1)-(6) of Example 2 are same as Example 1.
(7) Preparation of monoclonal antibodies by ascites inducing method 15 week old BALB/c mice were injected intraperitoneally with sterilized paraffin at 0.5 ml/mouse; After 10 days, intraperitoneally inoculated with hybridoma cells suspended in PBS at 5x10%mouse; After 10 days, the ascites was collected 4 times; The ascites was centrifuged at 1000xg for 10 minutes, uppermost adipose tissue was sucked off, then cell components and other precipitate were removed, and supernatant was collected; 3 ml of ascites supernatant was taken, after centrifugation, precipitation, redissolution, and recentrifugation, it was concentrated to 5 ml; the concentrated solution was passed through protein G purifying resin, eluted with 15 column volumes of pre-eluent (00.15 M NaCl, 40 mM Na;HPO., pH 7.0), monoclonal antibodies were eluted with 10 column volumes of elution buffer (0.3 M glycine, pH 3.0), after being concentrated, to obtain the monaclonal antibodies of the present invention, the yield was 500 mg/l ascites, the purity was 87.2%, the Tobacco leaves carrying inactivated TRSV were detected, the detection signal was positive. Reaction of this antibody to Tobacco sample not infected by TRSV was negative, and reactions to Tobacco mosaic virus, Arabis mosaic virus, Bean pod mottle virus etc. were negative.
Example 3 Steps (1) ~ (6) of Example 3 are same as Example 1. Preparation of monoclonal antibodies by ascites inducing method 5 11.5-week old BALB/c mice were taken and injected intraperitoneally with sterilized paraffin at 0.3 ml/mouse; After 7 days, inoculated intraperitoneally with hybridoma cells suspended in PBS at
1.25x108/mouse; After 7 days, ascites was collected 3 times; Ascites was centrifuged at 1000 x g for 10 minutes, the uppermost adipose tissue was sucked off, the cell components and other precipitates were removed, and a supernatant was collected; 3 ml of ascites supernatant was taken, after centrifugation, precipitation, redissolution, recentrifugation, it was concentrated to 5 ml; The concentrated solution was passed through protein G purifying resin, monoclonal antibodies were eluted with 13 column volumes of pre-eluant (0.125 M NaCl, 25 mM Na2HPO,, pH 7.0), and eluted with 7 column volumes of elution buffer (0.2 M glycine, pH 3.0), after being concentrated, the monoclonal antibodies of the present invention were obtained, the yield was 500~5000 mg/l ascites, the purity was 93.5%, the tobacco leaves carrying inactivated TRSV were detected, the detection signal was positive. Reaction of this antibody to tobacco sample not infected by TRSV of was negative, and reactions to Tobacco mosaic virus, T7 bacteriophage, Arabis mosaic virus, and Bean pod mottle virus were negative.
SEQUENCE LISTING <110> China Jiliang University <120> Hybridoma cell strain secreting monoclonal antibody against Tobacco ringspot virus as well as antibody and antibody preparation method thereof <130> BJS - Hybridoma NL <160> © <170> PatentIn version 3.5 <210> 1 <211> 185 <212> PRT <213> Artificial Sequence <220> <223> Heavy chain variable region of a monoclonal antibody against TRSV <400> 1 Met Val Gln Leu Gln Gln Ser Gly Thr Val Leu Leu Ala Arg Pro Gly 1 5 10 15 Ala Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Ser Phe Gly Thr
Ser Tyr Trp Met His Trp Val Lys Gln Arg Pro Gly Gly Gln Gly Leu 40 45 Glu Trp Ile Gly Ala Ile Tyr Pro Gly Lys Asn Ser Asp Thr Asn Tyr 50 55 60 Asn Gln Lys Phe Lys Gly Lys Ala Lys Leu Thr Ala Val Thr Ser Ala 65 70 75 80 Ser Thr Ala Tyr Met Glu Leu Ser Ser Leu Thr Asn Glu Asp Ser Ala 85 90 95 Val Tyr Tyr Cys Thr Arg Leu Ser Met Leu Gly Arg Ser Tyr Tyr Phe 100 105 110 Asp Tyr Trp Gly Gln Gly Thr Thr Leu Thr Val Ser Ser Ala Lys Ala 115 120 125 Thr Pro Pro Ser Val Tyr Pro Leu Ala Pro Gly Cys Gly Asp Thr Thr 130 135 140 Gly Ser Ser Val Thr Leu Gly Cys Leu Val Lys Gly Tyr Phe Pro Glu 145 150 155 160
Ser Val Thr Val Thr Trp Asn Ser Gly Ser Leu Ser Ser Ser Val His 165 170 175 Thr Phe Pro Asp Ser Cys Ser Phe Thr 180 185 <210> 2 <211> 121 <212> PRT <213> Artificial Sequence <220> <223> Light chain variable region of a monoclonal antibody against TRSV <400> 2 Met Ala Cys Arg Pro Ser Ile Val Leu Tyr Thr Gln Ser Pro Ser Ser 1 5 10 15 Leu Ala Met Ser Val Gly Gln Arg Tyr Val Thr Met Ser Cys Lys Ser
Ser Gln Ser Leu Leu Asn Ser Ser Asn Gln Lys Asn Tyr Cys Leu Ala 40 45 Trp Cys Gln Gln Arg Pro Gly Gln Ser Pro Lys Leu Leu Glu Ser Gly 50 55 60 Val Pro Asp Arg Phe Ile Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu 65 70 75 80 Thr Ile Ser Ser Val Gln Ala Glu Asp Leu Ala Asp Tyr Phe Cys Gln 85 90 95 Leu His Tyr Ser Thr Pro His Val Arg Cys Trp Glu Gln Ala Gly Asp 100 105 110 Pro Thr Lys Leu Val Arg Ala Thr Arg 115 120 <210> 3 <211> 555 <212> DNA <213> Artificial Sequence <220> <223> Nucleotide sequence encoding the heavy chain variable region of a monoclonal antibody against TRSV <400> 3 atggtacaac tgcaacaatc tggtaccgtt ctgctggcac gtcctggtgc atccgtgaaa 60 atgagctgca aagcaagcgg ctactccttc ggtactagct actggatgca ctgggttaag 120 cagcgtccgg gtggccaggg tctggaatgg atcggtgcaa tctatccggg caaaaatagc 180 gacacgaact acaatcagaa attcaaaggc aaggctaaac tgaccgcggt aacctccgcc 240 tctactgcat acatggagct gtccagcctg accaatgaag attccgcggt ttactattgc 300 acccgcctgt ctatgctggg tcgtagctac tattttgact attggggcca aggtaccacc 360 ctgaccgttt ctagcgctaa agctacgcca ccgtccgtgt atccgctggc tccaggttgt 420 ggtgatacca cgggttctag cgttaccctg ggttgcctgg ttaaaggcta cttcccagag 480 agcgttacgg tcacctggaa ttccggtagc ctgtccagct ccgtgcatac cttcccagat 540 agctgctcct tcacg 555 <210> 4 <211> 363 <212> DNA <213> Artificial Sequence <220> <223> Nucleotide sequence encoding the light chain variable region of a monoclonal antibody against TRSV <400> 4 atggcgtgtc gcccttcgat tgtgctgtat actcaatctc catcctccct ggctatgtca 60 gtaggacaga ggtatgtcac tatgagctgc aagtccagtc agagcctttt aaatagtagc 120 aatcaaaaga actattgctt ggcctggtgc cagcagagac caggacagtc tcctaaactt 180 ctggaatctg gggtccctga tcgcttcata ggcagtggat ctgggacaga tttcactctt 240 accatcagca gtgtgcaggc tgaagacctg gcagattact tctgtcagct acattatagc 300 actcctcacg ttcggtgctg ggaacaagct ggagatccaa cgaagcttgt aagggcgaca 360 cgc 363 <210> 5 <211> 1572 <212> DNA <213> Artificial Sequence <220> <223> Recombinant gene sequence of TRSV coat protein (Genbank KP144328.1) <400> 5 atggccgctg tgacggttgt tcccgatccc acttgttgtg ggacattgtc ctttaaggtt 60 cccaaagatg cgaagaaagg aaagcatctt ggaacttttg acattcggca agccattatg 120 gaatatggtg gtttgcattc ccaagaatgg tgtgcaaagg gcattgttaa tcccactttt 180 acagtgagga tgcatgcccc acgcaacgcc tttgcaggtt tgtctatagc gtgcaccttt 240 gatgattaca aacgcataga cttaccagcg cttgggaatg aatgtcctcc ctccgagatg 300 tttgaactgc ctaccaaggt tttcatgctt aaagatgcag atgtgcatga atggcagttc 360 aactatgggg aacttacagg acatgggttg tgcaattggg caaatgtagt tacccagccc 420 acattgtact tttttgttgc gtccacaaat caagtgacga tggctgctga ttggcagtgt 480 attgttacta tgcatgtgga catggggccc gtcattgatc gttttgagtt agatccaact 540 atgacgtggc ctattcaatt gggtgacact ttcgccattg atagatatta tgaggcgaaa 600 gaaattaaac ttgacgggtc aacctccatg ttgtctatat cttataattt tggaggtccc 660 gtcaagcatt ctaagaaaca tgccatttca tattcccggg cagttatgtc taggaatctt 720 gggtggtctg gcactataag cggaagtgtc aagagtgttt cttctttatt ttgtaccgct 780 tettttgtta tttttccatg ggaacacgaa gcacctccaa ccttacgtca ggtgttatgg 840 ggcccacatc agataatgca cggagatggc caatttgaaa ttgctatcaa aactcgtctt 900 cattcagctg ctacaactga agaagggttt ggtagacttg gtatactccc gctttctggg 960 cctatagctc ctgatgcaca tgttggatcg tacgagttta ttgtacatat agacacttgg 1020 cgacccgact ctcaggtgca tcctcccatg ttttctagtg cggagcttta taattggttc 1080 actttaacca atttgaaacc agatgcgaac actggcgtag tcaactttga tattcccgga 1140 tacatccatg acttcgcctc taaggacgca actgtgacgc tcgcatcaaa tcccctctct 1200 tggcttgtcg cagctactgg ctggcattat ggtgaggtgg atctctgcat ctcctggtca 1260 aggtccaaac aggcccaggc tcaggagggt agtgtttcca ttaccactaa ttatagagat 1320 tggggtgctt actggcaagg ccaggcccgg atttatgatt tgcggcgtac tgaagcggaa 1380 attcccatct tcttgggttc ttacgctggt gcgacgccat ctggtgcctt gggtaagcaa 1440 aactatgtcc ggatttcaat tgtcaatgct aaggacatag ttgcactgcg agtgtgtttg 1500 cgacccaaat ctataaagtt ctggggtcgc tccgccactt tgtttctcga gcaccaccac 1560 caccaccact ga 1572 <210> © <211> 523 <212> PRT <213> Artificial Sequence <220> <223> Recombinant protein sequence derived from TRSV coat protein (Genbank KP144328.1) <400> © Met Ala Ala Val Thr Val Val Pro Asp Pro Thr Cys Cys Gly Thr Leu 1 5 10 15
Ser Phe Lys Val Pro Lys Asp Ala Lys Lys Gly Lys His Leu Gly Thr
Phe Asp Ile Arg Gln Ala Ile Met Glu Tyr Gly Gly Leu His Ser Gln 40 45 Glu Trp Cys Ala Lys Gly Ile Val Asn Pro Thr Phe Thr Val Arg Met 50 55 60 His Ala Pro Arg Asn Ala Phe Ala Gly Leu Ser Ile Ala Cys Thr Phe 65 70 75 80 Asp Asp Tyr Lys Arg Ile Asp Leu Pro Ala Leu Gly Asn Glu Cys Pro 85 90 95 Pro Ser Glu Met Phe Glu Leu Pro Thr Lys Val Phe Met Leu Lys Asp 100 105 110 Ala Asp Val His Glu Trp Gln Phe Asn Tyr Gly Glu Leu Thr Gly His 115 120 125 Gly Leu Cys Asn Trp Ala Asn Val Val Thr Gln Pro Thr Leu Tyr Phe 130 135 140 Phe Val Ala Ser Thr Asn Gln Val Thr Met Ala Ala Asp Trp Gln Cys 145 150 155 160 Ile Val Thr Met His Val Asp Met Gly Pro Val Ile Asp Arg Phe Glu 165 170 175 Leu Asp Pro Thr Met Thr Trp Pro Ile Gln Leu Gly Asp Thr Phe Ala 180 185 190 Ile Asp Arg Tyr Tyr Glu Ala Lys Glu Ile Lys Leu Asp Gly Ser Thr 195 200 205 Ser Met Leu Ser Ile Ser Tyr Asn Phe Gly Gly Pro Val Lys His Ser 210 215 220 Lys Lys His Ala Ile Ser Tyr Ser Arg Ala Val Met Ser Arg Asn Leu 225 230 235 240 Gly Trp Ser Gly Thr Ile Ser Gly Ser Val Lys Ser Val Ser Ser Leu 245 250 255
Phe Cys Thr Ala Ser Phe Val Ile Phe Pro Trp Glu His Glu Ala Pro 260 265 270 Pro Thr Leu Arg Gln Val Leu Trp Gly Pro His Gln Ile Met His Gly 275 280 285 Asp Gly Gln Phe Glu Ile Ala Ile Lys Thr Arg Leu His Ser Ala Ala 290 295 300 Thr Thr Glu Glu Gly Phe Gly Arg Leu Gly Ile Leu Pro Leu Ser Gly 305 310 315 320 Pro Ile Ala Pro Asp Ala His Val Gly Ser Tyr Glu Phe Ile Val His 325 330 335 Ile Asp Thr Trp Arg Pro Asp Ser Gln Val His Pro Pro Met Phe Ser 340 345 350 Ser Ala Glu Leu Tyr Asn Trp Phe Thr Leu Thr Asn Leu Lys Pro Asp 355 360 365 Ala Asn Thr Gly Val Val Asn Phe Asp Ile Pro Gly Tyr Ile His Asp 370 375 380 Phe Ala Ser Lys Asp Ala Thr Val Thr Leu Ala Ser Asn Pro Leu Ser 385 390 395 400 Trp Leu Val Ala Ala Thr Gly Trp His Tyr Gly Glu Val Asp Leu Cys 405 410 415 Ile Ser Trp Ser Arg Ser Lys Gln Ala Gln Ala Gln Glu Gly Ser Val 420 425 430 Ser Ile Thr Thr Asn Tyr Arg Asp Trp Gly Ala Tyr Trp Gln Gly Gln 435 440 445 Ala Arg Ile Tyr Asp Leu Arg Arg Thr Glu Ala Glu Ile Pro Ile Phe 450 455 460 Leu Gly Ser Tyr Ala Gly Ala Thr Pro Ser Gly Ala Leu Gly Lys Gln 465 470 475 480 Asn Tyr Val Arg Ile Ser Ile Val Asn Ala Lys Asp Ile Val Ala Leu 485 490 495 Arg Val Cys Leu Arg Pro Lys Ser Ile Lys Phe Trp Gly Arg Ser Ala 500 505 510
Thr Leu Phe Leu Glu His His His His His His 515 520
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| Title |
|---|
| ANONYMOUS: "PM 7/2 (2) Tobacco ringspot virus", PO BULLETIN: A JOURNAL OF REGULATORY PLANT PROTECTION, vol. 47, no. 2, 29 May 2017 (2017-05-29), GB, pages 135 - 145, XP055823749, ISSN: 0250-8052, Retrieved from the Internet <URL:https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fepp.12376> DOI: 10.1111/epp.12376 * |
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