CN108047321B - Litopenaeus vannamei beta-1, 3-glucan binding protein antibacterial peptide and application thereof - Google Patents
Litopenaeus vannamei beta-1, 3-glucan binding protein antibacterial peptide and application thereof Download PDFInfo
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Abstract
The invention discloses a beta-1, 3-glucan binding protein antibacterial peptide of a litopenaeus vannamei, and an amino acid sequence of the antibacterial peptide is shown as a sequence table SEQ ID NO. 1. The molecular weight of the antibacterial peptide is 1810 Da. The invention also discloses application of the beta-1, 3-glucan binding protein antibacterial peptide of the litopenaeus vannamei, and application of the antibacterial peptide in preparing a medicament for treating or preventing gram-negative bacteria or gram-positive bacteria. The invention lays a foundation for further researching the defense immune mechanism of the litopenaeus vannamei and the development of antibacterial drugs.
Description
Technical Field
The invention relates to the technical field of aquaculture, in particular to a beta-1, 3-glucan binding protein antibacterial peptide of litopenaeus vannamei and application thereof.
Background
Litopenaeus vannamei (Litopenaeus vannamei), also known as Penaeus vannamei, belongs to the arthropoda, Crustacea, decapod, swimming sub-order, Paralithoidae, Paralithodes, Lito-penaeus sub-genus. The yield of the litopenaeus vannamei in the totally spherical prawn breed which is bred in a large scale accounts for the absolute advantage and accounts for 75 percent of the total yield of the global single breed breeding. With the annual increase of the culture yield of the prawns, the culture problems are gradually emerged, wherein the influence of the shrimp diseases on the industry is almost devastating, so the disease prevention and control technology is the key of the culture link. There are three main types of diseases: white spot syndrome, microsporidiosis (EHP) and early death syndrome (EMS) of prawns. In recent years, the development of antibacterial peptides capable of replacing antibiotics is becoming more important due to the drug resistance of microorganisms and water pollution caused by abuse of antibiotics.
The antibiotic peptide (antibiotic peptide), also called antibiotic peptide (antibiotic peptide), is a kind of polypeptide which is produced by specific gene coding of various biological cells and induced by external condition and has the active functions of broad-spectrum antibacterial, fungus, virus, protozoon, tumor cell inhibition and killing, etc. So far, about 2000 kinds of antibacterial peptides have been identified and separated in domestic and foreign reports, and thousands of simulated peptides artificially synthesized by using natural antibacterial peptides as templates have been obtained. The antibacterial peptides naturally occurring in the biological world can be classified into four major groups according to their structures: beta-pleated type antibacterial peptide, alpha-helical type antibacterial peptide, extension structure type polypeptide and loop structure type polypeptide.
At present, the common key problems which are urgently needed to be solved by the prawn breeding industry in China comprise: the method comprises the steps of control of the infectious diseases of the prawns, breeding of the varieties, nutrition research, culture environment control, prawn processing technology upgrading and the like. To solve these problems successfully, it is a prerequisite and foundation to elucidate the immune defense mechanism of prawns. In view of the above, the present inventors have studied and designed a beta-1, 3-glucan binding protein antimicrobial peptide of Litopenaeus vannamei and applications thereof, and have produced the peptide.
Disclosure of Invention
The invention aims to provide a beta-1, 3-glucan binding protein antibacterial peptide of the litopenaeus vannamei and application thereof, and provides a thought for searching new strategies of disease prevention and control and fine breed breeding of the litopenaeus vannamei through the research on the beta-1, 3-glucan binding protein antibacterial peptide of the litopenaeus vannamei, and promotes the healthy and sustainable development of the litopenaeus vannamei breeding industry in China.
In order to solve the above-mentioned purpose, the invention adopts the following technical scheme:
the antibacterial peptide of the beta-1, 3-glucan binding protein of the litopenaeus vannamei has an amino acid sequence shown in a sequence table SEQ ID NO. 1.
In a preferred embodiment, the antimicrobial peptide has a molecular weight of 1810 Da.
An application of the beta-1, 3-glucan binding protein antibacterial peptide of the litopenaeus vannamei in preparing the medicines for treating or preventing gram-negative bacteria or gram-positive bacteria.
As a preferred mode of embodiment, the gram-negative bacteria include Escherichia coli and Vibrio alginolyticus.
By way of example, the gram-positive bacteria include staphylococcus aureus, streptococcus type b.
The invention takes the beta-1, 3-glucan binding protein of litopenaeus vannamei as a main research object and uses AntiBP and CAMPR3And three pieces of on-line software APD3 predict the antibacterial peptide section which is likely to generate the antibacterial effect, and the most likely peptide section is selected for further antibacterial activity experiments. And analyzing the surface affinity of the antibacterial peptide by using NetSurfP ver.1.1 online software, performing 3D modeling by using SWISS-MODEL, I-TASSER and Pymol software, and analyzing the physicochemical properties of the antibacterial peptide by using HeliQuest online software. The antibacterial activity of the antibacterial peptide G1 is analyzed, and experimental results show that the antibacterial peptide G1 has an obvious antibacterial effect, so that an idea is provided for avoiding the application of antibiotics in the prawn breeding industry.
Drawings
FIG. 1 is a graph showing the effect of antibacterial activity analysis of the antibacterial peptide G1 of the present invention on Staphylococcus aureus; wherein: a: sterile water; b-k is G1; b: 1 mg/mL; c: 0.5 mg/mL; d: 0.25 mg/mL; e: 0.125 mg/mL; f: 0.063 mg/mL; g: 0.031 mg/mL; h: 0.016 mg/mL; i: 0.008 mg/mL; j: 0.004 mg/mL; k: 0.002 mg/mL; l: 0.25mg/mL ampicillin;
FIG. 2 is a graph showing the effect of the antibacterial activity of the antibacterial peptide G1 of the present invention on Escherichia coli; wherein: a: sterile water; b-k is G1; b: 1 mg/mL; c: 0.5 mg/mL; d: 0.25 mg/mL; e: 0.125 mg/mL; f: 0.063 mg/mL; g: 0.031 mg/mL; h: 0.016 mg/mL; i: 0.008 mg/mL; j: 0.004 mg/mL; k: 0.002 mg/mL; l: 0.063mg/mL ampicillin;
FIG. 3 is a diagram showing the effect of the antibacterial activity of the antibacterial peptide G1 of the present invention on Vibrio alginolyticus; wherein: a: sterile water; b-k is G1; b: 1 mg/mL; c: 0.5 mg/mL; d: 0.25 mg/mL; e: 0.125 mg/mL; f: 0.063 mg/mL; g: 0.031 mg/mL; h: 0.016 mg/mL; i: 0.008 mg/mL; j: 0.004 mg/mL; k: 0.002 mg/mL; l: 0.001 mg/mL; m: 0.016mg/mL ampicillin;
FIG. 4 is a graph showing the effect of G1 on the antibacterial activity of Streptococcus B; wherein: a: sterile water; b-k is G1; b: 1 mg/mL; c: 0.5 mg/mL; d: 0.25 mg/mL; e: 0.125 mg/mL; f: 0.063 mg/mL; g: 0.031 mg/mL; h: 0.016 mg/mL; i: 0.008 mg/mL; j: 0.25mg/mL ampicillin;
FIG. 5 is a 3D model of the antimicrobial peptide G1 of the present invention in β -1, 3-glucan binding protein; wherein: the segment indicated by the arrow is antibacterial peptide G1;
FIG. 6 is a 3D MODEL of the predicted antimicrobial peptide G1 of SWISS-MODEL of the present invention; wherein: the segment indicated by the arrow is antibacterial peptide G1;
FIG. 7 is a diagram showing the prediction of the physicochemical properties of the antimicrobial peptide G1 of the present invention.
Detailed Description
Example 1 prediction of the antibacterial peptide of the beta-1, 3-glucan binding protein of Litopenaeus vannamei
And searching the amino acid sequence of the beta-1, 3-glucan binding protein of the litopenaeus vannamei in an NCBI database. The sequence number name of the beta-1, 3-glucan binding protein of the litopenaeus vannamei is UniProtKB/Swiss-Prot: P81182.2, and the total length is 1454. Using AntiBP, CAMPR3And APD3, predicting the antibacterial peptide fragment of the beta-1, 3-glucan binding protein of the litopenaeus vannamei, and predicting 20 antibacterial peptide fragments which possibly have antibacterial activity and have degradation domains of alpha helical domains as shown in Table 1. Of these, 11 peptides (shown in bold) may have the possibility of forming alpha helix structures and may interact with the bacterial membrane, each peptide having a molecular weight in the size range of 1.4-1.9 kDa.
TABLE 1 Limnaeus vannamei beta-1, 3-glucan binding protein antimicrobial peptide prediction
Note: bold polypeptide sequence: alpha helices may be formed according to physicochemical properties.
Antibacterial peptide G1 fragment was selected from the above, and antibacterial activity test was performed on G1 (FLKLGRKSRYGMLKL).
Example 2 analysis of the bacteriostatic Activity of the beta-1, 3-glucan binding protein of Litopenaeus vannamei
2.1 materials of the experiment
2.1.1 principal Material
The polypeptide is synthesized by Beijing Zhongke matte biological technology Limited company, N-terminal acetylation and C-terminal amidation modification of the polypeptide are carried out, and the purity is more than 95 percent.
The aquatic pathogenic bacteria for experiments are respectively staphylococcus aureus, escherichia coli, streptococcus type B and vibrio alginolyticus.
2.1.2 Primary reagents
Ampicillin: provided by the university of college aquatic college laboratory.
The nutrient broth culture medium and LB agar are all produced by Guangdong Huanji microbial science and technology Limited.
2.1.3 Main instrumentation
A biochemical incubator: shanghai Pudong Rongfeng scientific instruments Co., Ltd
Electric heating constant temperature air-blast drying oven (DHG-9140A): shanghai fodder horse constant temperature equipment factory
Emmett electromagnetic oven (CE2132-Z)
Electric heating constant temperature water bath (DK-826): shanghai Jinghong experiment equipment Co Ltd
Double-sided vertical air supply (Economy type) clean bench (SW-CJ-2D) Suzhou Zhijing clean and clean Equipment Co., Ltd
Electronic analytical balance (ME203/AR 1530): Mettler-Tollido instruments (Shanghai) Co., Ltd
Double-layer large-capacity full-temperature constant-temperature culture oscillator (double-layer full-temperature constant-temperature shaking table) (ZHHWY-2102): shanghai Zhicheng analytical instruments manufacturing Co., Ltd
Autoclave (KT-30L): japan ALP Co
A liquid transferring gun: sammer Feishale (Shanghai) Instrument Co., Ltd
2.1.4 solutions
2.1.4.1 artificially synthesized polypeptide solution
The synthesized lyophilized powdery polypeptide product is taken out from a refrigerator in a laboratory, and is dissolved and mixed with 1mL of sterile water to prepare 1mg/mL of polypeptide solution. From this, 0.5mL was taken into another sterilized container, and 0.5mL of sterile water was added to prepare a 0.5mg/mL polypeptide solution. And by analogy, preparing a plurality of concentration gradients. And putting the mixture into a refrigerator for refrigeration and preservation.
2.1.4.2 ampicillin solution
2mg of ampicillin was weighed out accurately, and placed in a sterilized container, and 2mL of sterile water was added to prepare a 1mg/mL solution. Multiple concentration gradients were prepared from the polypeptide solution. And putting the mixture into a refrigerator for refrigeration and preservation.
2.1.4.3 culture medium
Nutrient broth formula (per liter):
3.0g of beef extract powder, 5.0g of sodium chloride and 10.0g of peptone. Final pH 7.4. + -. 0.2.
The using method comprises the following steps: weighing 18g of the product, adding 1L of distilled water or deionized water, stirring, heating, boiling to dissolve completely, packaging into test tubes or triangular flasks, and autoclaving at 121 deg.C for 15 min.
The LB agar formula:
5.0g of yeast extract powder, 10.0g of peptone, 5.0g of sodium chloride, 15.0g of agar and 1.0g of glucose. Final pH 7.0 ± 0.2.
The using method comprises the following steps: weighing 36g of the product, adding 1L of distilled water or deionized water, stirring, heating, boiling to dissolve completely, subpackaging in triangular flask, and sterilizing at 121 deg.C for 15 min.
2.2 analysis of bacteriostatic Activity by plate colony counting
The method comprises the following steps:
(1) activating Staphylococcus aureus, Escherichia coli, Streptococcus B, and Vibrio alginolyticus to small amount, i.e. 1mL nutrient broth +50 μ L bacteria liquid, and culturing in constant temperature shaking table at 37 deg.C for 6-12 h.
(2) Inoculating the activated bacterial liquid to an LB agar slant culture medium by using an inoculating loop, and putting the culture medium into a constant-temperature incubator at 37 ℃ for 6-12 h.
(3) Washing thallus Porphyrae with 3mL sterile water, adding into triangular flask containing 97mL sterile water, mixing, and diluting to 10%-2Doubling; taking 1mL of diluted bacterial liquid from the bacteria culture medium, mixing the diluted bacterial liquid with a test tube filled with 9mL of sterile water uniformly, and diluting the mixture to 10-3And (4) doubling. By analogy, the four pathogenic bacteria are diluted to corresponding times according to the required concentration.
(4) Taking 50 mu L of diluted bacterial liquid and 50 mu L of polypeptide solution with different components, mixing uniformly, taking sterile water as negative control, and taking ampicillin as positive control.
(5) The bacteriostatic ratio (%) was calculated as (number of negative control colonies-number of experimental group colonies)/number of negative control colonies × 100. The results are expressed as "mean ± standard deviation".
2.3 analysis of results
2.3.1 analysis of the bacteriostatic Activity of antimicrobial peptide G1
2.3.1.1 analysis of antibacterial activity of synthesized polypeptide G1 on staphylococcus aureus
The bacteriostatic activity of G1 on Staphylococcus aureus was analyzed by plate colony counting method, and the results are shown in Table 2 and FIG. 1:
TABLE 2 bacteriostasis rate of G1 to Staphylococcus aureus
The synthetic polypeptide G1 has an obvious antibacterial effect on staphylococcus aureus, the minimum inhibitory concentration is 0.004mg/mL, and the inhibitory rate is 56.45 +/-5.55%; the minimum inhibitory concentration of ampicillin to staphylococcus aureus is 0.25mg/mL, and the inhibitory rate is 43.64 +/-2.42%. 2.3.1.2 analysis of antibacterial activity of synthesized polypeptide G1 on Escherichia coli
The bacteriostatic activity of G1 on E.coli was analyzed by plate colony counting method, and the results are shown in Table 3 and FIG. 2:
TABLE 3 inhibition rate of G1 on E.coli
The synthesized polypeptide G1 has obvious antibacterial effect on escherichia coli, the minimum inhibitory concentration is 0.004mg/mL, and the inhibitory rate is 54.17 +/-0.83%; the minimum inhibitory concentration of ampicillin to colibacillus is 0.0625mg/mL, and the inhibitory rate is 31.39 + -0.28%.
2.3.1.3 analysis of antibacterial activity of synthesized polypeptide G1 on vibrio alginolyticus
The bacteriostatic activity of G1 on Vibrio alginolyticus was analyzed by plate colony counting method, and the results are shown in Table 4 and FIG. 3:
TABLE 4 inhibition rate of G1 to Vibrio alginolyticus
The synthesized polypeptide G1 has obvious antibacterial effect on vibrio alginolyticus, the minimum antibacterial concentration is 0.002mg/mL, and the antibacterial rate is 41.38 +/-31.03%; the minimum bacteriostasis concentration of the ampicillin to the vibrio alginolyticus is 0.016mg/mL, and the bacteriostasis rate is 68.97 +/-1.15%.
2.3.1.4 analysis of antibacterial activity of synthesized polypeptide G1 on streptococcus B
The bacteriostatic activity of G1 on Streptococcus B was analyzed by plate colony counting method, and the results are shown in Table 5 and FIG. 4:
TABLE 5 inhibition rate of G1 against Streptococcus B
The synthetic polypeptide G1 has obvious antibacterial effect on vibrio alginolyticus, the minimum inhibitory concentration is 0.016mg/mL, and the inhibitory rate is 75 +/-0.52%; the minimum inhibitory concentration of ampicillin to streptococcus B is 0.25mg/mL, and the inhibitory rate is 8.31 +/-2.11%.
2.3.1.5 summary of antibacterial effect of synthetic polypeptide G1
In conclusion, the synthetic polypeptide G1 has antibacterial effect on gram-negative bacteria (Escherichia coli, Vibrio alginolyticus) and gram-positive bacteria (Staphylococcus aureus and Streptococcus B). For negative bacteria such as escherichia coli and vibrio alginolyticus, the minimum inhibitory concentration is 0.004mg/mL and 0.002mg/mL respectively, and the inhibitory rate reaches 40-60%. The minimum inhibitory concentrations of the ampicillin are respectively 0.063mg/mL and 0.016 mg/mL; for positive bacteria such as staphylococcus aureus and streptococcus B, the minimum inhibitory concentrations are 0.004mg/mL and 0.016mg/mL respectively, the inhibitory rate reaches 50% -75%, and the minimum inhibitory concentrations of ampicillin are 0.25 mg/mL. That is, the synthetic polypeptide G1 is capable of inhibiting pathogenic bacteria at relatively low concentrations relative to antibiotics. This indicates that the synthetic polypeptide G1 has the potential to be an alternative to antibiotics. However, if the bacteriostatic effect is so strong, there may be a high possibility of killing both bacteria and cells, and further research is required.
Example 3 Structure prediction and analysis of the synthetic polypeptide G1
3.1 antimicrobial peptide G1 surface affinity and Secondary Structure prediction
Predicted by NetSurfP ver.1.1-Protein Surface access and Secondary Structure Predictions (http:// www.cbs.dtu.dk/services/NetSurfP /) online software.
3.1.1 surface affinity and Secondary Structure prediction of antimicrobial peptide G1
TABLE 6 predicted values of surface affinity and secondary structure of antimicrobial peptide G1
As can be seen from table 6, G1 has both hydrophilic and hydrophobic amino acids, which is consistent with the amphipathic nature of the antimicrobial peptides. Among them, 8 have surface affinity less than 0.5, strong hydrophobicity, easy interaction with bacterial cell membrane, and strong bacteriostatic activity. Structurally, the probability of forming a β -sheet is greater than that of forming an α -helix.
3.2I-TASSER 3D model for predicting antimicrobial peptide G1
3.2.1 methods
The amino acid sequence of the beta-1, 3-glucan binding protein was calculated for the antimicrobial peptide G1(FLKLGRKSRYGMLKL) using I-TASSER (http:// zhangglab. ccmb. med. umich. edu/I-TA SSER /) online software and finally displayed using Pymol software.
3.2.2 predictive 3D model of antimicrobial peptides
3.2.2.1 3D model for predicting antimicrobial peptide G1
As shown in fig. 5, antimicrobial peptide G1 may be a β sheet structure.
3.3 3D Model of SWISS-Model predicted antimicrobial peptide G1
3.3.1 methods
3D Model prediction is carried out on the antibacterial peptide G1(FLKLGRKSRYGMLKL) by SWISS-Model (https:// swisssmall. expay. org/interactive) online software on the antibacterial peptide G1, and finally Pymol software is used for displaying.
3.3.2 3D model prediction of antimicrobial peptide G1
The antibacterial peptide G1 predicted by using SWISS-MODEL is similar to MODEL 1fug.1.B, the similarity is 45.16%, wherein 1fug.1.B is S-Adenosylmethionine Synthetase (SAMS), and the research shows that SAMS can improve the resistance of plants.
3.4 physicochemical Properties of antimicrobial peptide G1
3.4.1 methods
The physicochemical properties of the antimicrobial peptide G1 were predicted by using HeliQuest (http:// helix. ipmc. cnrs. fr.) -online software, as shown in FIG. 7.
3.4.2 analysis of physicochemical Properties of antimicrobial peptide G1
TABLE 7 physicochemical Properties of antimicrobial peptide G1
As shown in table 7, the hydrophobicity of antimicrobial peptide G1 was 0.383; a net charge of 5; 8 polar residues, of which serine 1, glycine 2, lysine 3, arginine 2; 7 nonpolar residues, 1 tryptophan and 1 phenylalanine.
3.4.4 analysis of results
The primary structure of the antimicrobial peptides has similarities: the N end is rich in hydrophilic basic amino acid residue and lysine; the C end is rich in hydrophobic amino acid.
The antibacterial peptide G1 may be a beta-sheet structure, has 5 net charges and is a cationic antibacterial peptide. Most of the antibacterial peptide contains 2-7 positive charges, and the positive charges are beneficial to the aggregation of the antibacterial peptide on the surface of the membrane so as to achieve effective bactericidal concentration. The number of positive charges affects the bacteriostatic activity. The hydrophobicity has influence on the activity of cell membranes, and the too high hydrophobicity can cause the aggregation of the surface of the antibacterial peptide so as to precipitate and separate out, so that the antibacterial activity is reduced; too low hydrophobicity may cause a decrease in the membrane insertion ability of the antimicrobial peptide, and thus a decrease in the bacteriostatic activity.
The above description is only a preferred embodiment of the present invention, and therefore should not be taken as limiting the scope of the invention, which is defined by the appended claims and their equivalents.
Sequence listing
<110> college university
<120> a vannamei prawn beta-1, 3-glucan binding protein antibacterial peptide and application thereof
<130> 2017
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 15
<212> PRT
<213> Artificial sequence (artificial)
<400> 1
Pro Leu Leu Leu Gly Ala Leu Ser Ala Thr Gly Met Leu Leu Leu
1 5 10 15
Claims (3)
1. A beta-1, 3-glucan binding protein antibacterial peptide of a litopenaeus vannamei, which is characterized in that: its amino acid sequence is FLKLGRKSRYGMLKL.
2. The antibacterial peptide of the beta-1, 3-glucan binding protein of the litopenaeus vannamei as claimed in claim 1, wherein: the molecular weight of the antibacterial peptide is 1810 Da.
3. The use of the antibacterial peptide of the beta-1, 3-glucan binding protein of the litopenaeus vannamei according to claim 1 or 2, wherein: the application in preparing the medicine for treating or preventing colibacillus, vibrio alginolyticus, staphylococcus aureus or streptococcus B.
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| CN111333716B (en) * | 2020-03-23 | 2021-12-21 | 集美大学 | Pseudosciaena crocea hemoglobin antibacterial peptide and application thereof |
| CN112707960A (en) * | 2020-12-28 | 2021-04-27 | 集美大学 | Penaeus vannamei beta-1, 3-glucan binding protein antibacterial peptide |
| CN112898386B (en) * | 2021-03-02 | 2022-06-28 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN113087771B (en) * | 2021-04-25 | 2022-06-28 | 集美大学 | Penaeus vannamei DNA (deoxyribonucleic acid) combined antibacterial peptide VPDB40 and application thereof |
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