CN111100201B - Murine monoclonal antibody against envelope protein of Zika virus - Google Patents
Murine monoclonal antibody against envelope protein of Zika virus Download PDFInfo
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- CN111100201B CN111100201B CN201911415795.1A CN201911415795A CN111100201B CN 111100201 B CN111100201 B CN 111100201B CN 201911415795 A CN201911415795 A CN 201911415795A CN 111100201 B CN111100201 B CN 111100201B
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- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
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- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Abstract
The invention discloses a mouse-derived monoclonal antibody aiming at envelope protein of Zika virus, which has good specificity, strong neutralizing activity and increased aggregation resistance after screening and gene modification, and is suitable for preventing and treating Zika virus.
Description
Technical Field
The invention relates to the technical field of biology, in particular to a murine monoclonal antibody aiming at envelope proteins of Zika viruses.
Background
Zika virus (ZIKV) is a flaviviridae virus that, when infected, can cause microcephaly in newborns and affect neurological development in infants and adults who may develop Guillain Barre Syndrome (GBS) after infection causing neurological damage. At present, no licensed vaccine or specific medicine exists, and the mouse is immunized by using the self-constructed envelope protein of the Zika virus to obtain the murine monoclonal antibody with stronger neutralizing activity, so that the murine monoclonal antibody can be applied to the prevention and treatment of the Zika virus in the future.
Disclosure of Invention
The invention aims to fill the blank of the prior art and provide a mouse-derived monoclonal antibody aiming at envelope protein of Zika virus with good specificity.
In order to achieve the aim, the invention provides a murine monoclonal antibody aiming at envelope proteins of the Zika virus, wherein the light chain sequence of the murine monoclonal antibody is shown as SEQ No.1, and the heavy chain sequence of the murine monoclonal antibody is shown as SEQ No. 3.
The base sequence corresponding to the murine monoclonal antibody directed against the envelope protein of Zika virus is shown in SEQ No.4 for the light chain sequence and SEQ No.5 for the heavy chain sequence.
On the basis of the research of the Chinese patent application 201811613477.1, the inventor of the application screens and further modifies the gene by using the method for constructing the phage library to obtain the mouse-derived monoclonal antibody with better effect.
The invention has the beneficial effects that: after screening and gene modification, the obtained antibody has good specificity, strong neutralizing activity and enhanced aggregation resistance, and is suitable for preventing and treating Zika virus.
Drawings
FIG. 1-1 shows the region of easy aggregation of the amino acid sequence of D10 predicted by Tango software.
FIGS. 1-2 show the regions of susceptibility to aggregation of the amino acid sequence of D11 predicted by Tango software.
FIGS. 1-3 are graphs comparing the heavy chain mutation regions of D10 and D11.
FIG. 2 shows SDS-PAGE detection of D11 antibody.
FIG. 3 is a graph showing the binding of the antibody D11 to the envelope protein of Zika virus by ELISA analysis.
FIG. 4 is a graph showing the neutralizing activity of the D11 antibody against Zika virus.
Detailed Description
The invention is described in further detail below with reference to the figures and specific embodiments. The following examples are carried out on the premise of the technical scheme of the invention, and detailed embodiments and specific operation procedures are given, but the scope of the invention is not limited to the following examples.
Example 1: obtaining of D10 antibody sequence
Based on a constructed immune mouse Fab phage display library (the method for obtaining the library is from fusion protein of flaviviridae virus envelope protein disclosed in Chinese patent application 201811613477.1, and a preparation method and application thereof, the fusion protein is used as immunogen to immunize a mouse to obtain cDNA of the mouse, and the cDNA is used as a construction material of the phage display library), three rounds of screening are carried out, a monoclonal phage ELISA is used for sequencing positive clones in the mouse, a base sequence of a D10 candidate clone is obtained, an amino acid sequence of the D10 candidate clone is obtained through amino acid translation software, a light chain amino acid sequence is shown as SEQ No.1, and a heavy chain amino acid sequence is shown as SEQ No. 2.
Example 2: optimization of the obtained D10 amino acid sequence by using Tango software
The amino acid sequence of the D10 candidate clone is subjected to aggregation region prediction by utilizing Tango software (http:// Tango. crg. es /), and a strong aggregation region exists in the D10 candidate clone, as shown in a figure 1-1, so that point mutation is carried out on the region to obtain the D11 antibody, wherein the amino acid sequence of a light chain is shown as SEQ No.1, the amino acid sequence of a heavy chain is shown as SEQ No.3, the corresponding base sequence is shown as the light chain, and the heavy chain is shown as SEQ No.4, and the heavy chain is shown as SEQ No. 5. The mutated amino acid sequence was re-predicted by Tango software, and the aggregation-prone region was found to be significantly improved, as shown in FIGS. 1-2, 1-3.
Example 3: 293F cells express the D11 antibody and are detected by SDS-PAGE
Cloning the mutated base sequence to a double-start vector pVitro2-neo-mcs (InvivoGen), transfecting 293F cells by using PEI, expressing proteins, expressing for 5-7 days, purifying the culture supernatant of the 293F cells by Protein A (GE), and concentrating and replacing the purified proteins to obtain the D11 antibody dissolved in PBS buffer. SDS-PAGE electrophoresis detected it was found to present both light and heavy chains as shown in FIG. 2.
Example 4: ELISA analysis of binding of D11 antibody to Zika Virus envelope protein
Envelope proteins of Zika virus were coated on ELISA plates, using the D11 antibody as a primary antibody after gradient dilution and HRP-labeled Goat-anti-mouse IgG (Abcam) as a secondary antibody, and after color development, EC50 was calculated from the change in signal intensity, at about 200nM, as shown in FIG. 3.
Example 5: neutralization experiment of Zika virus of D11 antibody.
The antibody D11 was diluted in a gradient and incubated with 100PFU of Zika virus for 1h at 37 ℃ separately, the mixture was added to a 24-well plate plated one day ahead with Vero cells, incubated for 1h at 37 ℃, the virus mixture was discarded, and the supernatant (2% hydroxymethyl cellulose in DMDM, containing 2% serum) was added and the incubation continued for 2-3 days. After formation of distinct viral plaques, the upper cover was discarded and fixed by addition of 3.7% formaldehyde solution, followed by staining of the plaques with 1% concentration of crystal violet and calculation of the IC50 value, approximately 100nM, based on the reduction in viral plaques at different antibody concentrations, as shown in FIG. 4.
SEQUENCE LISTING
<110> Wuhan Spanish Biotechnology Ltd
<120> murine monoclonal antibody against envelope protein of Zika virus
<130> 2019004
<160> 5
<170> PatentIn version 3.5
<210> 1
<211> 215
<212> PRT
<213> light chain (Artificial Sequence)
<400> 1
Asp Ala Val Val Thr Gln Glu Ser Ala Leu Thr Thr Ser Pro Gly Glu
1 5 10 15
Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser
20 25 30
Asn Tyr Ala Asn Trp Val Gln Glu Lys Pro Asp His Leu Phe Thr Gly
35 40 45
Leu Ile Gly Gly Thr Asn Asn Arg Ala Pro Gly Val Pro Ala Arg Phe
50 55 60
Ser Gly Ser Leu Ile Gly Asp Lys Ala Ala Leu Thr Ile Thr Gly Ala
65 70 75 80
Gln Thr Glu Asp Glu Ala Ile Tyr Phe Cys Ala Leu Trp Tyr Ser Asn
85 90 95
His Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gln Pro
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Lys Ser Ser Pro Ser Val Thr Leu Phe Pro Pro Ser Ser Glu Glu Leu
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Glu Thr Asn Lys Ala Thr Leu Val Cys Thr Ile Thr Asp Phe Tyr Pro
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Gly Val Val Thr Val Asp Trp Lys Val Asp Gly Thr Pro Val Thr Gln
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Gly Met Glu Thr Thr Gln Pro Ser Lys Gln Ser Asn Asn Lys Tyr Met
165 170 175
Ala Ser Ser Tyr Leu Thr Leu Thr Ala Arg Ala Trp Glu Arg His Ser
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Ser Tyr Ser Cys Gln Val Thr His Glu Gly His Thr Val Glu Lys Ser
195 200 205
Leu Ser Arg Ala Asp Cys Ser
210 215
<210> 2
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Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu
1 5 10 15
Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp Tyr
20 25 30
Ser Met His Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Met Trp Met
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Gly Trp Ile Asn Pro Glu Thr Gly Glu Pro Thr Tyr Ala Asp Asp Phe
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Thr Gly Arg Phe Ala Phe Val Val Glu Thr Ser Ala Ser Thr Ala Tyr
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Leu Lys Ile Asn Ser Leu Arg Asn Glu Asp Thr Ala Thr Tyr Phe Cys
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Gly Arg Gly Gly Asp Asp Tyr Ser Ile Asp Tyr Trp Gly Gln Gly Thr
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Ser Val Thr Val Ser Ser Ala Lys Thr Thr Pro Pro Ser Val Tyr Pro
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Leu Ala Pro Gly Ser Ala Ala Gln Thr Asn Ser Met Val Thr Leu Gly
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Cys Leu Val Lys Gly Tyr Phe Pro Glu Pro Val Thr Val Thr Trp Asn
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Ser Gly Ser Leu Ser Ser Gly Val His Thr Phe Pro Ala Val Leu Gln
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Ser Asp Leu Tyr Thr Leu Ser Ser Ser Val Thr Val Pro Ser Ser Thr
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Trp Pro Ser Glu Thr Val Thr Cys Asn Val Ala His Pro Ala Ser Ser
195 200 205
Thr Thr Val Asp Lys Lys Leu Glu Pro Arg Gly Pro Thr Ile Lys Pro
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Cys Pro Pro Cys Lys Cys Pro Ala Pro Asn Leu Leu Gly Gly Pro Ser
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Val Phe Ile Phe Pro Pro Lys Ile Lys Asp Val Leu Met Ile Ser Leu
245 250 255
Ser Pro Ile Val Thr Cys Val Val Val Asp Val Ser Glu Asp Asp Pro
260 265 270
Asp Val Gln Ile Ser Trp Phe Val Asn Asn Val Glu Val His Thr Ala
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Gln Thr Gln Thr His Arg Glu Asp Tyr Asn Ser Thr Leu Arg Val Val
290 295 300
Ser Ala Leu Pro Ile Gln His Gln Asp Trp Met Ser Gly Lys Glu Phe
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Lys Cys Lys Val Asn Asn Lys Asp Leu Pro Ala Pro Ile Glu Arg Thr
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Ile Ser Lys Pro Lys Gly Ser Val Arg Ala Pro Gln Val Tyr Val Leu
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Pro Pro Pro Glu Glu Glu Met Thr Lys Lys Gln Val Thr Leu Thr Cys
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Met Val Thr Asp Phe Met Pro Glu Asp Ile Tyr Val Glu Trp Thr Asn
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Asn Gly Lys Thr Glu Leu Asn Tyr Lys Asn Thr Glu Pro Val Leu Asp
385 390 395 400
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Asn Trp Val Glu Arg Asn Ser Tyr Ser Cys Ser Val Val His Glu Gly
420 425 430
Leu His Asn His His Thr Thr Lys Ser Phe Ser Arg Thr Pro
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<210> 3
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<213> D11 heavy chain (Artificial Sequence)
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Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu
1 5 10 15
Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Asp Tyr
20 25 30
Ser Met His Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Met Trp Met
35 40 45
Gly Trp Ile Asn Pro Glu Thr Gly Glu Pro Thr Tyr Ala Asp Asp Phe
50 55 60
Thr Gly Arg Phe Ala Phe Ser Leu Glu Thr Ser Ala Ser Thr Ala Tyr
65 70 75 80
Leu Lys Ile Asn Ser Leu Arg Asn Glu Asp Thr Ala Thr Tyr Phe Cys
85 90 95
Gly Arg Gly Gly Asp Asp Tyr Ser Ile Asp Tyr Trp Gly Gln Gly Thr
100 105 110
Ser Val Thr Val Ser Ser Ala Lys Thr Thr Pro Pro Ser Val Tyr Pro
115 120 125
Leu Ala Pro Gly Ser Ala Ala Gln Thr Asn Ser Met Val Thr Leu Gly
130 135 140
Cys Leu Val Lys Gly Tyr Phe Pro Glu Pro Val Thr Val Thr Trp Asn
145 150 155 160
Ser Gly Ser Leu Ser Ser Gly Val His Thr Phe Pro Ala Val Leu Gln
165 170 175
Ser Asp Leu Tyr Thr Leu Ser Ser Ser Val Thr Val Pro Ser Ser Thr
180 185 190
Trp Pro Ser Glu Thr Val Thr Cys Asn Val Ala His Pro Ala Ser Ser
195 200 205
Thr Thr Val Asp Lys Lys Leu Glu Pro Arg Gly Pro Thr Ile Lys Pro
210 215 220
Cys Pro Pro Cys Lys Cys Pro Ala Pro Asn Leu Leu Gly Gly Pro Ser
225 230 235 240
Val Phe Ile Phe Pro Pro Lys Ile Lys Asp Val Leu Met Ile Ser Leu
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Ser Pro Ile Val Thr Cys Val Val Val Asp Val Ser Glu Asp Asp Pro
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Asp Val Gln Ile Ser Trp Phe Val Asn Asn Val Glu Val His Thr Ala
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Gln Thr Gln Thr His Arg Glu Asp Tyr Asn Ser Thr Leu Arg Val Val
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Ser Ala Leu Pro Ile Gln His Gln Asp Trp Met Ser Gly Lys Glu Phe
305 310 315 320
Lys Cys Lys Val Asn Asn Lys Asp Leu Pro Ala Pro Ile Glu Arg Thr
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Ile Ser Lys Pro Lys Gly Ser Val Arg Ala Pro Gln Val Tyr Val Leu
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Pro Pro Pro Glu Glu Glu Met Thr Lys Lys Gln Val Thr Leu Thr Cys
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Met Val Thr Asp Phe Met Pro Glu Asp Ile Tyr Val Glu Trp Thr Asn
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Asn Gly Lys Thr Glu Leu Asn Tyr Lys Asn Thr Glu Pro Val Leu Asp
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Ser Asp Gly Ser Tyr Phe Met Tyr Ser Lys Leu Arg Val Glu Lys Lys
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Asn Trp Val Glu Arg Asn Ser Tyr Ser Cys Ser Val Val His Glu Gly
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<213> light chain (Artificial Sequence)
<400> 4
gacgctgttg tgactcagga atctgcactc accacatcac ctggtgaaac agtcacactc 60
acttgtcgct caagtactgg ggctgttaca actagtaact atgccaactg ggtccaagaa 120
aaaccagatc atttattcac tggtctaata ggtggtacca acaaccgagc tccaggtgtt 180
cctgccagat tctcaggctc cctgattgga gacaaggctg ccctcaccat cacaggggca 240
cagactgagg atgaggcaat atatttctgt gctctatggt acagcaacca ttgggtgttc 300
ggtggaggaa ccaaactgac tgtcctaggc cagcccaagt cttcgccatc agtcaccctg 360
tttccacctt cctctgaaga gctcgagact aacaaggcca cactagtgtg tacgatcact 420
gatttctacc caggtgtggt gacagtggac tggaaggtag atggtacccc tgtcactcag 480
ggtatggaga caacccagcc ttccaaacag agcaacaaca agtacatggc tagcagctac 540
ctgaccctga cagcaagagc atgggaaagg catagcagtt acagctgcca ggtcactcat 600
gaaggtcaca ctgtggagaa gagtttgtcc cgtgctgact gttcc 645
<210> 5
<211> 1338
<212> DNA
<213> D11 heavy chain (Artificial Sequence)
<400> 5
cagatccagt tggtgcagtc tggacctgag ctgaagaagc ctggagagac agtcaagatc 60
tcctgcaagg cttctggtta taccttcaca gactattcaa tgcactgggt gaagcaggct 120
ccaggaaagg gtttaatgtg gatgggctgg ataaaccctg agactggtga gccaacatat 180
gcagatgact tcacgggacg gtttgccttc tctttggaaa cctctgccag cactgcctac 240
ttaaagatca acagcctcag aaatgaggac acggctacat atttttgtgg tagagggggc 300
gacgactatt ctattgacta ctggggtcaa ggaacctcag tcaccgtctc ctcagccaaa 360
acgacacccc catctgtcta tccactggcc cctggatctg ctgcccaaac taactccatg 420
gtgaccctgg gatgcctggt caagggctat ttccctgagc cagtgacagt gacctggaac 480
tctggatccc tgtccagcgg tgtgcacacc ttcccagctg tcctgcagtc tgacctctac 540
actctgagca gctcagtgac tgtcccctcc agcacctggc ccagcgagac cgtcacctgc 600
aacgttgccc acccggccag cagcaccacg gtggacaaaa aacttgagcc cagagggccc 660
acaatcaagc cctgtcctcc atgcaaatgc ccagcaccta acctcttggg tggaccatcc 720
gtcttcatct tccctccaaa gatcaaggat gtactcatga tctccctgag ccccatagtc 780
acatgtgtgg tggtggatgt gagcgaggat gacccagatg tccagatcag ctggtttgtg 840
aacaacgtgg aagtacacac agctcagaca caaacccata gagaggatta caacagtact 900
ctccgggtgg tcagtgccct ccccatccag caccaggact ggatgagtgg caaggagttc 960
aaatgcaagg tcaacaacaa agacctccca gcgcccatcg agagaaccat ctcaaaaccc 1020
aaagggtcag taagagctcc acaggtatat gtcttgcctc caccagaaga agagatgact 1080
aagaaacagg tcactctgac ctgcatggtc acagacttca tgcctgaaga catttacgtg 1140
gagtggacca acaacgggaa aacagagcta aactacaaga acactgaacc agtcctggac 1200
tctgatggtt cttacttcat gtacagcaag ctgagagtgg aaaagaagaa ctgggtggaa 1260
agaaatagct actcctgttc agtggtccac gagggtctgc acaatcacca cacgactaag 1320
agcttctccc ggactccg 1338
Claims (2)
1. A murine monoclonal antibody directed against envelope protein of Zika virus is characterized in that the light chain sequence is shown in SEQ No.1, and the heavy chain sequence is shown in SEQ No. 3.
2. The murine monoclonal antibody to envelope protein of Zika virus according to claim 1, wherein the coding nucleotide sequence of the light chain is represented by SEQ No.4 and the coding nucleotide sequence of the heavy chain is represented by SEQ No. 5.
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| WO2018010789A1 (en) * | 2016-07-13 | 2018-01-18 | Humabs Biomed Sa | Novel antibodies specifically binding to zika virus epitopes and uses thereof |
| TW201815821A (en) * | 2016-07-18 | 2018-05-01 | 美商再生元醫藥公司 | Anti-zika virus antibodies and methods of use |
| CN110172095B (en) * | 2016-08-10 | 2020-09-04 | 中国科学院微生物研究所 | Humanized monoclonal antibody of Zika virus with high neutralization activity and application thereof |
| JP2020500007A (en) * | 2016-10-13 | 2020-01-09 | マサチューセッツ インスティテュート オブ テクノロジー | Antibodies that bind to Zika virus envelope proteins and uses thereof |
| KR102071539B1 (en) * | 2016-11-18 | 2020-02-03 | 재단법인 바이오나노헬스가드연구단 | A Method of Detecting Anti-Zika Virus Antibodies Using Monoclonal Antibody Specific to the Zika Envelope and Non-Structural Protein 1 and Rapid Diagnostic Kit for Detecting Anti-Zika Virus Antibodies |
| CN109081868B (en) * | 2017-06-14 | 2022-06-24 | 中国科学院上海巴斯德研究所 | Monoclonal antibody targeting Zika virus envelope protein conserved epitope and application thereof |
| CN109705222A (en) * | 2018-12-27 | 2019-05-03 | 中国科学院武汉病毒研究所 | The fusion protein and the preparation method and application thereof of flaviviridae envelope protein |
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