Application of GW7647 in preparation of medicine for inhibiting cell lipid peroxidation caused by African swine fever virus protein

Abstract

The invention discloses application of GW7647 in preparation of a medicine for inhibiting cell lipid peroxidation caused by African swine fever virus protein, and belongs to the technical field of medicine. The invention proves the application of GW7647 in preparation of drugs for inhibiting cell lipid peroxidation caused by African swine fever virus protein; the African swine fever virus protein is African swine fever virus A151R. Experiments prove that ASFV A151R can promote cell lipid peroxidation damage and induce cell lipid peroxidation; the GW7647 can inhibit cell lipid peroxidation caused by ASFV A151R, and can be applied to research on lipid peroxidation of the African swine fever virus on cells; the medicine for inhibiting cell lipid peroxidation has important value for researching the anti-infection capability of an African swine fever virus infected host, the relationship between cell lipid peroxidation and innate immunity and the like.

Description

Technical Field

[0001] The present invention belongs to the field of medical technology, and in particular relates to an application of GW7647 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein. Background Art

[0002] African swine fever (ASF) is a highly contagious disease caused by African swine fever virus (ASFV), which has caused serious economic losses to the pig farming industry. Although some achievements have been made in the research on ASF, its pathogenicity and immune escape mechanisms need to be further clarified. There is still no specific vaccine or drug for ASF. Therefore, further identification of ASFV virulence factors and immunosuppressive factors is crucial for the prevention and treatment of ASF. The innate immune response is the first line of defense for the host against pathogen invasion. The cGAS-STING signaling pathway can recognize viral DNA in the cytoplasm and produce a series of antiviral responses to protect the host. At the same time, viral infection often leads to an imbalance in cellular redox homeostasis, causing cellular lipid peroxidation and oxidative stress, which in turn leads to the immune escape of the virus, promotes viral replication, and reduces the host's ability to resist infection. Currently, there is no drug that inhibits lipid peroxidation caused by ASFV infection.

[0003] Oxidative stress refers to the excessive production of free radicals such as reactive oxygen species (ROSs) and reactive nitrogen species (RNSs) in cells after certain stimulation. The level exceeds the ability of cells to remove free radicals and other oxidants, and the cell redox system is unbalanced, resulting in cell damage. Lipid peroxidation (LPO) refers to the oxidative degradation of lipids. The specific process is initiation, diffusion, and termination. Specifically, under the stimulation of exogenous or endogenous factors, excessive reactive oxygen free radicals react with fat groups to produce peroxy fatty acid groups. After that, a series of chain reactions will occur, and different fatty acid free radicals will be generated in the middle, and finally lipid peroxides such as malondialdehyde (MDA) and 4-hydroxynonenal will be generated. Polyunsaturated fatty acids (PUFAs) are prone to LPO under the induction of free radicals. Therefore, cell membranes and lipoproteins rich in PUFA phospholipids and cholesterol are more easily damaged under oxidative stress. For example, the invasion of pathogens often causes cellular oxidative stress. The free radicals produced will react with lipids to form oxidized lipids. Cell membranes rich in polyunsaturated fatty acids are more vulnerable to attack, causing cell membrane rupture and leading to cell death.

[0004] Viral infection often causes an imbalance in cellular redox homeostasis. Many studies have found that viruses can upregulate lipid peroxidation levels in cells to take advantage of their own infection and replication. For example, Cheng et al. found that swine influenza virus (SIV) can inhibit GPX4 activity to enhance viral replication by downregulating SLC7A11 levels and causing GSH depletion. Cao et al. found that human immunodeficiency virus (HIV) reduces GPX4 levels in T cells in the early stages of infection to enhance ferroptosis, leading to CD4 + T cells are gradually consumed under the action of ferroptosis induced by T cell receptor activation, which is conducive to the occurrence and development of the disease.

[0005] Generally speaking, most studies have found that viruses can promote the spread of viruses between cells by promoting damage and rupture of cell membrane lipids, increase viral replication titers, reduce the anti-infection ability of humans or hosts, and lead to the occurrence of related viral diseases.

[0006] In summary, cellular lipid peroxidation has important research value in the process of viral infection and reproduction. Currently, there is no effective drug that can inhibit lipid peroxidation caused by ASFV infection. Summary of the invention

[0007] An embodiment of the present invention provides an application of GW7647 in the preparation of a drug for inhibiting cellular lipid peroxidation caused by African swine fever virus protein, aiming to solve the problem that there is currently no effective drug for inhibiting cellular lipid peroxidation caused by African swine fever virus protein.

[0008] The technical solution of the present invention is achieved in this way:

[0009] In the embodiment of the present invention, a eukaryotic expression plasmid of African swine fever virus A151R was constructed, and the relationship between African swine fever virus A151R and cellular lipid peroxidation was confirmed by experiments such as detecting cellular ROS levels and lipid ROS levels by fluorescent probes and immunofluorescence staining, and detecting cellular protein carbonylation levels by Western Blot. The results showed that A151R can significantly promote the production of cellular ROS and lipid ROS, indicating that ASFV A151R promotes cellular lipid peroxidation damage.

[0010] In order to further explore the role of GW7647 in the process of African swine fever virus A151R promoting cellular lipid peroxidation, the expression levels of GPX4 and related proteins and the cellular GSH content were detected, and the cellular ROS and lipid ROS levels were detected. The results showed that A151R can significantly inhibit the expression of GPX4 and SLC7A11, reduce the cellular GSH level, and increase the MDA level. GW7647 treatment can restore the accumulation of cellular ROS and lipid ROS caused by A151R, increase the GSH level, and reduce the MDA level.

[0011] The above experiments verified the application of GW7647 in the preparation of drugs for inhibiting cellular lipid peroxidation caused by African swine fever virus protein.

[0012] More preferably, the cell is a mammalian cell. Even more preferably, the mammalian cell is at least one of porcine alveolar macrophage 3D4 / 21A, human embryonic kidney cell 293T or porcine primary alveolar macrophage PAM.

[0013] Further preferably, the African swine fever virus protein is African swine fever virus A151R.

[0014] Further preferably, the chemical formula of GW7647 is C 29 H 46 N2O3S.

[0015] Further preferably, the structural formula of GW7647 is as shown in Formula I:

[0016]

[0017] Viral infection and viral proteins (such as A151R) often cause oxidative damage to cells, among which lipid peroxidation can affect protein structure and function through carbonylation of proteins, inhibit information transduction of signal pathways and thus affect the antiviral response of cells. Therefore, drugs that inhibit cellular lipid peroxidation are of great value for the study of viral infection and cellular lipid peroxidation.

[0018] Compared with the prior art, the technical solution of the present invention has the following beneficial effects:

[0019] The present invention confirms that GW7647 has the function of inhibiting cell lipid peroxidation caused by African swine fever protein, and can be used in the preparation of drugs for inhibiting cell lipid peroxidation caused by African swine fever virus protein. The present invention confirms through experiments that ASFV A151R can promote cell lipid peroxidation damage and induce cell lipid peroxidation. GW7647 can inhibit cell lipid peroxidation caused by ASFV A151R, and can be used in studying the lipid peroxidation of cells by African swine fever virus. Drugs that inhibit cell lipid peroxidation are of great value for the study of viral infection and cell lipid peroxidation. BRIEF DESCRIPTION OF THE DRAWINGS

[0020] Figure 1 The results of A151R promoting cellular lipid peroxidation, promoting protein carbonylation, and inhibiting the translocation of STING to the Golgi apparatus, including: (A) ROS fluorescent probe detection; (B) lipid ROS fluorescent probe detection; (C) protein carbonylation level detection; (D) STING and Golgi apparatus subcellular localization.

[0021] Figure 2 These are the detection results of A151R promoting lipid peroxidation, including (A) GSH detection; (B) MDA detection; (C) GPX4 mRNA level detection; (D) GPX4 and SLC7A11 protein band detection; (EH) are the detection results after cGAS-STING treatment, specifically (E) GSH detection; (F) MDA detection; (G) GPX4 mRNA detection; (H) GPX4 and SLC7A11 protein band detection.

[0022] Figure 3 This is a graph showing the results of protein carbonylation detection after A151R and GW7647 treatment.

[0023] Figure 4 This is a graph showing the detection results that GW7647 can restore the oxidative damage caused by A151R; including: (A) ROS fluorescent probe detection; (B) lipid ROS fluorescent probe detection; (C) MDA detection; (D, E) GPX4 expression level detection. DETAILED DESCRIPTION

[0024] The following will be combined with the drawings in the embodiments of the present invention to clearly and completely describe the technical solutions in the embodiments of the present invention. Obviously, the described embodiments are only part of the embodiments of the present invention, not all of the embodiments. Based on the embodiments in the present invention, all other embodiments obtained by ordinary technicians in this field without creative work are within the scope of protection of the present invention. In addition, the technical solutions between the various embodiments can be combined with each other, but they must be based on the ability of ordinary technicians in this field to implement them. When the combination of technical solutions is contradictory or cannot be implemented, it should be deemed that such a combination of technical solutions does not exist and is not within the scope of protection required by the present invention.

[0025] At present, there is a problem that there is no effective inducer of cellular lipid peroxidation that can be used for the study of cellular lipid peroxidation. In order to solve the above technical problems, the present invention proposes an application of African swine fever virus A151R in the preparation of a cellular lipid peroxidation inducer.

[0026] Experimental Materials

[0027] 1. Cells, strains and viruses

[0028] Porcine alveolar macrophages 3D4 / 21A and human embryonic kidney cells 293T were purchased, and primary porcine alveolar macrophages PAM were obtained from healthy piglet lungs and stored in the laboratory. DH5α competent cells were purchased from Novazonics Technologies Co., Ltd. ASFV SY2018 virus strain was stored in an Animal Biosafety Level 3 Laboratory (ABSL-3).

[0029] 2. Plasmid

[0030] The eukaryotic expression vectors pCAGGS-C-HA, pCAGGS-C-FLAG, and pcDNA3.1-EGFP used were purchased, and the expression plasmids cGAS-Flag and STING-Flag gene prokaryotic plasmids were stored in the applicant's laboratory. Restriction endonucleases were purchased from Thermo Fisher Scientific Inc. PCR product gel recovery kit, plasmid mini-extraction kit, and plasmid midi-extraction kit were purchased from Jiangsu Kangwei Century Biotechnology Co., Ltd.

[0031] 3. Main reagents and antibodies

[0032] PhantaTM Super-Fidelity DNA Polymerase, Clone II recombinase and nucleic acid dye were purchased from Nanjing Vazyme Biotechnology Co., Ltd. Anhydrous ethanol, methanol, isopropanol, sodium chloride and other reagents were purchased from Sinopharm Chemical Reagent Co., Ltd. SWE fast high-resolution electrophoresis buffer (dry powder), transfer buffer (dry powder), and TBS (dry powder) were purchased from Sevier Biotechnology Co., Ltd. PVDF membrane was purchased from Thermo Fisher Scientific. Anti-Flag tag antibody was purchased from Wuhan Sanying Biotechnology Co., Ltd. Anti-HA, STING, phospho-STING, TBK1, phospho-TBK1, IRF3, phospho-IRF3, NCOA4, GPX4, FTH, LC3, p62, GAPDH antibodies and HRP Goat Anti-Rabbit IgG (H+L), HRP Goat Anti-Mouse IgG (H+L) were purchased from Wuhan Abotek Biotechnology Co., Ltd. Anti-mouse and anti-rabbit IgG 488 green fluorescence and 594 red fluorescence secondary antibodies and HRP-conjugated Streptavidin were purchased from Wuhan Sanying Biotechnology Co., Ltd.

[0033] LB liquid medium: 4 g tryptone, 2 g yeast extract, 2 g sodium chloride, 400 mL ddH2O, sterilize at 121°C for 30 min before use.

[0034] LB solid medium: 4 g tryptone, 2 g yeast extract, 2 g sodium chloride, 4 g agar, 400 mL ddH2O, sterilize at 121°C for 30 min, cool to below 55°C, add antibiotics and plate for use.

[0035] 50% sterile glycerol: Take 100 mL of glycerol, dissolve it to 200 mL with ddH2O, sterilize it with high pressure steam at 121℃ for 30 min, and store it at room temperature.

[0036] 1% agarose gel: weigh 0.2g agarose and add 20mL 1×TAE. Heat thoroughly in a microwave oven. Add 2μL nucleic acid dye and shake thoroughly. Pour into a gel tank and cool to solidify.

[0037] 10% ammonium persulfate (AP): weigh 0.18 g of ammonium persulfate and dissolve it in 1.8 mL of ddH2O. Store at 4°C. It is best to prepare it before use.

[0038] 10% sodium dodecyl sulfate SDS solution (10% SDS): weigh 2 g of high-purity SDS and place it in a 100 mL beaker, add about 16 mL of deionized water, heat at 68°C to dissolve, slowly add concentrated hydrochloric acid to adjust the pH to 7.2, dilute to 20 mL, and store at room temperature.

[0039] TBST: Dissolve TBS powder in 1L ddH2O, and add 1% Tween-20 to mix thoroughly.

[0040] 75% ethanol: Add nuclease-free water to 100 mL for every 75 mL of anhydrous ethanol. This operation is performed in a nuclease-free environment.

[0041] Cell freezing solution: Prepare according to the ratio of FBS:DMSO=9:1, mix gently and use immediately after preparation.

[0042] Primary antibody diluent: Weigh an appropriate amount of BSA powder and fully dissolve it in TBST to prepare a 5% BSA solution, and store it at 4°C.

[0043] Western Blot blocking solution: Weigh an appropriate amount of skim milk powder and fully dissolve it in TBST to prepare 5% skim milk powder. Prepare and use it at room temperature.

[0044] Example

[0045] 1. Experimental Methods

[0046] 1.1 Plasmid construction

[0047] Target fragment amplification: According to the African swine fever virus strains included in NCBI GenBank: MK333180.1, the primer sequence of A151R was designed after codon optimization, and restriction sites were designed at both ends (see Table 1 for details). Vazyme's Phanta Super-Fidelity DNA Polymerase was used for amplification. The reaction conditions were 95℃30s pre-denaturation, 95℃15s, 55-65℃15s, 72℃30s, a total of 35 cycles, and 72℃ thorough extension for 5min. The PCR product was recovered by gel and stored at -20℃.

[0048] Enzyme digestion of the corresponding pCAGGS-Flag, pCAGGS-HA, and pcDNA3.1-EGFP expression vectors, 120V electrophoresis for 30 minutes and gel recovery. Use the Novus Agree source recombination reagent to connect the target fragment and the enzyme-cut vector. The ligation product DH5α competent cell transformation, pick the monoclonal colony and add 6mL of medium containing resistance to shake for 6-8h, PCR amplification and identification of the bacterial solution, and add 25mL of medium containing resistance to shake for 12-16h, use the endotoxin-free extraction kit to extract the plasmid, and perform gene sequencing (completed by Shanghai Shenggong Biotechnology Co., Ltd.), and store the correctly sequenced plasmid at -20℃.

[0049] Table 1 Target fragment amplification primers

[0050]

[0051] 1.2 Isolation and culture of PAM cells

[0052] Select piglets around 15 days old, and after killing, use hemostats to clamp the blood vessels and trachea, slowly peel off the complete lungs, and rinse the lung surface with PBS containing penicillin / streptomycin. Seal the lungs with a sterile sealing bag, spray the surface with alcohol for disinfection, and place on ice to transport to the cell room for separation. Prepare a 50mL sterile centrifuge tube and syringe in advance, clamp the upper end of the trachea with hemostats, use scissors to open a small hole in the trachea that can be inserted into the needle, and use a syringe to inject PBS until the lungs no longer expand. Repeat 3 to 4 times, collect the lavage fluid together, centrifuge at 1000g for 10 minutes, add RPMI-1640 medium to resuspend and count, and then add cell freezing solution to freeze the cells.

[0053] 1.3 Transient cell transfection

[0054] When the cell density (porcine alveolar macrophages 3D4 / 21A, human embryonic kidney cells 293T, porcine primary alveolar macrophages PAM) reaches 70-80%, wash the cells with PBS, add new cell culture medium, and according to the instruction manual of the liposome transfection reagent Lipofectamine 3000, take 2 μg of the target plasmid and 4 μL P3000 in 125 μL OPTI-MEN culture medium and mix them evenly, add them to 125 μL OPTI-MEN culture medium containing 4 μL Lipofectamine 3000 reagent and mix them evenly. After a brief centrifugation, let it stand at room temperature for 15 minutes, add it to the corresponding cell culture dish, replace the complete culture medium after 6 hours of transfection, and transfect at different times according to different experimental requirements and perform relevant tests.

[0055] In addition, dual luciferase reporter gene detection of IFN-β promoter activity, real-time fluorescence quantitative PCR, Western Blot, immunofluorescence staining, total protein carbonylation level detection, STING protein carbonylation level detection, cell malondialdehyde content kit detection, cell GSH content kit detection, cell total iron content kit detection, cell lipid ROS content detection, cell reactive oxygen content detection, and statistical analysis were all performed using conventional kits and conventional detection methods.

[0056] 2. Test results and analysis

[0057] 2.1 ASFV A151R promotes cellular lipid peroxidation

[0058] Viral infection often causes oxidative damage to cells, among which lipid peroxidation can affect protein structure and function through carbonylation of proteins, inhibit information transduction of signal pathways and thus affect the antiviral response of cells. Considering that A151R has a protein structure that mediates oxidative reactions, in order to further explore the molecular mechanism by which A151R promotes cellular lipid peroxidation and inhibits STING phosphorylation, cGAS-FLAG, STING-FLAG and HA-A151R eukaryotic expression plasmids were co-transfected into 3D4 / 21A cells for 24 hours, and the levels of cellular ROS and lipid ROS were detected using fluorescent probes, and the levels of total cellular protein carbonylation and STING protein carbonylation were detected using Western Blot. Immunofluorescence staining and laser confocal microscopy were used to observe and analyze the subcellular localization of STING (red) and cis-Golgi protein GM130 (green) in cells. The results are shown in Figure 2. Figure 1 As shown, A151R significantly promoted cellular ROS ( Figure 1 A) and lipid ROS ( Figure 1 B), promoting the carbonylation of total cellular proteins and STING protein ( Figure 1 C), inhibiting the translocation of STING to the Golgi ( Figure 1 D). It can be seen that A151R has a significant effect of promoting cellular lipid peroxidation, and by promoting cellular lipid peroxidation, it induces STING protein carbonylation, affects the translocation of STING to the Golgi apparatus, and then inhibits the signal transduction of the cGAS-STING pathway.

[0059] 2.2ASFV A151R inhibits GPX4 and promotes lipid peroxidation

[0060] GPX4 is an important antioxidant enzyme that inhibits lipid peroxidation in cells. GSH is an important substrate for GPX4 to exert its anti-lipid peroxidation effect. SLC7A11 is a membrane protein that transports cystine, the raw material for synthesizing GSH. MDA is the final product of cellular lipid peroxidation and can reflect the level of cellular oxidative damage. To further explore the molecular mechanism of A151R promoting cellular lipid peroxidation, HA-A151R eukaryotic expression plasmid was gradient transfected into 3D4 / 21A cells for 24 hours. qPCR was used to detect the GPX4 mRNA level, Western Blot was used to detect the GPX4 and SLC7A11 protein expression levels, and the kit was used to detect the cellular GSH and MDA levels. The results are shown in Figure 2. Figure 2 As shown, A151R significantly inhibited the transcription level of GPX4 ( Figure 2 C) and protein expression levels ( Figure 2 D), inhibiting cellular GSH levels ( Figure 2 A), promotes cell MDA ( Figure 2 B) levels, indicating that A151R inhibited the antioxidant capacity of cells and induced cellular lipid peroxidation.

[0061] 2.3 Inhibition of lipid peroxidation can rescue the inhibitory effect of ASFV A151R on the cGAS-STING signaling pathway

[0062] Based on the fact that lipid peroxidation can affect protein structure and function through carbonylation of proteins, it can inhibit the information transduction of signaling pathways and thus affect the antiviral response of cells. To further explore the effect of A151R promoting lipid peroxidation on carbonylation of proteins, GW7647 (100 nM), which was previously shown to inhibit cellular lipid peroxidation, was used to pretreat 3D4 / 21A cells for 24 hours. The cGAS-FLAG, STING-FLAG and HA-A151R eukaryotic expression plasmids were co-transfected into the cells for 24 hours, and the protein carbonylation level was detected by Western Blot. The results are shown in Figure 2. Figure 3 As shown, GW7647 can inhibit A151R-induced protein carbonylation ( Figure 3 ). It can be seen that when cellular lipid peroxidation is inhibited, the amount of carbonylated protein caused by A151R can be inhibited by pretreatment with GW7647.

[0063] 2.4 To test the inhibitory effect of GW7647 on A151R-induced cellular lipid peroxidation; 3D4 / 21A cells were pretreated with GW7647 for 24 hours, and then the cGAS-FLAG, STING-FLAG and HA-A151R eukaryotic expression plasmids were co-transfected into the cells for 24 hours. The levels of cellular ROS and lipid ROS were detected by fluorescent probes, the levels of cellular MDA were detected by kits, and the expression levels of GPX4 were detected by qPCR and Western Blot. Figure 4 As shown, GW7647 treatment can reduce the ROS caused by A151R ( Figure 4 A), lipid ROS ( Figure 4 B) and MDA( Figure 4 C) increased levels, restoring the GPX4 transcription level caused by A151R ( Figure 4 D) and protein expression levels ( Figure 4 E) decreased, indicating that GW7647 can reverse the lipid peroxidation damage caused by A151R.

[0064] In the embodiment of the present invention, an African swine fever virus A151R eukaryotic expression plasmid was constructed, and the relationship between African swine fever virus A151R and cellular lipid peroxidation was confirmed by detecting cellular ROS levels and lipid ROS levels, Western Blot detecting cellular protein carbonylation levels, immunofluorescence staining and other experiments. The results showed that A151R can significantly promote the production of cellular ROS and lipid ROS, indicating that ASFV A151R promotes cellular lipid peroxidation damage.

[0065] In order to further explore the role of GW7647 in the process of African swine fever virus A151R promoting cellular lipid peroxidation, the expression levels of GPX4 and related proteins and the cellular GSH content were detected, and the cellular ROS and lipid ROS levels were detected. The results showed that A151R could significantly inhibit the expression of GPX4 and SLC7A11 and reduce the cellular GSH level, while GW7647 treatment could restore the accumulation of cellular ROS and lipid ROS caused by A151R.

[0066] The above experiments verified the application of GW7647 in the preparation of drugs for inhibiting cellular lipid peroxidation caused by African swine fever virus protein.

[0067] More preferably, the cell is a mammalian cell. Even more preferably, the mammalian cell is at least one of porcine alveolar macrophage 3D4 / 21A, human embryonic kidney cell 293T or porcine primary alveolar macrophage PAM.

[0068] Further preferably, the African swine fever virus protein is African swine fever virus A151R protein.

[0069] Further preferably, the chemical formula of GW7647 is C 29 H 46 N2O3S.

[0070] Further preferably, the structural formula of GW7647 is as shown in Formula I:

[0071]

[0072] Viral infection and viral proteins (such as A151R) often cause oxidative damage to cells, among which lipid peroxidation can affect protein structure and function through carbonylation of proteins, inhibit information transduction of signal pathways and thus affect the antiviral response of cells. Therefore, drugs that inhibit cellular lipid peroxidation are of great value for the study of viral infection and cellular lipid peroxidation.

[0073] Compared with the prior art, the technical solution of the present invention has the following beneficial effects:

[0074] The present invention confirms that GW7647 has the function of inhibiting cellular lipid peroxidation and can be used in the preparation of drugs for inhibiting cellular lipid peroxidation caused by African swine fever virus protein. The present invention confirms through experiments that ASFV A151R can promote cellular lipid peroxidation damage and induce cellular lipid peroxidation. GW7647 can inhibit cellular lipid peroxidation caused by ASFV A151R and can be used in studying the lipid peroxidation of cells by African swine fever virus. Drugs that inhibit cellular lipid peroxidation are of great value for studying African swine fever virus infection, host anti-infection ability, and the relationship between cellular lipid peroxidation and natural immunity.

[0075] The above description is only a preferred embodiment of the present invention and is not intended to limit the present invention. Any modifications, equivalent substitutions and improvements made within the spirit and principles of the present invention should be included in the scope of protection of the present invention.

Claims

1. Application of GW7647 in the preparation of drugs for inhibiting cellular lipid peroxidation caused by African swine fever virus protein.

2. The use of GW7647 according to claim 1 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein, characterized in that: The cells are mammalian cells.

3. The use of GW7647 according to claim 2 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein, characterized in that: The mammalian cells are at least one of porcine alveolar macrophages 3D4 / 21A, human embryonic kidney cells 293T or porcine primary alveolar macrophages PAM.

4. The use of GW7647 according to claim 1 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein, characterized in that: The African swine fever virus protein is African swine fever virus A151R.

5. The use of GW7647 according to claim 1 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein, characterized in that: The chemical formula of GW7647 is C 29 H 46 N2O3S.

6. Use of GW7647 according to claim 1 in the preparation of a drug for inhibiting cell lipid peroxidation caused by African swine fever virus protein, characterized in that: The structural formula of GW7647 is shown in Formula I:

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