Use of my-1b in the preparation of a drug for preventing and treating nipah virus

Abstract

The application discloses application of MY-1B in preparation of medicines for preventing and treating nipah virus, and belongs to the technical field of medicines.The application is mainly directed to m5C modification of a host, and the methyltransferase activity of NSUN2 is inhibited, so that the m5C modification of the host is reduced, and the replication of the nipah virus is inhibited, and good effects are achieved.At present, most of the researches on virus medicines and vaccines are designed or modified according to the virus itself, and the application provides a new idea for future medicine research and development and vaccine research, and also provides a new use for MY-1B.

Description

TECHNICAL FIELD

[0001] The application belongs to the technical field of medicine, and particularly to the application of MY-1B in the preparation of a drug for preventing and treating Nipah virus. BACKGROUND

[0002] Nipah virus (NiV) is a highly infectious zoonosis pathogen, mainly causing acute fatal encephalitis, with a mortality rate of about 40%-92%, and is listed as a class pathogen in the List of Pathogenic Microorganisms for Human Transmission. In 2018, NiV was listed as one of the key diseases that can cause serious international outbreaks by the World Health Organization R&D Blueprint.

[0003] NiV was first discovered in Malaysia in 1998, and scientists first confirmed and named it as NiV virus in this epidemic. Subsequently, it broke out in Singapore, Bangladesh, India and other regions, causing hundreds of deaths. NiV is mainly transmitted by contact, and the natural host is mainly a specific type of bat such as Pteropus vampyrus. The intermediate host is pig, dog, cat, horse and the like, and the terminal host is human, and it can also be transmitted between humans. NiV infection mainly causes damage to the nervous system and respiratory system, which is called Nipah virus disease, and the typical symptoms are segmental myoclonus, hypertension, tachycardia, reflex loss and hypotonia. The patient may die if he has symptoms of encephalitis, and the survivors also have permanent brain damage.

[0004] NiV belongs to the order Mononegavirales, Paramyxoviridae family, Paramyxovirinae subfamily, Henipavirus genus. The particle is about 150-300 nm in diameter, spherical, polymorphic or filamentous, with a capsule, with a single-stranded negative strand RNA genome of about 18.2 kb. At both ends of the gene open reading frame are UTRs, which contain gene-start (GS) and gene-end (GE) sequences. The GS sequence can act as a signal to initiate mRNA transcription and capping, while the GE can guide mRNA polyadenylation and transcription termination. The NiV genome encodes six structural proteins N, P, L, F, G and M, and three non-structural proteins V, W and C. Among them, N, P, L proteins form a complex and directly bind to viral RNA, regulating viral genome transcription and replication; F and G are glycoproteins that form protrusions on the surface of NiV particles, participate in virus adsorption and membrane fusion to promote virus invasion, and are key determinants of infection and tropism, which can be the main object of vaccine strategies and antigen detection; M protein is involved in maintaining the morphology of viral membrane and regulating NiV-induced antiviral innate immunity, ubiquitination modification promotes the transport of M protein out of the nucleus and promotes virus budding. Although there are many studies on the mechanism of NiV infection and replication and the function of viral proteins in each replication step, the key host factors related to the pathogenic mechanism of NiV are still unclear. In addition, there is no effective antiviral drug for NiV, which has caused a gap in the prevention and treatment of this type of virus.

[0005] Currently, there are relatively mature pathogenic and serological detection and diagnosis techniques for NiV internationally, and our country has developed the industry standard of "Nipah Virus Diagnosis Technology". However, due to the need for high-level biosafety research conditions such as biosafety level 4 laboratory (BSL-4), the research on NiV is less and no antiviral drugs for NiV have been developed, and the main treatment method is still supportive care. Therefore, studying the replication mechanism of NiV and developing and reserving antiviral drugs for NiV are not only the basis for preventing and controlling the risk of NiV transmission, but also the demand of our national health plan.

[0006] m5C modification is an important epigenetic marker in gene regulation, which is not only a functionally defined DNA modification, but also widely exists in RNA. The m5C modification in RNA is the methylation of the fifth C atom on the cytosine of the CpG island, which widely exists in tRNA, rRNA, mRNA, snRNA, miRNA, lncRNA and eRNA, and its modification process is mainly completed by methyltransferase complex, demethylase and reading protein. Its methyltransferase includes NSUN1-NSUN7, TRDMT1 / DNMT2, etc. Demethylase is still controversial, and the methylation of m5C cannot be completely removed, but is oxidized into hm5C. The reported "erasers" mainly include TET (Ten-eleven translocation) family proteins and ALKBH1 proteins. The reading protein has identified ALYREF and YBX1. m5C modification plays an important regulatory function in RNA output, ribosome assembly, translation and RNA stability. MY-1B can covalently bind to the active site cysteine residue (C271) of NSUN2 and exhibit stereoselectivity as a covalent inhibitor of NSUN2, and inhibit the RNA methylation function by modifying the active site of the target protein. At present, its application research is in the initial stage, and the related reports are extremely limited. Only the Chinese invention patent application No. 202510239043.3 discloses the application of MY-1B in preparing a drug for improving ovarian aging. So far, there has been no research report on the application of MY-1B in the field of virus inhibition, and this direction is still blank, which has a large exploration space. SUMMARY

[0007] In view of the above problems, the application provides the application of MY-1B in preparing a drug for preventing and treating NiV. The application first proves that the increase of m5C modification level can promote the replication of NiV, MY-1B is a covalent inhibitor of RNA methyltransferase NSUN2, which can inhibit the expression of NSUN2 and reduce the m5C modification of the host to inhibit the replication of NiV. Developing an anti-NiV drug from the perspective of m5C modification is a new idea, and also provides a new use of MY-1B.

[0008] The MY-1B has a molecular weight of 436.30 and a molecular formula of C 22 H 18 BrN3O2, and the structural formula is as shown in the following formula:

[0009] .

[0010] The application is mainly aimed at the m5C modification of the host, by inhibiting the methyltransferase activity of NSUN2, thereby reducing the m5C modification of the host to inhibit the replication of the Nipah virus, and has good effect.

[0011] Preferably, the Nipah virus is selected from the Malaysian lineage NiV-MY.

[0012] Preferably, the Nipah virus prevention and treatment drug comprises MY-1B or a pharmaceutically acceptable salt of MY-1B, and a pharmaceutically acceptable adjuvant.

[0013] Preferably, the pharmaceutically acceptable adjuvant comprises one or more of a pharmaceutically acceptable carrier, excipient or diluent.

[0014] Preferably, the dosage form of the Nipah virus prevention and treatment drug comprises tablets, capsules, aqueous or oily suspensions, granules, emulsions, oral solutions, injection solutions or powders.

[0015] Preferably, the Nipah virus prevention and treatment drug further comprises at least one other anti-Nipah virus active ingredient.

[0016] Preferably, the administration mode of the drug comprises at least one of oral administration, intratumoral administration, rectal administration, parenteral injection and topical administration.

[0017] The application avoids conventional small molecule drugs that block the virus itself, starts from changing host factors, and achieves an antiviral effect without relying on viral gene sequences, which can well avoid the problem of drug off-target caused by viral mutation. The application finds that overexpression and knockdown of NSUN2 can promote and inhibit NiV replication, respectively, and m5C is reduced after inhibition of NSUN2 to inhibit viral replication. The application finds that MY-1B can significantly reduce the RNA abundance of NiV in infected cells and the yield of progeny viruses in the culture supernatant; in the golden hamster infection model, MY-1B reduces the viral RNA level in the lung tissue and spleen of the golden hamster. The above can show that MY-1B has good inhibitory effect on NiV in cell and animal infection models.

[0018] Compared with the prior art, the application has the following beneficial effects:

[0019] (1) In view of the characteristics that RNA viruses are prone to mutation, the application focuses on host factors rather than the virus itself, and changes the expression of host factors to inhibit viral replication without affecting normal life activities of cells, has better broad-spectrum, and better avoids the problem of viral mutation.

[0020] (2) MY-1B is currently less studied, and the application provides a new use for MY-1B.

[0021] (3) At present, most of the researches on virus drug development and vaccine research are designed or modified for the virus itself, and the present application provides a new idea for future drug development and vaccine development. BRIEF DESCRIPTION OF DRAWINGS

[0022] Figure 1 For overexpression of NSUN2, the m5C modification level of Nipah virus RNA is significantly increased.

[0023] Figure 2 For knockdown of NSUN2, the m5C modification level of Nipah virus RNA is significantly reduced.

[0024] Figure 3 For overexpression of NSUN2, the yield of Nipah virus progeny virus in the culture supernatant after Nipah virus infection is significantly increased.

[0025] Figure 4 For knockdown of NSUN2, the yield of Nipah virus progeny virus in the culture supernatant after Nipah virus infection is significantly reduced.

[0026] Figure 5 For MY-1B, the RNA abundance of virus in Nipah virus infected Vero cells is significantly reduced.

[0027] Figure 6 For MY-1B, the yield of Nipah virus progeny virus in the culture supernatant is significantly reduced.

[0028] Figure 7 For MY-1B, the RNA abundance of virus in the lung tissue and spleen of golden hamster infection model is reduced. DETAILED DESCRIPTION

[0029] The technical solutions of the present application are further described and explained by the following examples. The raw materials used in the examples can be purchased or prepared by conventional methods.

[0030] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this application belongs. The terminology used in the description herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the application. As used herein, the term "and / or" includes any and all combinations of one or more of the associated listed items.

[0031] NiV is mainly transmitted by contact, and the natural host is mainly a specific type of bat such as Pteropus vampyrus. Intermediate hosts include pigs, dogs, cats, and horses, and the final host is humans, and it can be transmitted from person to person. The genome of NiV belongs to the order of single-stranded negative-strand RNA viruses, the family of paramyxoviruses, the subfamily of paramyxoviruses, and the genus of henipaviruses. NiV outbreaks in Southeast Asia can be divided into at least two lineages: the NiV-MY of the Malaysia lineage and the NiV-BD of the Bangladesh lineage, but the pathogenicity difference between NiV-MY and NiV-BD is less studied and the specific molecular mechanism is unclear. The NiV particle is about 150-300 nm in diameter, spherical, polymorphic or filamentous, has a capsule, and has a single-stranded negative-strand RNA genome of about 18.2 kb, in which the 3' leader sequence and the 5' tail region can be used as a replication and transcription element. The UTR is at both ends of the gene open reading frame, which contains a gene-start (GS) sequence and a gene-end (GE) sequence in the UTR, the GS sequence can be used as a signal to start mRNA transcription and capping, and the GE can guide mRNA polyadenylation and transcription termination. The NiV genome encodes six structural proteins N, P, L, F, G and M and three non-structural proteins V, W and C. Among them, N, P, L proteins form a complex and directly bind to viral RNA to regulate viral genome transcription and replication; F and G are glycoproteins that form protrusions on the surface of NiV particles and are involved in virus adsorption and membrane fusion to promote virus invasion, which are key determinants of infection and tropism, and can be used as the main object of vaccine strategy and antigen detection; M protein is involved in maintaining the morphology of viral membrane and regulating NiV-induced antiviral innate immunity, ubiquitination modification promotes the transport of M protein out of the nucleus and promotes virus budding. Although there are many studies on the mechanism of NiV infection and replication and the function of viral proteins in each replication step, the key host factors related to the pathogenesis of NiV are still unclear. In addition, there is no effective antiviral drug for NiV, which has caused a gap in the field of prevention and treatment of this type of virus.

[0032] To solve at least one of the above technical problems, the present application provides an application of MY-1B in anti-NiV drugs with the following structure:

[0033] .

[0034] The MY-1B provided by the present application can inhibit the replication of Nipah virus by inhibiting the methyltransferase activity of NSUN2, and then reducing the m5C modification of the host. In subsequent studies, the present application found that MY-1B can significantly reduce the RNA abundance of NiV in infected cells and the yield of progeny virus in the culture supernatant. In the hamster infection model, MY-1B reduces the viral RNA level in the lungs and spleens of hamsters. These results show that MY-1B has good inhibitory effect on NiV in cell and animal infection models, and has important significance for the prevention and treatment of Nipah virus.

[0035] The MY-1B with the structure of the above formula in the present application can significantly inhibit the replication of Nipah virus in Vero cells.

[0036] The present application evaluates the inhibitory activity of MY-1B against Nipah virus infected cells by culturing Nipah virus. The inhibitory activity of MY-1B against Nipah virus replication in the hamster infection model is evaluated by intraperitoneal injection.

[0037] In some embodiments, the Nipah virus is selected from the Malaysian lineage NiV-MY.

[0038] The present application provides a medicine comprising the compound or pharmaceutically acceptable salt of the compound used in the above application, and a pharmaceutically acceptable auxiliary.

[0039] Specifically, "pharmaceutically acceptable" refers to those ligands, materials, compositions and / or dosage forms that are, within the scope of sound medical judgment, suitable for administration to patients and are commensurate with a reasonable benefit / risk ratio.

[0040] A "pharmaceutically acceptable carrier" refers to a pharmaceutically acceptable material, composition or vehicle, such as a liquid or solid filler, diluent, excipient, solvent or encapsulation material. As used herein, the language "pharmaceutically acceptable carrier" includes buffers, sterile water for injection, solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like, compatible with pharmaceutical administration. Each carrier must be "pharmaceutically acceptable" in the sense of being compatible with the other ingredients of the formulation and not injurious to the patient. Suitable examples include, but are not limited to: (1) sugars, such as lactose, glucose and sucrose; (2) starches, such as corn starch, potato starch, and substituted or unsubstituted beta -cyclodextrin; (3) cellulose and its derivatives, such as sodium carboxymethyl cellulose, ethyl cellulose and cellulose acetate; (4) powdered tragacanth; (5) malt; (6) gelatin; (7) talc; (8) excipients, such as cocoa butter and suppository waxes; (9) oils, such as peanut oil, cottonseed oil, safflower oil, sesame oil, olive oil, corn oil and soybean oil; (10) glycols, such as propylene glycol; (11) polyols, such as glycerin, sorbitol, mannitol and polyethylene glycol; (12) esters, such as ethyl oleate and ethyl laureate; (13) agar; (14) buffering agents, such as magnesium hydroxide and aluminum hydroxide; (15) alginic acid; (16) pyrogen-free water; (17) isotonic saline; (18) Ringer's solution; (19) ethyl alcohol; (20) phosphate buffer solutions; and (21) other non-toxic compatible substances employed in pharmaceutical formulations.

[0041] The dosage form of the drug includes at least one of a tablet, a capsule, an aqueous or oily suspension, a granule, an emulsion, an oral liquid, an injection liquid or a powder, according to different usage modes of the adjuvant.

[0042] The dosage form and administration mode of the compound of the present application or the pharmaceutical composition thereof are not particularly limited. For different dosage forms of the drug, a suitable administration mode can be selected for administration.

[0043] Representative administration modes include, but are not limited to: oral, rectal, parenteral (intravenous, intramuscular or subcutaneous) injection and topical administration.

[0044] Solid dosage forms for oral administration include capsules, tablets, pills, powders, and granules. In such solid dosage forms, the active compound is admixed with at least one inert excipient (or carrier) such as sodium citrate or dicalcium phosphate, or with such other ingredients as binders, (a) fillers or extenders, e.g., starches, lactose, sucrose, glucose, mannitol, and silicic acid, (b) humectants, e.g., hydroxymethylcellulose, alginic acid, gelatin, polyvinylpyrrolidone, sucrose, and acacia, (c) moisturizing agents, e.g., glycerol, (d) disintegrating agents, e.g., agar-agar, calcium carbonate, potato or tapioca starch, alginic acid, certain complex silicates, and sodium carbonate, (e) solution retarders, e.g., paraffin, (f) absoφtion accelerators, e.g., quaternary ammonium compounds, (g) wetting agents, e.g., cetyl alcohol and glycerol monostearate, (h) absorbents, e.g., kaolin, and (i) lubricants, e.g., talc, calcium stearate, magnesium stearate, solid polyethylene glycols, sodium lauryl sulfate, or mixtures thereof. In the case of capsules, tablets, and pills, the dosage forms also can comprise buffering agents. Solid compositions such as tablets, dragees, capsules, pills, and granules can be prepared with coatings and shells, e.g., enteric coatings and other coatings of

[0045] Liquid dosage forms for oral administration include pharmaceutically-acceptable emulsions, solutions, suspensions, syrups, and elixirs. In addition to the active compounds, the liquid dosage forms can contain inert diluents commonly used in the art, such as water or other solvents, solubilizing agents and emulsifiers, as, for example, ethyl alcohol, isopropyl alcohol, ethyl carbonate, ethyl acetate, benzyl alcohol, benzyl benzoate, propylene glycol, 1,3-butylene glycol, dimethylformamide, and the like, as well as mixtures thereof. In addition, the liquid dosage forms can contain adjuvants such as wetting agents, emulsifying and suspending agents, sweetening, flavoring, and perfuming agents. Suspensions, in addition to the active compounds, can contain suspending agents as, for example, ethoxylated isostearyl alcohols, polyoxyethylene sorbitol and sorbitan esters, microcrystalline cellulose, aluminum metahydroxide, and

[0046] Compositions for parenteral injection can contain physiologically acceptable sterile aqueous or nonaqueous solutions, dispersions, suspensions or emulsions, and sterile powders for reconstitution into sterile injectable solutions or dispersions. Suitable aqueous and nonaqueous carriers, diluents, solvents or vehicles include water, ethanol, polyols and suitable mixtures thereof.

[0047] Dosage forms for topical administration of a compound of this application include ointments, powders, sprays, and inhalers. The active component is admixed with a carrier, which can be a sterile oil, such as sesame oil, or a non-volatile oil such as paraffin oil, and can contain a preservative, a buffer, a stabilizer, or a parenterally acceptable salt, as necessary.

[0048] Embodiments of the application will now be described in detail in connection with the following examples.

[0049] Example 1

[0050] NSUN2 is a methyltransferase of m5C validation test:

[0051] S1, One day before transfection, prepare Vero (ATCC, CCL-81, African green monkey kidney cells) cells in a T75 bottle, and when the cells grow to 80%, transfect pFlag-NSUN2 into the Vero cells using Transit-X2 (Mirus, MIR 6004), and incubate at 37°C, 5% CO2 for 24 h;

[0052] S2, One day before infection, shNC, shNSUN2-1 and shNSUN2-2 knockdown cell lines are plated in a T75 bottle;

[0053] S3, On the day of infection, replace the culture medium with 2% FBS (Celligent) containing DMEM (Gibco, C11995500BT);

[0054] S4, infect (MOI=0.01) by NiV-MY Nipah virus (Microbial and Virus Culture Collection Center of Wuhan Institute of Virology, Chinese Academy of Sciences), and collect the cells after 48 h, take part of the cell sample, add 2x Laemmli buffer to it, and boil at 100°C for 5 min, and then detect NSUN2 expression by Western Blot;

[0055] S5, extract RNA from the remaining cell sample using Trizol, dissolve 100 μg of total RNA in 2 volumes of anhydrous ethanol and 1 / 10 volume of 3 mol / L sodium acetate, precipitate at -80°C for half an hour, then centrifuge at 13,000 r / min for 15 min at 4°C, discard the supernatant, blow dry the precipitate, and dissolve in 100 μL of RIP solution (150 mmol / L NaCl, 0.1% NP-40, 10 mmol / L Tris-HCl (pH=7.4));

[0056] S6, take out 1 μL of the solution as INPUT, and add 2 μg of anti-m5C (Abcam, ab10805) antibody to the remaining solution, and incubate overnight at 4°C with shaking;

[0057] S7, Take 20 μL of Dynabeads Protein G (Thermo Fisher, 10004D) and Dynabeads Protein A (Thermo Fisher, 10001D) washed with RIP buffer for 3 times, transfer the solution obtained in step S6 into it, incubate at 4 °C for 2 h;

[0058] S8, discard the supernatant, add 1 mL of RIP solution, repeat the washing of the magnetic beads for 6 times, after washing, extract RNA by Trizol, and detect the content of enriched viral RNA by RT-qPCR (Reverse Transcription Quantitative Polymerase Chain Reaction).

[0059] It can be seen from Figure 1 that the level of m5C is increased after overexpression of NSUN2. It can be seen from Figure 2 that the level of m5C is reduced after knockdown of NSUN2. It is proved that NSUN2 is a m5C methyltransferase.

[0060] Example 2

[0061] Experimental verification of m5C promoting NiV replication:

[0062] S1, prepare Vero (ATCC, CCL-81) cells in a 12-well plate one day before transfection, and when the cells grow to 80%, use Transit-X2 (Mirus, MIR 6004) to transfect pFlag-NSUN2 into the Vero cells, and culture at 37 °C, 5% CO2 for 24 h;

[0063] S2, prepare shNC, shNSUN2-1 and shNSUN2-2 knockdown cell lines in a 12-well plate one day before infection;

[0064] S3, replace with 2% FBS (Celligent) containing DMEM (Gibco, C11995500BT) medium on the day of infection;

[0065] S4, infect (MOI=0.01) by NiV-MY Nipah virus (provided by the Microorganism and Virus Culture Preservation Center of Wuhan Institute of Biology, Chinese Academy of Sciences), collect the supernatant after 48 h, and measure the change of virus titer by TCID50 (Tissue Culture Infective Dose 50, which refers to the amount of virus required to infect 50% of cell culture).

[0066] FromFigure 3 As can be seen from FIG. 1B, after overexpression of NUSN2, the viral titer rises. From FIG. 1C, after knockdown of NUSN2, the viral titer drops. By increasing or reducing the level of m5C modification through overexpression or knockdown of NSUN2, the increase in the level of m5C modification can promote the rise in viral titer, and the decrease in the level of m5C modification inhibits the rise in viral titer, so the above results show that the increase in the level of m5C modification can promote the replication of NiV. Figure 4 As can be seen from FIG. 1B, after overexpression of NUSN2, the viral titer rises. From FIG. 1C, after knockdown of NUSN2, the viral titer drops. By increasing or reducing the level of m5C modification through overexpression or knockdown of NSUN2, the increase in the level of m5C modification can promote the rise in viral titer, and the decrease in the level of m5C modification inhibits the rise in viral titer, so the above results show that the increase in the level of m5C modification can promote the replication of NiV.

[0067] Example 3

[0068] Cell experiment of MY-1B inhibiting Nipah virus replication:

[0069] S1, dimethyl sulfoxide (DMSO, sigma, item number: 67-68-5) was used to prepare a MY-1B (MCE, HY-158301) stock solution, and DMEM medium was used to dilute MY-1B to obtain a working concentration of 10 μM of MY-1B working solution;

[0070] S2, the Vero cells (African green monkey kidney cells) were treated with a MY-1B mixed solution with a concentration of 10 μM;

[0071] S3, the cells were infected (MOI=0.01) by NiV-MY Malaysia strain Nipah virus (Microbial and Virus Culture Collection Center of Wuhan Institute of Virology, Chinese Academy of Sciences), and after 48 h, the total RNA sample and supernatant of the cells were collected, and the viral copy number was detected by RT-qPCR (Reverse Transcription Quantitative Polymerase Chain Reaction);

[0072] As can be seen from FIG. 2B, after treatment of the cells with 10 μM of MY-1B, the viral copy number in the cells was significantly reduced. As can be seen from FIG. 2C, after treatment of the cells with 10 μM of MY-1B, the viral copy number of the progeny virus in the supernatant was significantly reduced. It shows that MY-1B at a concentration of 10 μM can effectively inhibit the replication of Nipah virus. Figure 5 Figure 6 As can be seen from FIG. 2B, after treatment of the cells with 10 μM of MY-1B, the viral copy number in the cells was significantly reduced. As can be seen from FIG. 2C, after treatment of the cells with 10 μM of MY-1B, the viral copy number of the progeny virus in the supernatant was significantly reduced. It shows that MY-1B at a concentration of 10 μM can effectively inhibit the replication of Nipah virus.

[0073] Example 4

[0074] Animal experiment of MY-1B inhibiting Nipah virus replication:

[0075] ​The healthy experimental golden hamsters with similar body weight were respectively infected with Nipah virus (intraperitoneal infection, 500 LD50 / golden hamster) on the same day, and intraperitoneal administration was performed on the second day after infection with Nipah virus (the concentration of golden hamster administration was 15 mg / kg according to the body weight of golden hamster), and the virus load in the lung tissue and spleen was detected respectively on the fourth day after infection with Nipah virus. Figure 7 ).

[0076] From Figure 7 It can be seen that the virus load in the lung tissue and spleen of the golden hamster in the MY-1B treatment group is obviously decreased compared with the control group, which means that MY-1B can inhibit the replication and spread of the virus in the host cell.

[0077] It should be understood that the above examples are only used to illustrate the content of the present application and are not used to limit the protection scope of the present application. In addition, it should be understood that after reading the content of the present application, those skilled in the art can make various modifications or changes to the present application, and these equivalent forms also fall within the scope defined by the claims attached to the present application.

Claims

1. The use of MY-1B in the preparation of a drug for preventing and treating nipah virus, characterized in that, The molecular structure of MY-1B is shown in the following formula: 。 2. The use of MY-1B according to claim 1 in the preparation of a drug for preventing and treating Nipah virus, characterized in that, The Nipah virus is selected from the Malaysian lineage NiV-MY.

3. The use of MY-1B according to claim 1 in the preparation of a drug for preventing and treating Nipah virus, characterized in that, The drug for preventing and treating Nipah virus comprises MY-1B or a pharmaceutically acceptable salt of MY-1B, and a pharmaceutically acceptable adjuvant.

4. The use of MY-1B according to claim 3 for the preparation of a drug for the prevention and treatment of Nipah virus, characterized in that, The pharmaceutically acceptable adjuvant comprises one or more of a pharmaceutically acceptable carrier, excipient or diluent. The pharmaceutically acceptable adjuvant comprises one or more of a pharmaceutically acceptable carrier, excipient or diluent.

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