CN113150106B - Antibacterial peptide derived from complement component C5a and application thereof - Google Patents
Antibacterial peptide derived from complement component C5a and application thereof Download PDFInfo
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- CN113150106B CN113150106B CN202110454244.7A CN202110454244A CN113150106B CN 113150106 B CN113150106 B CN 113150106B CN 202110454244 A CN202110454244 A CN 202110454244A CN 113150106 B CN113150106 B CN 113150106B
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Abstract
The invention discloses an antibacterial peptide derived from a complement component C5a and application thereof, belonging to the technical field of antibacterial preparations, wherein the amino acid sequence of the antibacterial peptide is shown in any one of sequence tables SEQ ID NO. 1-8. The invention synthesizes several overlapping peptides of 29-35 amino acids from N end to C end of complement component C5a of representative vertebrate in three segments, and utilizes agar diffusion method to screen, and according to the existence and diameter of bacteriostatic circle, 8 antibacterial peptides with antibacterial activity are obtained by screening, which has high antibacterial activity for colibacillus and/or Edwardsiella cati, can be used for preparing antibacterial agent or antibacterial drug, and has wide application prospect, and the antibacterial peptides also have the characteristics of small molecular weight, simple synthesis, and good application value.
Description
Technical Field
The invention belongs to the technical field of antibacterial preparations, and particularly relates to an antibacterial peptide derived from a complement component C5a and application thereof.
Background
In recent years, due to the use of a large amount of traditional antibiotics, the drug resistance of pathogenic bacteria is more prominent, which poses a great threat to the health of human beings and cultured animals. Therefore, researchers are eagerly engaged in the development of novel antibacterial agents.
Antimicrobial peptides (AMPs) are the earliest immunologically active molecules produced by organisms in order to adapt to the environment during long-term evolution, are important mediators of natural immunity, and play an extremely important role in host immune defense against pathogenic invasion. The antibacterial peptide is considered as one of the best substitutes of antibiotics due to the characteristics of thermal stability, difficult generation of drug resistance, stable effect and the like, and has wide application prospect for disease prevention and control. The complement system is an important component of the vertebrate immune system, and its activation produces the homologous small molecules C3a, C4a, and C5 a. Research shows that C3a and C4a from human have antibacterial peptide activity, but C5a does not have the antibacterial peptide activity, and whether the complement component C5a of other vertebrates has antibacterial activity or not is yet to be researched.
Disclosure of Invention
The invention aims to provide an antibacterial peptide derived from a complement component C5a and application thereof. The invention synthesizes a plurality of C5a overlapping peptides (with the length of about 29-35 amino acids) of representative vertebrates from N end to C end respectively in three segments, screens by an agar diffusion method, screens 8 antibacterial peptides with antibacterial activity from a complement component C5a of the representative vertebrates according to the existence and the diameter of an antibacterial ring, and part of the antibacterial peptides have high antibacterial activity to escherichia coli and Edwardsiella cati, can be used for preparing antibacterial agents, have the characteristics of small molecular weight and simple synthesis, and have better application value.
In order to achieve the purpose, the invention adopts the technical scheme that:
the invention provides an antibacterial peptide derived from a complement component C5a, and the amino acid sequence of the antibacterial peptide is shown in any one of sequence tables SEQ ID NO. 1-8.
Further, the amino acid sequence as shown in SEQ ID No.1-8 of the sequence Listing is an overlapping peptide from N-terminus to C-terminus of vertebrate complement component C5 a.
The invention also provides application of the antibacterial peptide derived from the complement component C5a in antibiosis.
Further, the application of the antibacterial peptide derived from the complement component C5a as shown in any one of the sequence table SEQ ID NO.1-8 in resisting Escherichia coli.
Further, the application of the antibacterial peptide derived from the complement component C5a as shown in any one of the sequence tables SEQ ID NO.1-5 and SEQ ID NO.7-8 in the anti-Edwardsiella catis provided.
Further, an antibacterial peptide having antibacterial activity was screened by the agar diffusion method.
Further, the agar diffusion method comprises:
s1, strain activation: taking a strain which is frozen and preserved, carrying out streak inoculation culture on a plate, selecting a single colony, inoculating the single colony into a liquid culture medium, culturing to a logarithmic phase, collecting thalli, and preparing a bacterial liquid;
s2, preparing bacteriostatic agar plates: adding the bacterial liquid obtained in the step S1 into a sterile culture medium containing agar, uniformly mixing, pouring into a flat plate, solidifying, punching by using a sterilization puncher, respectively adding antibacterial peptides shown in SEQ ID NO.1-8 of a sequence table into the holes, and incubating to diffuse the polypeptides;
s3, measurement of bacteriostatic diameter: and (5) culturing the bacteriostatic agar prepared in the step (S2) on a flat plate, then determining the diameter of the bacteriostatic circle, and judging the antibacterial activity by using the diameter of the bacteriostatic circle.
Further, the antimicrobial peptide is added to the pores in the step S2 at a concentration of 125 μ M.
The invention also provides application of the antibacterial peptide derived from the complement component C5a in preparation of antibacterial agents or antibacterial drugs.
Further, the dosage form of the antibacterial agent or the antibacterial drug comprises: topical ointment, topical liquid, oral tablet, oral liquid, disinfectant or cleanser.
Compared with the prior art, the invention has the beneficial effects that: in order to excavate the antibacterial activity of a complement component C5a of a vertebrate, a plurality of representative vertebrates are selected, overlapping peptides (about 29-35 amino acids in length) of C5a of the representative vertebrates are synthesized from the N end to the C end in three sections respectively, screening is carried out by using an agar diffusion method, and 8 antibacterial peptides with antibacterial activity are obtained by co-screening according to the existence and the diameter of an antibacterial ring.
Drawings
FIG. 1 shows the statistics of the detection of the anti-Escherichia coli activity of the polypeptide in example 2 of the present invention;
FIG. 2 is the statistic result of the detection of the activity of the polypeptide against Edwardsiella cati in example 3 of the invention.
Detailed Description
The technical solution of the present invention will be clearly and completely described below with reference to the embodiments of the present invention. It is to be understood that the described embodiments are merely exemplary of the invention, and not restrictive of the full scope of the invention. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
EXAMPLE 1 Synthesis of polypeptide
Selecting 6 representative vertebrate animals, mice, cattle, chicken, Xenopus laevis and zebra fish, respectively synthesizing overlapping peptides from the N end to the C end in three sections according to the amino acid sequence of the complement component C5a disclosed on NCBI, wherein the fragment length of each polypeptide is about 29-35 amino acids, entrusting Gill Biochemical (Shanghai) Limited company to synthesize, and selecting the polypeptide with the purity of more than 95% by mass spectrometry and liquid chromatography analysis, wherein the name, the source and the amino acid sequence of each polypeptide are shown in Table 1.
TABLE 1 amino acid sequence of artificially synthesized polypeptide
Example 2 detection of polypeptide Activity against Escherichia coli by agar diffusion
(1) And (3) activation of strains: coli ATCC 25922 strain, which was cryopreserved at-80 ℃ was streaked on a TSA solid medium, and after culturing at 37 ℃ for 24 hours, a single colony on the TSA plate was selected and inoculated into 5mL of TSB medium at a mass-to-volume ratio of 3%, and shaken to log phase (about 3 to 5 hours). Centrifuging at 5000g for 10min, discarding the supernatant culture medium, and collecting thallus. Washing thallus once with 10mM Tris buffer (pH7.4), centrifuging for 10min at 5000g, re-suspending with 10mM Tris buffer to obtain bacterial liquid, and regulating bacterial liquid concentration to 8 × 10 7 CFU/mL, ice bath for standby.
(2) Preparing a bacteriostatic agar plate: adding 0.03g of TSB medium and 1g of agar (Low EEO agar) to 100ml of MilliQ water, adjusting pH to 7.4, and autoclaving; adding Tween20 to final concentration of 0.02% after temperature is reduced, mixing, adding 1mL of the above 8 × 10 7 Fully and uniformly mixing CFU/mL bacterial liquid; sucking 5mL of the culture medium containing the bacterial liquid into a flat plate with the diameter of 90mm, and punching a hole with the diameter of 4mm by using a sterilization puncher after agar is solidified; adding 6 μ L of 125 μ M polypeptide per well, and incubating at 37 deg.C for 3h to diffuse the polypeptide; 5mL of sterilized upper agar (ingredients including: 6% by volume TSB medium, 1% by volume Low EE0 agar, pH7.4) was added.
(3) And (3) measuring the bacteriostatic diameter: culturing at 37 deg.C for 20h, measuring the diameter of the zone, and determining the antibacterial activity by the diameter of the zone.
The determination statistics result is shown in figure 1, and according to the detection result of figure 1, wherein only a part of polypeptides have activity of inhibiting escherichia coli, and are polypeptide mmC5a-1 (shown as sequence table SEQ ID No. 1) and polypeptide mmC5a-3 (shown as sequence table SEQ ID No. 2) derived from mouse C5a, polypeptide btC5a-1 (shown as sequence table SEQ ID No. 3) and polypeptide btC5a-3 (shown as sequence table SEQ ID No. 4) derived from bovine C5a, polypeptide ggC5a-2 (shown as sequence table SEQ ID No. 5) and polypeptide ggC5a-3 (shown as sequence table SEQ ID No. 6) derived from chicken C5a, polypeptide xtC5a-1 (shown as sequence table SEQ ID No. 7) derived from xenopus laevis C5a and polypeptide drC5a-2 (shown as sequence table SEQ ID No. 8) derived from zebra fish C5a, respectively. Wherein the polypeptides mmC5a-1 and drC5a-2 have relatively high activity of inhibiting Escherichia coli.
Example 3 detection of polypeptide Activity against Edwardsiella cati by agar diffusion
(1) Activation of strains: the strain HSN-1 of the Edwardsiella cati preserved in a freezing way at the temperature of minus 80 ℃ is taken and plated on a TSA solid culture medium in a streak way, after the strain is cultured for 24 hours at the temperature of 28 ℃, a single colony on the TSA plate is selected and inoculated into 5mL of TSB culture medium with the mass volume ratio of 3 percent, and the strain is shaken to the logarithmic phase (about 3 to 5 hours). Centrifuging at 5000g for 10min, discarding the supernatant culture medium, and collecting thallus. Washing thallus once with 10mM Tris buffer (pH7.4), centrifuging for 10min at 5000g, re-suspending with 10mM Tris buffer to obtain bacterial liquid, and regulating bacterial liquid concentration to 4 × 10 8 CFU/mL, ice bath for standby.
(2) Preparing a bacteriostatic agar plate: adding 0.03g of TSB medium and 1g of agar (Low EEO agar) to 100ml of MilliQ water, adjusting pH to 7.4, and autoclaving; adding Tween20 to final concentration of 0.02% after temperature is reduced, mixing, adding 1mL of the above 4 × 10 8 Fully and uniformly mixing CFU/mL bacterial liquid; sucking 5mL of the culture medium containing the bacterial liquid into a flat plate with the diameter of 90mm, and punching a hole with the diameter of 4mm by using a sterilization puncher after agar is solidified; adding 6 μ L of 125 μ M polypeptide per well, and incubating at 28 deg.C for 3h to diffuse the polypeptide; 5mL of sterilized upper agar (ingredients including: 6% by volume TSB medium, 1% by volume Low EE0 agar, pH7.4) was added.
(3) And (3) measuring the bacteriostatic diameter: culturing at 28 deg.C for 20h, measuring the diameter of the zone, and determining the antibacterial activity by the diameter of the zone.
The determination statistics result is shown in figure 1, and according to the detection result of figure 1, wherein only a part of polypeptides have the activity of inhibiting the catfish edwardsiella, respectively, polypeptide mmC5a-1 (shown in sequence table SEQ ID No. 1) and polypeptide mmC5a-3 (shown in sequence table SEQ ID No. 2) derived from mouse C5a, polypeptide btC5a-1 (shown in sequence table SEQ ID No. 3) and polypeptide btC5a-3 (shown in sequence table SEQ ID No. 4) derived from cow C5a, polypeptide ggC5a-2 (shown in sequence table SEQ ID No. 5) derived from chicken C5a, polypeptide xtC5a-1 (shown in sequence table SEQ ID No. 7) derived from xenopus C5a, and polypeptide drC5a-2 (shown in sequence table SEQ ID No. 8) derived from zebrafish C5 a. Wherein the polypeptide mmC5a-1 has relatively high activity of inhibiting Edwardsiella cati.
The above description is only for the preferred embodiment of the present invention, but the scope of the present invention is not limited thereto, and any changes or substitutions that can be easily conceived by those skilled in the art within the technical scope of the present invention are included in the scope of the present invention.
Sequence listing
<110> university of agriculture in Huazhong
<120> antibacterial peptide derived from complement component C5a and use thereof
<160> 8
<170> SIPOSequenceListing 1.0
<210> 1
<211> 32
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 1
Asn Leu His Leu Leu Arg Gln Lys Ile Glu Glu Gln Ala Ala Lys Tyr
1 5 10 15
Lys His Ser Val Pro Lys Lys Cys Cys Tyr Asp Gly Ala Arg Val Asn
20 25 30
<210> 2
<211> 33
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 2
Thr Ile Gly Pro Leu Cys Ile Arg Ala Phe Asn Glu Cys Cys Thr Ile
1 5 10 15
Ala Asn Lys Ile Arg Lys Glu Ser Pro His Lys Pro Val Gln Leu Gly
20 25 30
Arg
<210> 3
<211> 30
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 3
Met Leu Lys Lys Lys Ile Glu Glu Glu Ala Ala Lys Tyr Arg Asn Ala
1 5 10 15
Trp Val Lys Lys Cys Cys Tyr Asp Gly Ala His Arg Asn Asp
20 25 30
<210> 4
<211> 33
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 4
Gln Ala Gly Pro Ile Cys Ile Lys Ala Phe Lys Ser Cys Cys Ala Ile
1 5 10 15
Ala Ser Gln Phe Arg Ala Asp Glu His His Lys Asn Met Gln Leu Gly
20 25 30
Arg
<210> 5
<211> 31
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 5
Met His Gly Val Lys Ala Tyr Pro Val Ser Glu Thr Cys Ser Asp Arg
1 5 10 15
Ala Arg Arg Ile Gln Ser His Ala Lys Cys Val Ser Ala Phe Arg
20 25 30
<210> 6
<211> 33
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 6
Gln Ser His Ala Lys Cys Val Ser Ala Phe Arg His Cys Cys Glu Phe
1 5 10 15
Ala Asn Arg Leu Arg Glu Glu Glu Pro Ser Lys Leu Leu Ile Leu Ala
20 25 30
Arg
<210> 7
<211> 32
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 7
Ser Phe Asn Phe Lys Glu Glu Ile Asn Lys Lys Ala Arg Val Tyr Lys
1 5 10 15
Asp Arg Asn Ile Arg Lys Cys Cys Tyr Asp Gly Val Lys Cys Phe Leu
20 25 30
<210> 8
<211> 35
<212> PRT
<213> Artificial Sequence (Artificial Sequence)
<400> 8
Thr Arg Ser Ser Pro Thr Leu Glu Thr Cys Lys Asp Arg Ala Asn Arg
1 5 10 15
Val Thr Leu Pro Asn Lys Lys Thr Arg Arg Asp Tyr Glu Lys Glu Lys
20 25 30
Tyr Cys Arg
35
Claims (3)
1. The antibacterial peptide derived from a complement component C5a is characterized in that the amino acid sequence of the antibacterial peptide is shown in a sequence table SEQ ID NO. 1.
2. Use of an antimicrobial peptide derived from complement component C5a according to claim 1 in the manufacture of an antibacterial agent or medicament against e.
3. The use according to claim 2, wherein the antimicrobial agent or antimicrobial drug is in a dosage form comprising: topical ointment, topical liquid, oral tablet, oral liquid, disinfectant or cleanser.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1142854A (en) * | 1993-12-06 | 1997-02-12 | 西巴-盖尔基股份公司 | C5a receptor antagonists having substantially no agonist activity |
| CN105541987A (en) * | 2016-02-24 | 2016-05-04 | 中国科学院海洋研究所 | Recombinant protein of cynoglossus semilaevis complement component C5a and application thereof |
| CA3038502A1 (en) * | 2016-09-27 | 2018-04-05 | Caris Science, Inc. | Oligonucleotide probes and uses thereof |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9518265B2 (en) * | 2012-01-10 | 2016-12-13 | Noxxon Pharma Ag | C5a binding nucleic acids |
-
2021
- 2021-04-26 CN CN202110454244.7A patent/CN113150106B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1142854A (en) * | 1993-12-06 | 1997-02-12 | 西巴-盖尔基股份公司 | C5a receptor antagonists having substantially no agonist activity |
| CN105541987A (en) * | 2016-02-24 | 2016-05-04 | 中国科学院海洋研究所 | Recombinant protein of cynoglossus semilaevis complement component C5a and application thereof |
| CA3038502A1 (en) * | 2016-09-27 | 2018-04-05 | Caris Science, Inc. | Oligonucleotide probes and uses thereof |
Non-Patent Citations (5)
| Title |
|---|
| "Chain A, Complement C5";Schatz-Jakobsen,J.A.等;《genbank》;20201201;ACCESSION NO.4P3A_A * |
| "Complement activation links inflammation to dental tissue regeneration";Madison Bergmann 等;《Clinical Oral Investigations》;20201013;第24卷;第4185–4196页 * |
| "Distinctive structural hallmarks and biological activities of the multiple cathelicidin antimicrobial peptides in a primitive teleost fish";Xu-Jie Zhang 等;《J Immunol》;20150415;第194卷(第10期);第4974-4987页 * |
| "罗非鱼hepcidin 1-5成熟肽在毕赤酵母中的表达和活性研究";梁盈 等;《动物医学进展》;20140731;第35卷(第7期);第38-43页 * |
| "鱼类体液免疫因子研究进展";张永安 等;《水产学报》;20000831;第24卷(第4期);第376-381页 * |
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