CN114409750B - Bacteriocin A3 and application thereof - Google Patents
Bacteriocin A3 and application thereof Download PDFInfo
- Publication number
- CN114409750B CN114409750B CN202210122031.9A CN202210122031A CN114409750B CN 114409750 B CN114409750 B CN 114409750B CN 202210122031 A CN202210122031 A CN 202210122031A CN 114409750 B CN114409750 B CN 114409750B
- Authority
- CN
- China
- Prior art keywords
- bacteriocin
- staphylococcus aureus
- application
- polypeptide
- synthesis method
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108010062877 Bacteriocins Proteins 0.000 title claims abstract description 42
- 241000191967 Staphylococcus aureus Species 0.000 claims abstract description 22
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 2
- 239000000022 bacteriostatic agent Substances 0.000 claims description 6
- 239000003814 drug Substances 0.000 claims description 6
- 230000002401 inhibitory effect Effects 0.000 claims description 5
- 208000035473 Communicable disease Diseases 0.000 claims description 3
- 239000003085 diluting agent Substances 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 2
- 229920001184 polypeptide Polymers 0.000 abstract description 8
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 8
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 8
- 108090000623 proteins and genes Proteins 0.000 abstract description 6
- 241000894006 Bacteria Species 0.000 abstract description 5
- 230000000844 anti-bacterial effect Effects 0.000 abstract description 5
- 230000015572 biosynthetic process Effects 0.000 abstract description 3
- 235000013305 food Nutrition 0.000 abstract description 3
- 238000003786 synthesis reaction Methods 0.000 abstract description 3
- 229940124350 antibacterial drug Drugs 0.000 abstract description 2
- 239000007791 liquid phase Substances 0.000 abstract description 2
- 231100000053 low toxicity Toxicity 0.000 abstract description 2
- 238000000034 method Methods 0.000 abstract description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 abstract description 2
- 238000001308 synthesis method Methods 0.000 abstract description 2
- 239000003139 biocide Substances 0.000 abstract 1
- 230000002949 hemolytic effect Effects 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 206010041925 Staphylococcal infections Diseases 0.000 description 3
- 210000003743 erythrocyte Anatomy 0.000 description 3
- 239000002504 physiological saline solution Substances 0.000 description 3
- 238000004321 preservation Methods 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 206010018910 Haemolysis Diseases 0.000 description 2
- RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 230000000845 anti-microbial effect Effects 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000008588 hemolysis Effects 0.000 description 2
- 208000015688 methicillin-resistant staphylococcus aureus infectious disease Diseases 0.000 description 2
- 229960003085 meticillin Drugs 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 description 2
- DRDWXKWUSIKKOB-PJODQICGSA-N Arg-Trp-Ala Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](C)C(O)=O DRDWXKWUSIKKOB-PJODQICGSA-N 0.000 description 1
- 206010053555 Arthritis bacterial Diseases 0.000 description 1
- DJCAHYVLMSRBFR-QXEWZRGKSA-N Asp-Met-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@H](CCSC)NC(=O)[C@@H](N)CC(O)=O DJCAHYVLMSRBFR-QXEWZRGKSA-N 0.000 description 1
- 241000193755 Bacillus cereus Species 0.000 description 1
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 1
- 208000031729 Bacteremia Diseases 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- SWQALSGKVLYKDT-ZKWXMUAHSA-N Gly-Ile-Ala Chemical compound NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O SWQALSGKVLYKDT-ZKWXMUAHSA-N 0.000 description 1
- SWQALSGKVLYKDT-UHFFFAOYSA-N Gly-Ile-Ala Natural products NCC(=O)NC(C(C)CC)C(=O)NC(C)C(O)=O SWQALSGKVLYKDT-UHFFFAOYSA-N 0.000 description 1
- REJKOQYVFDEZHA-SLBDDTMCSA-N Ile-Asp-Trp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)O)N REJKOQYVFDEZHA-SLBDDTMCSA-N 0.000 description 1
- SVBAHOMTJRFSIC-SXTJYALSSA-N Ile-Ile-Asn Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(=O)N)C(=O)O)N SVBAHOMTJRFSIC-SXTJYALSSA-N 0.000 description 1
- 208000004575 Infectious Arthritis Diseases 0.000 description 1
- FLCMXEFCTLXBTL-DCAQKATOSA-N Lys-Asp-Arg Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N FLCMXEFCTLXBTL-DCAQKATOSA-N 0.000 description 1
- KYNNSEJZFVCDIV-ZPFDUUQYSA-N Lys-Ile-Asn Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(O)=O KYNNSEJZFVCDIV-ZPFDUUQYSA-N 0.000 description 1
- 208000037942 Methicillin-resistant Staphylococcus aureus infection Diseases 0.000 description 1
- 206010048723 Multiple-drug resistance Diseases 0.000 description 1
- AJHCSUXXECOXOY-UHFFFAOYSA-N N-glycyl-L-tryptophan Natural products C1=CC=C2C(CC(NC(=O)CN)C(O)=O)=CNC2=C1 AJHCSUXXECOXOY-UHFFFAOYSA-N 0.000 description 1
- 206010031252 Osteomyelitis Diseases 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 206010062255 Soft tissue infection Diseases 0.000 description 1
- BDWDMRSGCXEDMR-WFBYXXMGSA-N Trp-Ala-Asn Chemical compound C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)N BDWDMRSGCXEDMR-WFBYXXMGSA-N 0.000 description 1
- GQHAIUPYZPTADF-FDARSICLSA-N Trp-Ile-Arg Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)=CNC2=C1 GQHAIUPYZPTADF-FDARSICLSA-N 0.000 description 1
- UMPVMAYCLYMYGA-ONGXEEELSA-N Val-Leu-Gly Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(O)=O UMPVMAYCLYMYGA-ONGXEEELSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 108010078114 alanyl-tryptophyl-alanine Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000002924 anti-infective effect Effects 0.000 description 1
- 230000000941 anti-staphylcoccal effect Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000003113 dilution method Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 206010014665 endocarditis Diseases 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 238000004080 punching Methods 0.000 description 1
- 201000001223 septic arthritis Diseases 0.000 description 1
- 206010040872 skin infection Diseases 0.000 description 1
- 238000007711 solidification Methods 0.000 description 1
- 230000008023 solidification Effects 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Polymers & Plastics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Food Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- General Chemical & Material Sciences (AREA)
- Nutrition Science (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Mycology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Husbandry (AREA)
- Zoology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention belongs to the field of medical application, and particularly relates to bacteriocin A3 and application thereof. The bacteriocin A3 has an amino acid sequence shown as SEQ ID NO.1, can be synthesized by a polypeptide solid-phase synthesis method or a liquid-phase polypeptide synthesis method, and can be obtained by expressing a coding gene of the bacteriocin A3 in engineering bacteria. The novel antibacterial staphylococcus aureus killing agent has the advantages of simple structure, safety, low toxicity, easier synthesis, high efficiency of killing staphylococcus aureus, wide application prospect and the like, and can be used in the fields of antibacterial drugs, feeds, foods and the like.
Description
Technical Field
The invention belongs to the field of medical application, and particularly relates to bacteriocin A3 and application thereof.
Background
Staphylococcus aureus is the leading pathogen for infection in the world, and can cause skin and soft tissue infections, bacteremia, osteomyelitis, septic arthritis, pneumonia, endocarditis, and other diseases. More than 80% of the clinically isolated staphylococcus aureus pairs are methicillin-resistant staphylococcus aureus (MRSA), and due to their multiple drug resistance, anti-MRSA infection is increasingly becoming a hotspot and difficulty of anti-infection treatment, so new anti-MRSA drugs are urgently needed. Bacteriocins are a class of proteins or polypeptides with antibacterial activity produced by bacteria through the mechanism of ribosome synthesis. Currently, some bacillus produced bacteriocins, such as the lanthiobacterin cerecin reported in bacillus cereus as1.1846, have remarkable antibacterial activity against methicillin-resistant staphylococcus aureus (MRSA). Research shows that a large number of unidentified novel bacteriocins still exist in bacillus, and the novel bacteriocins can be identified and developed to be novel anti-MRSA medicaments, and have important development and application prospects.
Disclosure of Invention
The first object of the present invention is to provide a bacteriocin A3 having an amino acid sequence shown as SEQ ID NO. 1. The bacteriocin A3 can be synthesized by adopting a polypeptide solid-phase synthesis method or a liquid-phase polypeptide synthesis method, and the encoding gene of the bacteriocin A3 can also be obtained by expressing in engineering bacteria.
The second object of the invention is to provide the application of the bacteriocin B cin A3 in preparing a bacteriostatic agent, wherein the bacteriostatic agent inhibits staphylococcus aureus.
The third object of the invention is to provide the application of the bacteriocin A3 in preparing a medicament for treating staphylococcus aureus infectious diseases.
A fourth object of the present invention is to provide a medicament for the treatment of staphylococcus aureus infections comprising said bacteriocin A3, one or more pharmaceutically acceptable carriers, excipients and/or diluents.
A fifth object of the present invention is to provide a bacteriostatic agent for inhibiting staphylococcus aureus, comprising the bacteriocin A3.
The sixth object of the present invention is to provide a feed containing the bacteriostatic agent.
A seventh object of the present invention is to provide a food product containing the bacteriostatic agent.
The invention has the following beneficial effects:
the bacteriocin A3 provided by the invention has the advantages of simple structure, safety, low toxicity, easier synthesis and capability of killing staphylococcus aureus with high efficiency. The bacteriocin A3 provided by the invention can be used in the fields of antibacterial drugs, feeds, foods and the like, and has a wide application prospect.
Drawings
FIG. 1 is a graph showing the hemolytic activity of bacteriocin A3 in example 3.
Detailed Description
The present invention will now be described in detail with reference to the drawings and specific examples, which should not be construed as limiting the invention. Unless otherwise indicated, the technical means used in the following examples are conventional means well known to those skilled in the art, and the materials, reagents, etc. used in the following examples are commercially available unless otherwise indicated.
Example 1: obtaining bacteriocin A3
The bacteriocin provided by the invention is derived from a polypeptide sequence database of bacillus XIN-TL12B (bacillus sp. XIN-TL 2) constructed by us, the preservation number of the bacillus is CCTCC NO: M2021718, the preservation information and the preservation proof of biological material samples are shown in another patent application filed by the applicant on the same day, the application number is 202210122032.3, and the amino acid sequence (shown in SEQ ID NO. 1) is as follows: MITFLRIVAQLGARAARWAWANKDRVLGWIRDGIAIDWIINKINDMVN, as shown in SEQ ID NO.1 of the sequence Listing. Through online BlastP comparison analysis (Protein BLAST: search Protein databases using a Protein query (nih. Gov)), the bacteriocin has no homology with the amino acid sequence of the identified and reported bacteriocin, which shows that the bacteriocin is a novel bacteriocin and belongs to the first study, identification and report of the inventor. According to the amino acid sequence shown, the corresponding antimicrobial polypeptide is synthesized by Jier Biochemical (Shanghai) limited company, and the purity of the antimicrobial polypeptide is more than 95 percent.
Example 2: determination of the anti-Staphylococcus aureus Activity of bacteriocin A3
A series of gradient bacteriocin solutions (0.5,1,2,4,8. Mu.M) were prepared by a double dilution method using physiological saline as a diluent. The Minimum Inhibitory Concentration (MIC) of Bacin A3 against Staphylococcus aureus at various concentrations was determined by the agar diffusion method. Adding appropriate amount of indicator bacteria (bacterial count about 5×10) into non-coagulated agar medium 5 cfu/mL), mixing, and pouring into a plate. Staphylococcus aureus ATCC6538, staphylococcus aureus ATCC 43300, staphylococcus aureus ATCC 12600 were selected as indicator bacteria. And (5) punching by using a puncher with the aperture of 6mm after the solidification. About 50. Mu.L of sample was added to each wellThe plate is firstly placed at 4 ℃ for about 2 hours to allow the sample to be tested to fully diffuse, then placed at 30 ℃ for culturing for 12 hours, and the antibacterial effect is observed (whether a transparent antibacterial ring appears or not is observed). The minimum inhibitory concentrations of Bacin A3 were determined to be 0.5. Mu.M, 1. Mu.M for Staphylococcus aureus ATCC6538, staphylococcus aureus ATCC 43300, staphylococcus aureus ATCC 12600, respectively (Table 1).
TABLE 1 minimum inhibitory concentration of bacteriocin A3 against Staphylococcus aureus
Example 3: determination of the haemolytic Activity of bacteriocin A3
Fresh blood of healthy people (anticoagulant added) was collected, centrifuged at 3000g for 5min, and red blood cells were collected by discarding plasma. The collected erythrocytes were washed three times with physiological saline and the blood cells were resuspended at a ratio of 2% (V/V). 100 μl of red blood cell resuspension was added to a sterile 96-well cell culture plate, and bacteriocin solutions of different concentrations were added, 3 per bacteriocin concentration set in parallel. 0.1% Triton x-100 was used as a positive control for complete hemolysis and a physiological saline group was used as a negative control for non-hemolysis. Incubate at 37℃for 2h and centrifuge at 3000g for 10min. The centrifuged supernatant was transferred to a new sterile 96-well cell culture plate, and the absorbance at 570nm was detected by using an enzyme-labeled instrument to calculate the hemolytic activity of bacteriocin.
The hemolytic activity of the bacteriocin BacinA1 is shown in figure 1, and the bacteriocin only shows 1.3% of hemolytic activity at the concentration of 100 mu M, which shows that the toxic and side effects are very low.
While preferred embodiments of the present invention have been described, additional variations and modifications in those embodiments may occur to those skilled in the art once they learn of the basic inventive concepts. It is therefore intended that the following claims be interpreted as including the preferred embodiments and all such alterations and modifications as fall within the scope of the invention.
It will be apparent to those skilled in the art that various modifications and variations can be made to the present invention without departing from the spirit or scope of the invention. Thus, it is intended that the present invention also include such modifications and alterations insofar as they come within the scope of the appended claims or the equivalents thereof.
Sequence listing
<110> university of Huaibei
<120> bacteriocin A3 and use thereof
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 48
<212> PRT
<213> artificial sequence
<400> 1
Met Ile Thr Phe Leu Arg Ile Val Ala Gln Leu Gly Ala Arg Ala Ala
1 5 10 15
Arg Trp Ala Trp Ala Asn Lys Asp Arg Val Leu Gly Trp Ile Arg Asp
20 25 30
Gly Ile Ala Ile Asp Trp Ile Ile Asn Lys Ile Asn Asp Met Val Asn
35 40 45
Claims (5)
1. The bacteriocin A3 is characterized in that the amino acid sequence of the bacteriocin A3 is shown as SEQ ID NO. 1.
2. The use of bacteriocin A3 according to claim 1 for the preparation of a bacteriostatic agent, characterized in that it inhibits staphylococcus aureus.
3. Use of the bacteriocin A3 of claim 1 for the preparation of a medicament for the treatment of staphylococcus aureus infectious diseases.
4. A medicament for the treatment of staphylococcus aureus infectious diseases, characterized in that it comprises the bacteriocin A3 according to claim 1, one or more pharmaceutically acceptable carriers, excipients and/or diluents.
5. A bacteriostat for inhibiting staphylococcus aureus comprising the bacteriocin b cin A3 of claim 1.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210122031.9A CN114409750B (en) | 2022-02-09 | 2022-02-09 | Bacteriocin A3 and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210122031.9A CN114409750B (en) | 2022-02-09 | 2022-02-09 | Bacteriocin A3 and application thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN114409750A CN114409750A (en) | 2022-04-29 |
| CN114409750B true CN114409750B (en) | 2023-06-23 |
Family
ID=81279295
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202210122031.9A Active CN114409750B (en) | 2022-02-09 | 2022-02-09 | Bacteriocin A3 and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN114409750B (en) |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104762351A (en) * | 2015-04-13 | 2015-07-08 | 光明乳业股份有限公司 | Bacteriocin crude extract with bacteriostatic action, and preparation method and application thereof |
| CN105385729A (en) * | 2015-12-18 | 2016-03-09 | 广州市康优元生物科技有限公司 | Lactococcus garviea bacteriocin, preparing method thereof and application thereof |
| CN114410541A (en) * | 2022-02-09 | 2022-04-29 | 淮北师范大学 | Bacillus XIN-TL12 producing bacteriocin, product and application thereof |
-
2022
- 2022-02-09 CN CN202210122031.9A patent/CN114409750B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104762351A (en) * | 2015-04-13 | 2015-07-08 | 光明乳业股份有限公司 | Bacteriocin crude extract with bacteriostatic action, and preparation method and application thereof |
| CN105385729A (en) * | 2015-12-18 | 2016-03-09 | 广州市康优元生物科技有限公司 | Lactococcus garviea bacteriocin, preparing method thereof and application thereof |
| CN114410541A (en) * | 2022-02-09 | 2022-04-29 | 淮北师范大学 | Bacillus XIN-TL12 producing bacteriocin, product and application thereof |
Non-Patent Citations (2)
| Title |
|---|
| NCBI.aureocin A53 family class IId bacteriocin [Bacillus bingmayongensis] WP_221781903.1.NCBI.2021,ORIGIN. * |
| 王金生主编.植物病原细菌学.北京：中国农业出版社,2000,(第7-109-06344-5版),第313-314页. * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN114409750A (en) | 2022-04-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Mishra et al. | Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring temporins | |
| Cao et al. | StCT2, a new antibacterial peptide characterized from the venom of the scorpion Scorpiops tibetanus | |
| CN104151415B (en) | A kind of natural antibacterial peptide Alligatorin4 and its application | |
| WO2022268115A1 (en) | Scylla paramamosain antibacterial polypeptide spampcin 56-86 and application thereof | |
| CN104592360A (en) | Alkaline antibacterial peptide as well as targeting design and application thereof | |
| CN114478722B (en) | Bacteriocin A1 and application thereof | |
| CN114437187B (en) | Bacteriocin A4 and application thereof | |
| CN110498848B (en) | Melittin variant and application thereof | |
| CN114409750B (en) | Bacteriocin A3 and application thereof | |
| CN107141338B (en) | A kind of antibacterial peptide RW-P and preparation method thereof and application | |
| CN110305193B (en) | Anti-porphyromonas gingivalis polypeptide and application thereof | |
| CN116813712B (en) | Antibacterial peptide W33 with alpha-helical structure and rich in Trp, and preparation method and application thereof | |
| CN103288924B (en) | Catfish antimicrobial peptide mutant and preparation method thereof | |
| Tamaki et al. | Polycationic gramicidin S analogues with both high antibiotic activity and very low hemolytic activity | |
| CN104478996A (en) | New cationic antimicrobial peptide and application thereof | |
| CN115850409B (en) | Leader-free bacteriocin A3 resistant to multiple pathogenic bacteria, and preparation method and application thereof | |
| CN113603748B (en) | Beta-folded antibacterial peptide HINGE-RV and preparation method and application thereof | |
| Karimaei et al. | Antibacterial and antibiofilm activities of nisin from Lactococcus lactis and alteration of the bacteria-induced pro-inflammatory responses on kidney and bladder tumor cell lines | |
| CN110551191B (en) | Melittin with low hemolytic activity and application thereof | |
| CN115536737A (en) | Application of cobra antibacterial peptide OH-CATH30 in resisting aquatic animal pathogenic bacteria | |
| CN114702554A (en) | Application of antibacterial peptide NZX in preparation of streptococcus agalactiae antibacterial drugs | |
| CN112724198A (en) | Methicillin-resistant staphylococcus aureus-resistant antibacterial peptide and preparation method and application thereof | |
| CN111378023B (en) | Anti-streptococcus mutans polypeptide and application thereof | |
| CN109748949B (en) | Antibacterial peptide and application thereof | |
| CN117069819B (en) | Black-belly spider antibacterial peptide LC-AMP-I1 and application thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |