An isolated polypeptide and uses thereof

Abstract

The present application relates to the technical field of peptide preparation, and provides an isolated polypeptide and application thereof.The polypeptide has an amino acid sequence as shown in SEQ ID NO:1.The polypeptide can effectively inhibit common pathogenic bacteria, for example, Acinetobacter baumannii, multi-drug resistant Acinetobacter baumannii and the like, has low cytotoxicity, high safety, and is suitable for preparing products with bacteriostatic and / or bactericidal properties, such as food or pharmaceutical preparations and the like.

Description

Technical Field

[0001] This invention relates to the field of peptide formulation technology, and more specifically, to an isolated polypeptide and its applications. Background Technology

[0002] Acinetobacter baumannii ( Acinetobacter baumannii , A. baumannii Acinetobacter baumannii is a Gram-negative bacterium and one of the most common pathogens causing hospital-acquired infections, particularly in critically ill patients, causing pneumonia or bloodstream infections. This bacterium exhibits natural resistance to many antibiotics. According to research reports, the resistance rate of Acinetobacter baumannii to carbapenems is on the rise, making it a significant multidrug-resistant pathogen and posing a challenge to clinical treatment. The World Health Organization has listed it as one of the key multidrug-resistant bacteria of concern.

[0003] Antimicrobial peptides are a class of small molecule peptides composed of short-chain amino acids that possess antimicrobial activity and can act on pathogens such as bacteria, fungi, viruses, and parasites. These peptides primarily achieve their bactericidal or bacteriostatic effects by disrupting the cell membrane or cell wall of microorganisms, leading to the leakage of intracellular substances. Compared to traditional antibiotics, bacteria are less likely to mutate and alter their membrane structure to resist antimicrobial peptides; therefore, the risk of antibiotic resistance is lower, making antimicrobial peptides a potential alternative to traditional antibiotics.

[0004] Archaea are a class of prokaryotic single-celled microorganisms that live in extreme environments. Although they share many similarities with bacteria—namely, they lack a nucleus and any other membrane-bound organelles—they also possess certain characteristics of eukaryotes in terms of genome structure and cell physiology, such as the presence of repetitive sequences and nucleosomes. Archaea are widely distributed in various extreme natural environments, such as high-pressure hydrothermal vents, hot springs, and saline lakes on the ocean floor. Their unique survival mechanisms make them a potential functional molecular resource pool.

[0005] Currently, most antimicrobial peptides derived from microorganisms are discovered in bacteria, but the resources of antimicrobial peptides derived from archaea have not been fully explored. Therefore, it is urgent to strengthen the exploration and development of antimicrobial peptides derived from archaea to expand their diversity and application potential. Summary of the Invention

[0006] This invention aims to at least partially address one of the technical problems existing in the prior art, particularly the antibacterial needs for Acinetobacter baumannii and its multidrug-resistant strains. Therefore, one objective of this invention is to provide an isolated polypeptide with significant antibacterial and bactericidal properties and its related applications. The polypeptide exhibits antibacterial and bactericidal effects against various bacteria, such as Acinetobacter baumannii and multidrug-resistant Acinetobacter baumannii. This polypeptide is not prone to inducing drug resistance and has low mammalian cytotoxicity and hemolytic toxicity, demonstrating good application safety. It can be used to prepare antibacterial compositions for treating Acinetobacter baumannii and multidrug-resistant Acinetobacter baumannii, and can also be used as a peptide inhibitor in antibacterial compositions or antibacterial products in the food, pharmaceutical, or daily care fields.

[0007] Specifically, the technical solution of the present invention is as follows:

[0008] In a first aspect, the present invention provides an isolated polypeptide. According to an embodiment of the invention, the isolated polypeptide has an amino acid sequence as shown in SEQ ID NO: 1.

[0009] According to an embodiment of the present invention, the isolated polypeptide is derived from... PL-Br10-E2g29 Fungi.

[0010] According to an embodiment of the present invention, the isolated polypeptide is derived from... PL-Br10-E2g29 sp001563965 Archaeal strains.

[0011] In a second aspect, the present invention provides a nucleic acid molecule. According to an embodiment of the invention, the nucleic acid encodes the isolated polypeptide described in the first aspect. The isolated polypeptide can be obtained by expressing the nucleic acid molecule according to embodiments of the invention under suitable conditions.

[0012] It should be noted that the "suitable conditions" mentioned in this specification refer to conditions suitable for the expression of the isolated peptides described in this invention. Those skilled in the art will readily understand that suitable conditions for the expression of the isolated peptides include, but are not limited to, suitable transformation or transfection methods, healthy host cell status, suitable host cell density, and appropriate cell culture environment and time. The term "suitable conditions" is not particularly limited, and those skilled in the art can optimize the conditions for the optimal expression of the isolated peptides as needed.

[0013] In a third aspect, the present invention provides a composition. According to an embodiment of the invention, the composition comprises: the isolated polypeptide described in the first aspect.

[0014] According to embodiments of the present invention, the composition is a pharmaceutical, and the composition further comprises a pharmaceutically acceptable carrier. A "pharmaceutically acceptable carrier" can include any and all physiologically compatible solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic agents, and delayed absorption agents, etc. Specific examples may be water, saline, phosphate-buffered saline, glucose, glycerol, ethanol, and one or more combinations thereof. In many cases, the composition includes isotonic agents, such as sugars, polyols (e.g., mannitol, sorbitol), or sodium chloride. Of course, a pharmaceutically acceptable carrier may also include trace amounts of excipients, such as wetting agents or emulsifiers, preservatives, or buffers, to prolong the shelf life or potency of the antibody.

[0015] In a fourth aspect, the invention provides for the use of the isolated polypeptides described in the first aspect, the nucleic acid molecules described in the second aspect, or the compositions described in the third aspect in the preparation of products and / or pharmaceuticals. According to embodiments of the invention, the products and / or pharmaceuticals are used to inhibit the growth of pathogens and / or kill pathogens.

[0016] According to an embodiment of the present invention, the pathogen includes Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

[0017] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM.

[0018] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

[0019] Those skilled in the art will understand that the minimum inhibitory concentration of the peptide against pathogens can be used to estimate and calculate the dosage and frequency of the above-mentioned products and / or drugs, and to guide the content of the peptides contained in the above-mentioned products and / or drugs.

[0020] In a fifth aspect, the present invention provides a method for inhibiting the growth of pathogens and / or killing pathogens. According to an embodiment of the present invention, the method comprises: contacting a sample to be treated with an isolated polypeptide as described in the first aspect or a composition as described in the third aspect, wherein the sample to be treated contains the pathogen.

[0021] According to an embodiment of the present invention, the pathogen includes Acinetobacter baumannii and / or multidrug-resistant Acinetobacter baumannii.

[0022] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM.

[0023] According to an embodiment of the present invention, the minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

[0024] Those skilled in the art will understand that the dosage and frequency of use of the aforementioned polypeptide or composition can be estimated and calculated based on the minimum inhibitory concentration of the polypeptide against pathogens.

[0025] In a sixth aspect, the present invention provides a daily necessities and / or care products. According to an embodiment of the invention, the daily necessities and / or fabrics include the isolated polypeptides described in the first aspect of the invention as active ingredients.

[0026] According to an embodiment of the present invention, the daily necessities are selected from at least one of hand sanitizer, shower gel, shampoo, mouthwash, toothpaste, soap, cosmetics, feminine wash, laundry soap, laundry detergent, laundry powder, dish soap, spray, ointment, gel matrix, disinfectant and toilet cleaner; and / or the care products include at least one of sanitary napkins, diapers and incontinence pads.

[0027] As mentioned above, those skilled in the art will understand that the content of the polypeptide contained in the above-mentioned daily necessities and / or care products can be estimated and calculated based on the minimum inhibitory concentration of the polypeptide against pathogens.

[0028] In a seventh aspect, the present invention provides an antibacterial additive. According to an embodiment of the present invention, the antibacterial additive comprises the polypeptide described in the first aspect of the present invention.

[0029] The polypeptide described in this invention has the following beneficial technical effects:

[0030] 1) The isolated polypeptide provided by this invention is derived from deep-sea archaea and has antibacterial activity against Acinetobacter baumannii, multidrug-resistant Acinetobacter baumannii, etc.

[0031] 2) It has been verified that the polypeptide of the present invention is not prone to drug resistance, has low mammalian cytotoxicity and low hemolytic toxicity, and can be used to prepare antibacterial compositions for Acinetobacter baumannii and multidrug-resistant Acinetobacter baumannii infections; in addition, the polypeptide can be used as a peptide inhibitor in daily necessities, food or pharmaceutical fields.

[0032] Additional aspects and advantages of the invention will be set forth in part in the description which follows, and in part will be obvious from the description, or may be learned by practice of the invention. Attached Figure Description

[0033] The above and / or additional aspects and advantages of the present invention will become apparent and readily understood from the description of the embodiments taken in conjunction with the following drawings, in which:

[0034] Figure 1 This is a schematic diagram of the HPLC detection results of the antimicrobial peptide cAMP102 in an embodiment of the present invention;

[0035] Figure 2 This is a schematic diagram of the LC-MS detection results of the antimicrobial peptide cAMP102 in an embodiment of the present invention;

[0036] Figure 3 This is a schematic diagram illustrating the results of the minimum inhibitory concentration (MIC) determination of the antimicrobial peptide cAMP102 in an embodiment of the present invention; wherein,

[0037] (a) Acinetobacter baumannii A. baumannii ATCC 19606;

[0038] (b) Acinetobacter baumannii multi-drug resistant (MDR) A. baumannii BAA-1605;

[0039] Figure 4 This is a schematic diagram showing the results of the mammalian cell toxicity assay of the antimicrobial peptide cAMP102 in an embodiment of the present invention;

[0040] Figure 5 This is a schematic diagram showing the hemolytic toxicity assay results of the antimicrobial peptide cAMP102 in an embodiment of the present invention. Detailed Implementation

[0041] The technical solutions of the embodiments of the present invention will be clearly and completely described below with reference to the accompanying drawings. Obviously, the described embodiments are only some embodiments of the present invention, and not all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those skilled in the art without creative effort are within the scope of protection of the present invention.

[0042] It should be noted that the terms "first," "second," etc., in the specification, claims, and accompanying drawings of this invention are used to distinguish similar objects and are not necessarily used to describe a specific order or sequence. It should be understood that such data can be interchanged where appropriate so that the embodiments of the invention described herein can be implemented in orders other than those illustrated or described herein. Furthermore, the terms "comprising" and "having," and any variations thereof, are intended to cover non-exclusive inclusion; for example, a process, method, system, product, or server that comprises a series of steps or units is not necessarily limited to those steps or units explicitly listed, but may include other steps or units not explicitly listed or inherent to such processes, methods, products, or devices.

[0043] In this document, the term "composition" generally refers to a unit dose form and can be prepared by any method well known in the pharmaceutical industry. All methods involve the step of combining the active ingredient with a carrier constituting one or more adjunct components. Typically, compositions are prepared by uniformly and adequately combining an active antibody or antigen-binding fragment with a liquid carrier, a finely fragmented solid carrier, or both.

[0044] This invention utilizes the Extreme Environment Microbiome Catalogue (EEMC) database constructed by the Sanya BGI Life Sciences Research Institute to screen for novel antimicrobial peptides. First, antiSMASH (v7.0) software (Kai Blin, Simon Shaw, Hannah E Augustijn, et al., antiSMASH 7.0: new and improved predictions for detection, regulation, chemical structures and visualisation, Nucleic Acids Research, Volume 51, Issue W1, 5 July 2023, Pages W46–W50) was used with parameters set to minlength 5000 to identify biosynthesis gene clusters (BGCs) in archaea genomes from extreme environments. Then, a deep learning model (RNN, LSTM) was used to predict the core peptide sequences in RiPPs-type BGCs. Furthermore, three pre-trained protein language models (ESM2-3B, ESM3, PTRAS) were used to predict low-toxicity antimicrobial peptides from the obtained core peptide sequences. Peptide sequences ranking in the top 50% of each model's prediction scores were selected as candidate low-toxicity antimicrobial peptides. These candidate antimicrobial peptides were compared with known antimicrobial peptide databases, and peptide sequences identical to those in known databases were removed to obtain novel candidate low-toxicity antimicrobial peptide sequences, which were then used for further experimental verification. Species annotation of the archaea from extreme environments was obtained using GTDB-Tk (The GenomeTaxanomy Database Toolkit) and its associated R220 database. Finally, through the above steps, this invention obtained an archaea from extreme environments such as the deep sea. PL-Br10-E2g29 sp001563965 The antimicrobial peptide was named cAMP102. The following is the experimental verification process for the antimicrobial function and toxicity of this antimicrobial peptide.

[0045] In this invention, A. baumannii refers to Acinetobacter baumannii (ATCC 19606), and MDR A. baumannii refers to multidrug-resistant Acinetobacter baumannii (BAA-1605 from Shanghai Beinuo Biotechnology Co., Ltd.).

[0046] The sequences involved in this invention are shown in Table 1.

[0047] Table 1

[0048]

[0049] The technology of the present invention will be described below through specific embodiments. Where specific techniques or conditions are not specified in the embodiments, they shall be performed in accordance with the techniques or conditions described in the literature in this field or according to the product instructions. Reagents or instruments whose manufacturers are not specified are all conventional products that can be obtained commercially.

[0050] Example 1: Synthesis and purification of the antimicrobial peptide cAMP102

[0051] The antimicrobial peptide cAMP102 in Table 1 was chemically synthesized by Shanghai Sangon Biotech Co., Ltd. using a solid-phase peptide synthesis method based on its amino acid sequence (SEQ ID NO: 1). The purity of the antimicrobial peptide was then determined by high-performance liquid chromatography (HPLC), and the accurate molecular weight of cAMP102 was detected using liquid chromatography-mass spectrometry (LC-MS). The specific experimental procedures are as follows:

[0052] 1.1 Determination of the purity of the antimicrobial peptide cAMP102 by high performance liquid chromatography (HPLC)

[0053] HPLC column model: SHIMADZU shim-pack GIST (4.6*250mm*5UM);

[0054] Mobile phase A: Deionized water containing 0.1% trifluoroacetic acid (TFA);

[0055] Mobile phase B: Acetonitrile containing 0.1% trifluoroacetic acid (TFA);

[0056] Sample to be tested: Dissolve 0.5 mg of antimicrobial peptide cAMP102 in 10% acetonitrile and 90% water to make 0.5 mL.

[0057] Measurement method: The total flow rate of the mobile phase was fixed at 1 mL / min, and the detection wavelength was 214 nm. From 0 to 20 minutes, the gradient of mobile phase B was linearly increased (20%–80%), while the gradient of mobile phase A was linearly decreased (80%–20%). 30 μL of the sample was injected, and the detection signal was recorded. The results are as follows: Figure 1 As shown.

[0058] from Figure 1 The results show that the purity of the synthesized antimicrobial peptide cAMP102 is greater than 95%.

[0059] 1.2 Determination of the molecular weight of the antimicrobial peptide cAMP102 by liquid chromatography-mass spectrometry (LC-MS)

[0060] Mass spectrometer: Shimadzu LC-MS-2020;

[0061] Mobile phase: 50% water / 50% methanol;

[0062] The sample to be tested was prepared by dissolving 0.1 mg of the antimicrobial peptide cAMP102 in 50% acetonitrile and 50% water to make 0.5 mL.

[0063] Detection method: The atomizing gas flow rate was set to 1.50 L / min, CDL temperature to 250℃, CDL voltage to 0 V, module temperature to 200℃, rod tip deviation to +4.5 kV, detector voltage to -0.2 kV, and T.Flow to 0.2 mL / min. 1 μL of the sample was injected, and the detection signal was recorded. The results are as follows: Figure 2 As shown.

[0064] The amino acid sequence of the antimicrobial peptide cAMP102 is STATICIGRVSRSSTSERSARLRTVS (SEQ ID No. 1). Its theoretical molecular weight is 2782.123. From... Figure 2 The mass spectrometry results shown indicate that the molecular weight of the antimicrobial peptide cAMP102 synthesized in this embodiment is consistent with the theoretical molecular weight.

[0065] Example 2: Activity Analysis of Antimicrobial Peptides

[0066] 2.1 Determination of Minimum Inhibitory Concentration (MIC)

[0067] Acinetobacter baumannii A. baumannii and multidrug-resistant Acinetobacter baumannii MDR A. baumannii Two bacterial strains were streaked on Luriae–Bertani (LB) agar and incubated overnight at 37°C.

[0068] Single colonies of the two bacterial strains were inoculated into Mueller-Hinton Broth (MHB) liquid medium (Thermo Fisher Scientific Inc.) and cultured overnight with shaking at 37°C and 120 rpm. The next day, the overnight culture was diluted 1:100 with fresh MHB and cultured until the exponential growth phase (OD200). 600(0.4~0.6). Subsequently, the bacterial suspension was diluted to a final concentration of 1×10⁻⁶ using sterile MHB. 6 CFU / mL available for use.

[0069] In the antimicrobial activity assay, the antimicrobial peptide cAMP102 was first serially diluted twice using MHB medium to prepare working solutions with concentrations ranging from 0.5, 1, 2, 4, 8, 16, 32, 64, 128, to 256 μM. The dilution procedure was as follows: first, the highest concentration working solution (128 μM) was prepared, and then each solution was diluted 1:1 with an equal volume of MHB to form a series of consecutive twice-dose concentrations. Each concentration gradient of cAMP102 solution (100 μL) was mixed with an equal volume of diluted bacterial culture (100 μL) and added to a 96-well microplate to ensure that the final reaction system covered the antimicrobial peptide concentration gradient from 0.5 to 256 μM. The experimental groups included:

[0070] Negative control group: 100 μL MHB and 100 μL bacterial culture were added, without the addition of antimicrobial peptides;

[0071] Blank control group: 200 μL of MHB was added, without bacterial culture and antimicrobial peptides;

[0072] Antimicrobial peptide group: a mixture of diluted antimicrobial peptide solution and bacterial culture, with final antimicrobial peptide concentrations ranging from 0.5, 1, 2, 4, 8, 16, 32, 64, 128, to 256 μM.

[0073] After incubation at 37°C for 16-18 hours, the MIC value was determined. The MIC value is the lowest concentration of antimicrobial peptide at which no bacterial growth was observed visually. All experiments were repeated 3 times. This method is a routine method in the field and will not be described in detail here.

[0074] Figure 3 Experimental results showed that the antimicrobial peptide cAMP102 had an effect on... A. baumannii (a) has a MIC of 64 μM and a response to MDR. A. baumannii (b) has a MIC of 128 μM.

[0075] 2.2 Mammalian cytotoxicity assay

[0076] To evaluate the potential toxicity of the candidate antimicrobial peptide cAMP102 to mammalian cells, four experimental treatments were set up: blank control group, negative control group (PBS group), positive control group (cisplatin treatment group), and experimental group (cAMP102 treatment group). The antimicrobial peptide solution was prepared with sterile PBS buffer at a concentration of 60 μM.

[0077] The cells used in the experiment included L-02 normal human hepatocytes (Beina Biotechnology) and HEK-293T human embryonic kidney cells (Pronosei Biotechnology). After trypsin digestion, the cells were resuspended in DMEM medium (Gibco, USA) containing 10% fetal bovine serum (FBS, catalog number 04-001-1ACS, Biological Industries, Israel) to prepare a single-cell suspension, and the cell density was adjusted to 5 × 10⁶ cells / year. 4 Cells / mL. Cells from each treatment group were seeded into 96-well culture plates, with 90 μL of cell suspension added to each well. Only the control group received no cells, but only 100 μL of FBS-DMEM culture medium. After seeding, the cells were incubated in a 5% CO2, 37°C incubator for 24 hours to promote cell adhesion. After 24 hours, the following treatments were performed for each group:

[0078] Negative control group (Control): 10 μL of PBS was added to each well;

[0079] Positive control group (cisplatin): 10 μL of pre-prepared cisplatin solution (catalog number D8810, Solarbio) was added to each well to make the final concentration 60 μM;

[0080] Experimental group (cAMP102): 10 μL of antimicrobial peptide cAMP102 solution was added to each well to make the final concentration 60 μM;

[0081] The blank group remained in its original state without any treatment fluid being added.

[0082] After treatment, incubation continued for 48 hours. Then, the culture medium and treatment solution in the wells were discarded, and 100 μL of CCK-8 assay reagent diluted 10-fold with DMEM (final concentration 10% (v / v), catalog number BS350A, BaiSha Biotechnology) was added to each well. Incubation continued for 1 hour in a 5% CO2, 37°C environment under dark conditions. After incubation, absorbance (OD value) was measured at 450 nm using a microplate reader, and the raw data results were recorded. The formula for calculating the mammalian cell inhibition rate is (OD...). Control - OD cAMP102 / 顺铂 ) / (OD Control - OD Blank () × 100%, and all experiments were repeated 3 times.

[0083] Figure 4 The results showed that the antimicrobial peptide cAMP102 group had a lower inhibition rate and significantly lower mammalian cytotoxicity compared to the positive control group (cisplatin group). The antimicrobial peptide cAMP102 showed a 0% inhibition rate against L-02 human hepatocytes and a 7.38% inhibition rate against 293T human embryonic kidney cells.

[0084] 2.3 Hemolytic toxicity assay

[0085] To evaluate the hemolytic activity of the candidate antimicrobial peptide cAMP102, this experiment included three treatment groups: a blank group (Blank), a positive control group (Triton X-100 group), and an experimental group (cAMP102 group). The red blood cells used in the experiment were obtained from fresh defibrinated sheep blood (Bickman Biotechnology, China). The plasma and red blood cells were separated by centrifugation at 1500 rpm for 10 minutes, and the plasma fraction was discarded. The obtained red blood cells were washed repeatedly with sterile PBS buffer 3-4 times until the supernatant was clear and transparent to remove residual plasma and other components. The washed red blood cells were resuspended in PBS to prepare a 4% (v / v) red blood cell suspension. 100 μL of the red blood cell suspension was added to each well of a 96-well plate, followed by the following treatment:

[0086] Blank group: 100 μL of PBS buffer without any hemolysing agent was added to each well;

[0087] Positive control group (Triton X-100, Control): Triton X-100 (final concentration 1%) was added to each well to induce complete hemolysis;

[0088] Experimental group (cAMP102): Add candidate antimicrobial peptide cAMP102 solution to each well to achieve a final concentration of 60 μM.

[0089] After processing, the 96-well plate was incubated at 37°C for 1 hour. After incubation, the plate was centrifuged at 1500 rpm for 10 minutes at 4°C, and the supernatant from each well was collected into a new 96-well plate. The absorbance (OD) was then measured at 570 nm using a microplate reader, and the raw data were recorded. The hemolysis rate was calculated using the formula (OD). cAMP102 - OD Blank ) / (OD Control -OD Blank () × 100%, and all experiments were repeated 4 times.

[0090] Figure 5 The results showed that, compared with the positive control group, the antimicrobial peptide cAMP102 group had a lower OD value and significantly lower hemolytic toxicity. The calculated hemolysis rate of the antimicrobial peptide cAMP102 was 2.32%.

[0091] In the description of this specification, the references to terms such as "one embodiment," "some embodiments," "example," "specific example," or "some examples," etc., refer to specific features, structures, materials, or characteristics described in connection with that embodiment or example, which are included in at least one embodiment or example of the present invention. In this specification, the illustrative expressions of the above terms do not necessarily refer to the same embodiment or example. Furthermore, the specific features, structures, materials, or characteristics described may be combined in any suitable manner in one or more embodiments or examples. Moreover, without contradiction, those skilled in the art can combine and integrate the different embodiments or examples described in this specification, as well as the features of different embodiments or examples.

[0092] Although embodiments of the present invention have been shown and described above, it is understood that the above embodiments are exemplary and should not be construed as limiting the present invention. Those skilled in the art can make changes, modifications, substitutions and variations to the above embodiments within the scope of the present invention.

Claims

1. An isolated polypeptide, characterized in that, Its amino acid sequence is shown in SEQ ID NO:

1.

2. The isolated polypeptide according to claim 1, characterized in that, The isolated polypeptides are derived from PL-Br10- E2g29 sp001563965 Archaeal strains.

3. A nucleic acid molecule, characterized in that, The nucleic acid molecule encodes the isolated polypeptide according to any one of claims 1 to 2, and the nucleotide sequence of the nucleic acid molecule is shown in SEQ ID NO:

2.

4. A composition, characterized in that, The composition comprises the isolated polypeptide as described in any one of claims 1 to 2.

5. The use of the isolated polypeptide according to any one of claims 1-2, the nucleic acid molecule according to claim 3, or the composition according to claim 4 in the preparation of products and / or pharmaceuticals, characterized in that, The product and / or drug are used to inhibit the growth of pathogens and / or kill pathogens, wherein the pathogen is Acinetobacter baumannii.

6. The use according to claim 5, characterized in that, The pathogen is multidrug-resistant Acinetobacter baumannii.

7. A method for inhibiting the growth of pathogens and / or killing pathogens in vitro, characterized in that, include: The isolated polypeptide of any one of claims 1 to 2 or the composition of claim 4 is contacted with the sample to be treated, wherein the sample to be treated contains the pathogen, and the pathogen is Acinetobacter baumannii.

8. The method according to claim 7, characterized in that, The pathogen is multidrug-resistant Acinetobacter baumannii.

9. The method according to claim 7, characterized in that, The minimum inhibitory concentration of the polypeptide against Acinetobacter baumannii is 64 μM.

10. The method according to claim 8, characterized in that, The minimum inhibitory concentration of the polypeptide against multidrug-resistant Acinetobacter baumannii is 128 μM.

11. A daily necessity and / or care product, characterized in that, The daily necessities and / or care products include the isolated polypeptides as described in any one of claims 1 to 2 as active ingredients.

12. The daily necessities and / or care products according to claim 11, characterized in that, The daily necessities include at least one selected from hand sanitizer, shower gel, shampoo, mouthwash, toothpaste, soap, cosmetics, feminine wash, laundry soap, laundry detergent, laundry powder, dish soap, spray, ointment, gel base, disinfectant, and toilet cleaner; and / or the care products include at least one of sanitary napkins, diapers, and incontinence pads.

13. An antibacterial additive, characterized in that, The antibacterial additive includes the isolated polypeptide as described in any one of claims 1 to 2.

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