KR20220046436A - A polypeptide product - Google Patents

Abstract

In the present invention, a research on the CoVid-19 virus structural protein is conducted with the aim of activating an MHC-I immune system based on an AI-deep-learning technology research. Based on the prediction of an immune system through the AI technology, a polypeptide sequence of 9-14 amino acids in length is constructed, and the polypeptide can significantly activate the immune system of the human body, thereby providing the foundation of a safe and effective peptide vaccine design.

Description

Polypeptide formulation {A POLYPEPTIDE PRODUCT}

FIELD OF THE INVENTION The present invention relates to biological products, and more particularly to polypeptide preparations.

In immune mechanisms, primordial T-cells must receive two independent pieces of information from antigen presenting cells (APCs). The first information is antigen specificity, wherein an antigen receptor on the T-cell meets the appropriate antigen-MHC complex on the APC, and antigen-independent information 2 binds to the APC-expressing ligand via a T-cell costimulating molecule. do. Antigen independence information 2 can be positive stimulation or negative stimulation, i.e. result in an antigen-specific non-reactive state or result in the natural death of T-cells.

Data from extensive studies of acute and chronic infectious diseases have provided negative costimulatory receptors, and important roles in transmission control. Memory CD8 T-cells generated after infection with an acute virus are highly functional and important components of protective immunity. There are already studies demonstrating its effectiveness in optimizing viral immunity.

Chronic infectious diseases are usually characterized by functional impairment depending on the extent to which virus-specific T-cells respond, and this defect is also a major cause of the host's inability to clear persistent pathogens. In the early stages of infection, effector T-cells are first generated, but due to continuous exposure to exogenous antigens, they gradually lose their function in the course of chronic infection, which leads to T-cell exhaustion. .

T-cell exhaustion can be reversed through blockade of the co-suppression pathway, and the therapeutic potential of co-suppression blockade to treat viral infections has already been extensively studied through blockade of the PD-1/PD-L1 pathway. It has been shown to be effective in some animal models of infection.

In addition to blocking co-inhibition pathways to treat chronic infections, studies using current viral infection models have already highlighted the importance of positive costimulatory information in the memory process for viruses. Costimulatory molecules such as CD28, 4-1BB, and OX40 are also already involved in the survival, generation, maintenance and quality of virus-specific memory CD8+ T-cells. Transmission of costimulatory information may help to increase the production and function of virus-specific memory CD8+ T-cells.

CorVid-19 is an RNA-virus, and the total genome sequence length is 29,903, and it is estimated that there are a total of 10 putative proteins (CDS, Coding Sequence) created by CorVid-19.

Proteins produced by CoVid-19 are substances that make up viral particles (mainly proteins or glycoproteins, etc.), so theoretically, they can be detected by the immune system of a healthy human body and have a high probability of spontaneous healing.

However, since CoVid-19 is a relatively novel strain, it takes more time for our immune system to recognize and respond to CoVid-19, and if it develops into a serious infection or disease state before the immune system can work, it can have fatal consequences. may cause

As we humans have already experienced many times, if we can quickly and easily produce a "vaccine" for CoVid-19, we can prevent the crisis the world currently faces due to the contagious/lethality/fear of CoVid-19. There will be.

Although we do not yet fully understand the human immune system, these known facts show that some of the proteins produced by "foreign agents (germs or viruses)" Because they can be identified, an “immune defense mechanism” can be manufactured.

Based on this understanding and research, our researchers studied the MHC-I activated immune system through the means of AI-Deep-Learning technology. Studying polypeptides and applying them to the diagnosis and treatment of viruses has important meaning.

Based on the AI-Deep-Learning technology research, our researchers conducted a study on the CoVid-19 virus structural protein with the goal of activating the MHC-I immune system, and found a total of 10 proteins. Based on the prediction of the immune system through AI technology, a total of 37 polypeptide sequences with a length of 9-14 amino acids (see Table 1) were constructed. The polypeptide can significantly activate the immune system of an organism as follows.

Therefore, the technical problem to be solved by the present invention is to provide a polypeptide preparation capable of remarkably activating the immune system against the CoVid-19 virus.

The present invention provides a polypeptide having an immune activating action in a first aspect, wherein the amino acid sequence code of the polypeptide is SEQ ID NO:1-37 (see Table 1) or at least 95% sequence identity with the amino acid sequence thereof It is one or more types of derived polypeptides having a sex.

In addition, the amino acid sequence code of the polypeptide is SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:33, or one or more of the derived polypeptides having at least 95% sequence identity with such an amino acid sequence.

The present invention provides a virus therapeutic composition in a second aspect, wherein the composition has the amino acid sequence code of SEQ ID NO:1-37 (see Table 1) or a derived polynucleotide having at least 95% sequence identity with the amino acid sequence and at least one of peptides. The derived polypeptide may have the same or similar immune activating action as the corresponding polypeptide in SEQ ID NOs: 1-37, and it is preferable that the amino acid sequence of the derived polypeptide reaches 98% to 99%.

In addition, the virus therapeutic composition is SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:18 ID NO: 33 or at least 95% sequence identity with such an amino acid sequence. The derived polypeptide has the corresponding SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:18 It may have the same or similar immune activating action as the polypeptide of ID NO:33, and it is preferable that the amino acid sequence of the derived polypeptide reaches 98% to 99%.

In a third aspect, the present invention provides a vector (eg, a plasmid and a recombinant viral vector), and a host cell comprising the vector, wherein the amino acid sequence code for expression thereof is SEQ ID NO:1-37 (see Table 1) or or one or more of a derived polypeptide having at least 95% sequence identity with the amino acid sequence thereof, and the preferred expression code is SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, one or more of SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:33 or a derived polypeptide having at least 95% sequence identity with such an amino acid sequence. The derived polypeptide has the corresponding SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:18 It may have the same or similar immune activating action as the polypeptide of ID NO:33, and it is preferable that the amino acid sequence of the derived polypeptide reaches 98% to 99%.

In a fourth aspect, the present invention provides one or more of the following methods for performing in a subject:

a: up-regulating cellular factors;

b: inducing proliferation of T cells;

c: promoting antigen specific T cell immunity;

d: promoting CD4+ and/or CD8+ T cell activation.

The method comprises administering to said subject any one of said viral therapeutic compositions of the invention, wherein preferred viral therapeutic compositions are SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO one or more of :18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:33 or a derived polypeptide having at least 95% sequence identity with such an amino acid sequence includes The derived polypeptide has the corresponding SEQ ID NO:8, SEQ ID NO:11, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:23, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:18 It may have the same or similar immune activating action as the polypeptide of ID NO:33, and it is preferable that the amino acid sequence of the derived polypeptide reaches 98% to 99%.

The present invention also provides a method for treating or preventing a related symptom of the immune system, said method comprising administering to a subject in need thereof an effective amount of a viral therapeutic composition of any one of the present invention. The immune-related symptom includes a viral infection, and the viral infection includes a coronavirus infection, a flu virus infection, a hepatitis virus infection, and the like.

In addition, this treatment is used in conjunction with the method for treating another viral infection, and the method for treating the other viral infection may include other previously known and validated effective methods, for example, the antiviral drug bevirolase, mara maraviroc et al; Raltegravir, an integrase strand transfer inhibitor; Bevirimat, a maturation inhibitor; neuraminidase inhibitors, such as Oseltamivir, zanamivir, and Peramivir.

The virus of the present invention includes viral peptides, polypeptide proteins capable of inducing an immune response, and viral microorganisms capable of inducing an immune response, for example, hepatitis A virus, hepatitis B virus, hepatitis C virus, herpes simplex virus, Further includes HIV (human immunodeficiency virus), HPV, influenza virus, respiratory syncytial virus, and the like.

The drug composition administered to the subject of the present invention further includes a drug or a drug thereof that is transferred, delivered, introduced or transported to the subject in any manner, and such methods include oral administration, local contact, intravenous administration, intramuscular administration, Including intranasal and subcutaneous administration. The present invention also contemplates administering the drug using a device or for a limited period. In addition, the medicament includes a pharmaceutically acceptable excipient such as any vector, diluent, suppository or the like.

According to the peptide preparation of the present invention, it is possible to achieve a remarkable effect of remarkably activating the immune system of the human body against CoVid-19 virus.

It also provides the basis for safe and effective peptide vaccine design.

1 is a diagram of detection of the formation of a peptide-HLA-I complex.
Figure 2 is the binding percentage of HLA-I tetramers and CD8 T-cells for 2 hours.
Fig. 3 shows the binding percentage of HLA-I tetramers and CD8 T-cells for 4 hours.
Figure 4 is the CD8 T-cell activation status of HLA-I tetramer for 2 hours.
Figure 5 is the CD8 T-cell activation status of HLA-I tetramer for 4 hours.

The present invention will be described in more detail with respect to the following examples.

Example One: peptide - HLA -I complex formation

The experiment was carried out according to the experimental operation procedure of the Monomer/Tetramer production protocol of the easYmer HLA-A*02:01 MHC Tetramers Kit of Immunaware.

1. Take an appropriate amount of the sample peptide to be measured (Table 1), and dissolve dimethyl sulfoxide to 1 mm.

2. A positive control peptide (the positive control peptide is provided by the immunaware easYmer HLA-A*02:01 MHC Tetramers Kit). Dilute the sample peptide to be measured to 25 μm with re-distilled water.

3. Prepare each reaction tube on ice according to the table below (refer to Table 2), separate repeatedly using a pipette, and mix thoroughly to prevent bubble formation.

4. After sealing with sealing tape, prepare by incubating at 18 degrees Celsius for 48 hours.

polypeptide sequence No size sequence No size sequence One# 1,380 GVAPGTAVLRQW 19# 1,380 RTVYDDGARRVW 2# 1,265 VAPGTAVLRQW 20# 1,265 TVYDDGARRVW 3# 1,150 VAIKITEHSW 21# 1,035 VSFLAHIQW 4# 1,150 GRVDGQVDLF 22# 1,150 RRVVFNGVSF 5# 1,265 GRVDGQVDLFR 23# 1,265 YLFDESGEFKL 6# 1,150 KRFKESPFEL 24# 1,035 LYDKLVSSF 7# 1,035 KRVDWTIEY 25# 1,150 TTDPSFLGRY 8# 1,610 VTDVTQLYLGGMSY 26# 1,150 TEIDPKLDNY 9# 1,035 IYNDKVAGF 27# 1,265 TEIDPKLDNYY 10# 1,150 VENPDILRVY 28# 1,265 AEAELAKNVSL 11# 1,035 KLFDRYFKY 29# 1,380 IALKGKIVNNW 12# 1,150 KSAGFPFNKW 30# 1,035 LLLDRLNQL 13# 1,035 VENPHLMGM 31# 1,495 ITVEELKKLLEQW 14# 1,150 QEYADVFHLY 32# 1,150 EELKKLLEQW 15# 1,150 LTDNTSRYW 33# 1,035 NRFLYIIKL 16# 1,495 ARFPKSDGTGTIY 34# 1,150 KRFDNPVLPF 17# 1,265 ISMDNSPNLAW 35# 1,150 TEKSNIIRGW 18# 1,035 FLLPSLATV 36# 1,495 RSYLTPGDSSSGW 37# 1,495 YRFNGIGVTQNVL

Conditions for preparing the HLA-I peptide complex positive control voice contrast sample peptide re-distilled water 3 μl 4 μl 3 μl Peptide (25 μM) 1 μl 1 μl 6x buffer solution 1 μl 1 μl 1 μl easymer lμl lμl lμl

Example 2: flow cytometry based on peptide - HLA -I complex formation detection

Prepare a sufficient amount of dilution buffer (phosphate buffer containing 5% glycerol) and FACS solution (phosphate buffer containing 1% bovine serum albumin) before the experiment.

1. Take 4 μl of the peptide-HLA-I complex solution, add it to 46 μl of dilution buffer, and mix evenly.

2. Take 25 μl of the peptide-HLA-I complex solution, add it to 50 μl of dilution buffer, and mix evenly.

3. Pour 40 μl of the dilution from step 2 into a new EP tube.

4. Dilute streptavidin-coated Magnetic Particles (6-8 μm) 45-fold with dilution buffer, add 25 μl to each tube, and mix thoroughly.

5. Incubate for 1 hour in a shaker at 37°C.

6. Add 160 μl of FACS solution to each tube.

7. After centrifugation for 3 minutes, remove the supernatant.

8. Resuspend the FACS solution in 200 μl, centrifuge at 700 g for 3 min and remove the supernatant, repeat this step, and then wash twice.

9. Dilute the PE-marked monoclonal antibody BBM.1 200-fold with FACS solution.

10. Add 50 μl of antibody dilution to each tube to resuspend, and incubate by blocking light at 4° C. for 30 min.

11. Add 150 μl of FACS solution, centrifuge at 700 g for 3 min, and remove the supernatant.

12. Resuspend 200 μl of FACS solution, centrifuge at 700 g for 3 min and remove the supernatant, repeat this step and wash twice.

13. Resuspend 200 μl of FACS solution and perform detection analysis by flow cytometry.

Results (see FIG. 1 ): The fluorescence intensity of SEQ ID NOs: 18, 23, 30 was similar to that of the positive polypeptide, indicating that the 18, 23, 30 polypeptides were successfully bound to HLA.

Example 3: tetramer relation:

The experiment was performed according to the experimental operation procedure of the Monomer/Tetramer production protocol of the easYmer HLA-A*02:01 MHC Tetramers Kit of Immunaware.

tetrameric Produce

1. Take 6 μl of the prepared 500 nm peptide 18#, 23#, 30# and HLA-I monomer complex mixture, put it in a 0.2 mL centrifuge tube, and 0.48 μl Streptavidin-BV421 (BD; Cat #563259; 0.1 mg/ ml) is added.

2. After mixing evenly, incubate at 4°C for 1 hour while blocking light.

single human peripheral blood of nuclear cells (PBMC) separation

1. Take fresh anticoagulated whole blood (EDTA) (collected from human venous blood) and dilute it with an equal volume of physiological saline.

2. Put an appropriate amount of the lymphocyte separation solution into a 15ml centrifuge tube, and spread the diluted blood flat on top of the separation solution to keep the interface between the two liquid levels clean.

3. Horizontal centrifuge at room temperature at 600 g for 35 min.

4. After centrifugation, it can be seen that the inside of the tube is separated into three layers, the upper layer is plasma and physiological saline, the lower layer is mainly red blood cells and granulocytes, and the middle layer is the lymphocyte cell separation solution. At the interface between the upper and middle layers, there is a narrow band of single-nucleated, white misty cells, and the single-nucleated cells contain lymphocytes and monocytes, and in addition, platelets are more present.

5. A pipette is inserted into the mist layer to aspirate single nuclear cells, put in a separate 15ml centrifuge tube, add 5 times the volume of physiological saline, and centrifuge at 250g for 10 minutes, then the cells are washed once Wash.

6. Add 10 ml of PBS or cell washing solution, take 10 μl and count, centrifuge at 250 g for 10 minutes, and wash the cells once.

with tetramers PBMC co-incubation of

1. Take a new 1.5ml centrifuge tube, put 2*10^6 PBMC into each tube, add 200 μl of FACS buffer, and centrifuge at 700 g for 3 minutes to remove the supernatant.

2. Dilute the tetramer to 300 nmol using a FACS buffer, and resuspend PBMC for the tetramer after dilution with 40 μl of each tube, and then incubate at 37° C. for 2-4 hours under light blocking.

3. Wash the cells once with pre-chilled FACS buffer.

4. A flowing antibody (CD3-percp-cy5.5, CD8-APC, CD4-PE-cy7, CD69-PE, antibody source-BioLegend) is added and stained at 4°C for 30 minutes.

5. Wash cells once with FACS buffer and detect with instrument.

The results show that the polypeptide-HLA tetramers of SEQ ID NOs: 18, 23 and 30 did not bind to CD8 T-cells for 2 hours (see FIG. 2 ), and when the SEQ ID NOs: 23 polypeptide-HLA tetramers were CD8 T cells for 4 hours - It was shown to be associated with cells (see FIG. 3).

SEQ ID NOs: 18, 23 and 30 polypeptide-HLA tetramers were unable to activate CD8+ T-cells for 2 hours (see FIG. 4 ), but CD69 was positive for 4 hours, and the SEQ ID NO:23 polypeptide-HLV tetramers were CD8+ It was shown that T-cells can be remarkably activated, that is, the immune activation effect is distinct (see FIG. 5 ).

<110> Azothbio Inc. QINGDAO KEZHIXING ROBOT CO.,LTD. <120> A POLYPEPTIDE PRODUCT <130> JPA20-KK089 <140> 10-2020-0129206 <141> 2020-10-07 <160> 37 <170> KoPatentIn 3.0 <210> 1 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> 1# peptide <400> 1 Gly Val Ala Pro Gly Thr Ala Val Leu Arg Gln Trp 1 5 10 <210> 2 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 2# peptide <400> 2 Val Ala Pro Gly Thr Ala Val Leu Arg Gln Trp 1 5 10 <210> 3 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 3# peptide <400> 3 Val Ala Ile Lys Ile Thr Glu His Ser Trp 1 5 10 <210> 4 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 4# peptide <400> 4 Gly Arg Val Asp Gly Gln Val Asp Leu Phe 1 5 10 <210> 5 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 5# peptide <400> 5 Gly Arg Val Asp Gly Gln Val Asp Leu Phe Arg 1 5 10 <210> 6 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 6# peptide <400> 6 Lys Arg Phe Lys Glu Ser Pro Phe Glu Leu 1 5 10 <210> 7 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 7# peptide <400> 7 Lys Arg Val Asp Trp Thr Ile Glu Tyr 1 5 <210> 8 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> 8# peptide <400> 8 Val Thr Asp Val Thr Gln Leu Tyr Leu Gly Gly Met Ser Tyr 1 5 10 <210> 9 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 9# peptide <400> 9 Ile Tyr Asn Asp Lys Val Ala Gly Phe 1 5 <210> 10 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 10# peptide <400> 10 Val Glu Asn Pro Asp Ile Leu Arg Val Tyr 1 5 10 <210> 11 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 11# peptide <400> 11 Lys Leu Phe Asp Arg Tyr Phe Lys Tyr 1 5 <210> 12 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 12# peptide <400> 12 Lys Ser Ala Gly Phe Pro Phe Asn Lys Trp 1 5 10 <210> 13 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 13# peptide <400> 13 Val Glu Asn Pro His Leu Met Gly Met 1 5 <210> 14 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 14# peptide <400> 14 Gln Glu Tyr Ala Asp Val Phe His Leu Tyr 1 5 10 <210> 15 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 15# peptide <400> 15 Leu Thr Asn Asp Asn Thr Ser Arg Tyr Trp 1 5 10 <210> 16 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> 16# peptide <400> 16 Ala Arg Phe Pro Lys Ser Asp Gly Thr Gly Thr Ile Tyr 1 5 10 <210> 17 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 17# peptide <400> 17 Ile Ser Met Asp Asn Ser Pro Asn Leu Ala Trp 1 5 10 <210> 18 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 18# peptide <400> 18 Phe Leu Leu Pro Ser Leu Ala Thr Val 1 5 <210> 19 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> 19# peptide <400> 19 Arg Thr Val Tyr Asp Asp Gly Ala Arg Arg Val Trp 1 5 10 <210> 20 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 20# peptide <400> 20 Thr Val Tyr Asp Asp Gly Ala Arg Arg Val Trp 1 5 10 <210> 21 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 21# peptide <400> 21 Val Ser Phe Leu Ala His Ile Gln Trp 1 5 <210> 22 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 22# peptide <400> 22 Arg Arg Val Val Phe Asn Gly Val Ser Phe 1 5 10 <210> 23 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 23# peptide <400> 23 Tyr Leu Phe Asp Glu Ser Gly Glu Phe Lys Leu 1 5 10 <210> 24 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 24# peptide <400> 24 Leu Tyr Asp Lys Leu Val Ser Ser Phe 1 5 <210> 25 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 25# peptide <400> 25 Thr Thr Asp Pro Ser Phe Leu Gly Arg Tyr 1 5 10 <210> 26 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 26# peptide <400> 26 Thr Glu Ile Asp Pro Lys Leu Asp Asn Tyr 1 5 10 <210> 27 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 27# peptide <400> 27 Thr Glu Ile Asp Pro Lys Leu Asp Asn Tyr Tyr 1 5 10 <210> 28 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> 28# peptide <400> 28 Ala Glu Ala Glu Leu Ala Lys Asn Val Ser Leu 1 5 10 <210> 29 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> 29# peptide <400> 29 Ile Ala Leu Lys Gly Gly Lys Ile Val Asn Asn Trp 1 5 10 <210> 30 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 30# peptide <400> 30 Leu Leu Leu Asp Arg Leu Asn Gln Leu 1 5 <210> 31 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> 31# peptide <400> 31 Ile Thr Val Glu Glu Leu Lys Lys Leu Leu Glu Gln Trp 1 5 10 <210> 32 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 32# peptide <400> 32 Glu Glu Leu Lys Lys Leu Leu Glu Gln Trp 1 5 10 <210> 33 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> 33# peptide <400> 33 Asn Arg Phe Leu Tyr Ile Ile Lys Leu 1 5 <210> 34 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 34# peptide <400> 34 Lys Arg Phe Asp Asn Pro Val Leu Pro Phe 1 5 10 <210> 35 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> 35# peptide <400> 35 Thr Glu Lys Ser Asn Ile Ile Arg Gly Trp 1 5 10 <210> 36 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> 36# peptide <400> 36 Arg Ser Tyr Leu Thr Pro Gly Asp Ser Ser Ser Gly Trp 1 5 10 <210> 37 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> 37# peptide <400> 37 Tyr Arg Phe Asn Gly Ile Gly Val Thr Gln Asn Val Leu 1 5 10

Claims (6)

In the polypeptide having an immune activating action,
The amino acid sequence code of the polypeptide is SEQ ID NO:18 or at least 95% sequence identity with the amino acid sequence of the polypeptide or at least one kind of a derived polypeptide. In the virus therapeutic composition,
The composition comprises one or more of the amino acid sequence code of SEQ ID NO:18 or a derivative polypeptide having at least 95% sequence identity with the amino acid sequence. In the virus detection composition,
The composition comprises one or more of the amino acid sequence code of SEQ ID NO:18 or a derivative polypeptide having at least 95% sequence identity with the amino acid sequence. In the host cell containing the expression vector,
The host cell is a host cell capable of expressing one or more of the amino acid sequence code of SEQ ID NO:18 or a derived polypeptide having at least 95% sequence identity with the amino acid sequence. For use in the manufacture of a therapeutic composition for a virus that promotes CD4+ and/or CD8+ T-cell activation of a polypeptide,
The use of the polypeptide is at least one kind of derived polypeptide having an amino acid sequence code of SEQ ID NO: 18 or at least 95% sequence identity with the amino acid sequence. For use in the manufacture of a pharmaceutical composition for treating a viral infection of a polypeptide,
The use of the polypeptide is at least one kind of derived polypeptide having an amino acid sequence code of SEQ ID NO: 18 or at least 95% sequence identity with the amino acid sequence.

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