CN108047321A - A kind of litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide and its application - Google Patents
A kind of litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide and its application Download PDFInfo
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- CN108047321A CN108047321A CN201711324203.6A CN201711324203A CN108047321A CN 108047321 A CN108047321 A CN 108047321A CN 201711324203 A CN201711324203 A CN 201711324203A CN 108047321 A CN108047321 A CN 108047321A
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Abstract
The invention discloses a kind of 1,3 glucan-binding protein antibacterial peptides of litopenaeus vannamei β, amino acid sequence such as sequence table SEQ ID NO:Shown in 1.The molecular weight of the antibacterial peptide is 1810Da.The present invention discloses a kind of application of 1,3 glucan-binding protein antibacterial peptides of litopenaeus vannamei β again, the application in the drug for treating or preventing Gram-negative bacteria or gram-positive bacteria is prepared.The present invention lays a good foundation for the defence immunologic mechanism of follow-up further research litopenaeus vannamei and the exploitation of antibacterials.
Description
Technical field
The present invention relates to the technical field of aquaculture more particularly to a kind of litopenaeus vannamei β -1,3- glucan binding domian eggs
White antibacterial peptide and its application.
Background technology
Litopenaeus vannamei (Litopenaeus vannamei), also known as Penaeus Vannmei, Penaeus vannamei, belong to arthropod
Door, Crustachia, Decapoda, swimming suborder, Penaeidae, Penaeus, Lito-penaeus subgenus.It is cultivated in global type established practice modelling
Prawn kind in the yield of litopenaeus vannamei account for absolute advantage, account for the 75% of global single variety cultivation total output.With
The increase year by year of prawn culturing yield, cultivation problem are also emerged in large numbers gradually, and wherein prawn disease is that the influence to industry is almost crushing
, so, disease Control Technology is the key that cultivating link.Main disease has three classes：White spot syndrome, microsporidian
Sick (EHP) and prawn Deaths syndrome (EMS).The abuse of antibiotic causes drug resistance, the water pollution of microorganism in recent years
So that exploitation can replace the antibacterial peptide of antibiotic to become particularly important.
Antibacterial peptide (Antibac-terial peptide) be called antimicrobial peptide (Antimicrobial pep-tide),
Antibiotic peptide (Antibiotics peptide) is to be induced to generate through external condition by a variety of biological cell specific genes coding
One kind have broad spectrum antibiotic, fungi, virus, protozoon, press down tumor killing cell isoreactivity effect polypeptide.So far, state
It is inside and outside to report that kind of an antibacterial peptide is accredited, separates about more than 2000, it is artificial synthesized that template progress is made with natural antibacterial peptide
Simulating peptide has reached thousands of kinds.Four major classes can be divided into according to the difference of its structure in the antibacterial peptide of living nature naturally occurring：β-pleated sheet
Type antibacterial peptide, α screw types antibacterial peptide, extended structure type polypeptide and loop structural type polypeptides.
At present, the general character key issue that China's shrimp culture industry is badly in need of solving includes：The prevention and control of prawn infectiousness epidemic disease, product
Selection and breeding, nutrient research, Aquaculture Environmental Control and the upgrading of prawn processing technology of kind etc..And successfully to solve the problems, such as these, it explains
Bright prawn immune defence mechanism is premise and basis.In view of this, the present inventor study and devise a kind of litopenaeus vannamei β-
Thus 1,3- glucan-binding protein antibacterial peptide and its application, this case generate.
The content of the invention
It is an object of the invention to provide a kind of litopenaeus vannamei β -1,3- glucan-binding proteins antibacterial peptide and its application,
Pass through litopenaeus vannamei β -1, the research of 3- glucan-binding protein antibacterial peptides, to find new shrimp disease prevention and control, breeding choosing
The strategy educated provides thinking, promotes health, the sustainable development of China's shrimp culture industry.
In order to solve above-mentioned purpose, the technical solution adopted by the present invention is as follows：
A kind of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide, amino acid sequence such as sequence table SEQ ID
NO:Shown in 1.
As the preferred embodiment of embodiment, the molecular weight of the antibacterial peptide is 1810Da.
The application of a kind of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide treats or prevents gram preparing
Application in the drug of negative bacterium or gram-positive bacteria.
As the preferred embodiment of embodiment, the Gram-negative bacteria includes Escherichia coli, vibrio alginolyticus.
As the preferred embodiment of embodiment, the gram-positive bacteria includes staphylococcus aureus, beta streptococcus.
For the present invention with litopenaeus vannamei β -1,3- glucan-binding proteins are main study subject, by AntiBP,
CAMPR3, the prediction of tri- online softwares of APD3 there may be the antibacterial peptide fragment of fungistatic effect, it is further to choose most possible peptide fragment
Carry out bacteriostatic activity test.The surface affinity of antibacterial peptide is analyzed with NetSurfP ver.1.1 online softwares again,
3D modeling is carried out with SWISS-MODEL, I-TASSER, Pymol software, antibacterial peptide is analyzed with HeliQuest online softwares
Physicochemical property.The present invention carries out bacteriostatic activity analysis to antibacterial peptide G1, the experimental results showed that, antibacterial peptide G1 of the invention has
Apparent fungistatic effect, and then for application of the antibiotic in shrimp culture industry is avoided to provide thinking.
Description of the drawings
Fig. 1 is bacteriostatic activity analytical effect figures of the antibacterial peptide G1 of the present invention to staphylococcus aureus；Wherein：a：It is sterile
Water；B-k is G1；b：1mg/mL；c：0.5mg/mL；d：0.25mg/mL；e：0.125mg/mL；f：0.063mg/mL；g：
0.031mg/mL；h：0.016mg/mL；i：0.008mg/mL；j：0.004mg/mL；k：0.002mg/mL；l：0.25mg/mL ammonia
Parasiticin；
Fig. 2 is bacteriostatic activity analytical effect figures of the antibacterial peptide G1 of the present invention to Escherichia coli；Wherein：a：Sterile water；B-k is
G1；b：1mg/mL；c：0.5mg/mL；d：0.25mg/mL；e：0.125mg/mL；f：0.063mg/mL；g：0.031mg/mL；h：
0.016mg/mL；i：0.008mg/mL；j：0.004mg/mL；k：0.002mg/mL；l：0.063mg/mL ampicillins；
Fig. 3 is bacteriostatic activity analytical effect figures of the antibacterial peptide G1 of the present invention to vibrio alginolyticus；Wherein：a：Sterile water；B-k is
G1；b：1mg/mL；c：0.5mg/mL；d：0.25mg/mL；e：0.125mg/mL；f：0.063mg/mL；g：0.031mg/mL；h：
0.016mg/mL；i：0.008mg/mL；j：0.004mg/mL；k：0.002mg/mL；l：0.001mg/mL；m：0.016mg/mL ammonia
Parasiticin；
Fig. 4 is bacteriostatic activity analytical effect figures of the G1 of the present invention to beta streptococcus；Wherein：a：Sterile water；B-k is G1；
b：1mg/mL；c：0.5mg/mL；d：0.25mg/mL；e：0.125mg/mL；f：0.063mg/mL；g：0.031mg/mL；h：
0.016mg/mL；i：0.008mg/mL；j：0.25mg/mL ampicillins；
Fig. 5 is 3D models of the antibacterial peptide G1 of the present invention in β -1,3- glucan-binding proteins；Wherein：Arrow meaning segment
For antibacterial peptide G1；
Fig. 6 is the 3D models that SWISS-MODEL of the present invention predicts antibacterial peptide G1；Wherein：Arrow meaning segment is antibacterial peptide
G1；
Fig. 7 is the physicochemical property prognostic chart of antibacterial peptide G1 of the present invention.
Specific embodiment
The prediction of 1 litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide of embodiment
The protein-bonded amino acid sequence of beta-1,3-dextran of litopenaeus vannamei is searched in ncbi database.Vannamei boone
Prawn beta-1,3-dextran binding protein sequence number title is UniProtKB/Swiss-Prot:P81182.2, overall length are
1454.With AntiBP, CAMPR3, tri- online softwares of APD3, predict litopenaeus vannamei β -1,3- glucan-binding protein antibacterial
Peptide fragment as shown in table 1, predicts 20 antibacterial peptide fragments that may have antibacterial activity, degradation domain is α helical domains altogether.
Wherein 11 peptide section sequences (overstriking expression) may have the possibility for forming αhelix, thereby increases and it is possible to it interacts with mycoderm,
Each peptide fragment molecular size range scope is 1.4-1.9kDa.
1 litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide of table is predicted
Note：Overstriking peptide sequence：α spirals can be formed according to physicochemical property.
Antibacterial peptide G1 segments are therefrom selected, bacteriostatic activity test is carried out to G1 (FLKLGRKSRYGMLKL).
The bacteriostatic activity analysis of 2 litopenaeus vannamei beta-1,3-dextran binding protein antibacteria degradation peptide fragment of embodiment
2.1 experiment material
2.1.1 main material
Polypeptide is synthesized by BeiJing ZhongKe Yaguang Biology Science Co., Ltd, the acetylation of polypeptide N-terminal, C-terminal amidation modification, pure
Degree>95%.
Experimental water production pathogenic bacteria are respectively staphylococcus aureus, Escherichia coli, beta streptococcus, vibrio alginolyticus.
2.1.2 main agents
Ampicillin：It is provided by Aquatic Products Inst. Attached to Jimei Univ. laboratory.
Nutrient broth medium, LB agar are Huankai Microbes Tech Co., Ltd., Guangdong's production.
2.1.3 key instrument equipment
Biochemical cultivation case：Pudong, Shanghai Rong Feng scientific instrument Co., Ltd
Electric heating constant-temperature blowing drying box (DHG-9140A)：Shanghai Mo Ma thermostatic equipments factory
Amy spy electromagnetic oven (CE2132-Z)
Electric-heated thermostatic water bath (DK-826)：The upper grand experimental facilities Co., Ltd of Nereid
Double dual-sided perpendicular air-supply (economical) clean work station (SW-CJ-2D):Suzhou Zhi Jing cleaning equipments Co., Ltd
Electronic analytical balance (ME203/AR1530)：Mettler-Toledo Instrument (Shanghai) Co., Ltd.
Double-deck large capacity total temperature constant temperature culture oscillator (double-deck total temperature constant-temperature table) (ZHWY-2102)：Shanghai intelligence
City analytical instrument Manufacturing Co., Ltd
High-pressure sterilizing pot (KT-30L)：Japanese ALP companies
Liquid-transfering gun：Sai Mo flies generation that (Shanghai) Instrument Ltd.
2.1.4 solution
2.1.4.1 artificial synthetic polypeptide solution
The lyophilized powder polypeptide products of synthesis are taken out from laboratory freezer, the sterile water dissolution mixings of 1mL is added in, is made into
1mg/mL polypeptide solutions.0.5mL is therefrom taken to add the sterile water of 0.5mL in sterilized another container, be configured to
The polypeptide solution of 0.5mg/mL.And so on, prepare multiple concentration gradients.It is put into refrigerator cold-storage preservation.
2.1.4.2 ampicillin solution
2mg ampicillins accurately are weighed, is put into sterilized container, is added in the sterile water of 2mL, be made into 1mg/mL's
Solution.Multiple concentration gradients are prepared by polypeptide solution.It is put into refrigerator cold-storage preservation.
2.1.4.3 culture medium
Nutrient broth formula (every liter)：
Beef extract powder 3.0g, sodium chloride 5.0g, peptone 10.0g.Final pH 7.4 ± 0.2.
Application method：This product 18g is weighed, adds in distilled water or deionized water 1L, agitating and heating is boiled to being completely dissolved, divided
Fill test tube or triangular flask, 121 DEG C of high pressure sterilization 15min.
LB agar formulas：
Yeast extract powder 5.0g, peptone 10.0g, sodium chloride 5.0g, agar 15.0g, glucose 1.0g.Final pH 7.0 ±
0.2。
Application method：This product 36g is weighed, adds in distilled water or deionized water 1L, agitating and heating is boiled to being completely dissolved, divided
Fill triangular flask, 121 DEG C of sterilizing 15min.
2.2 the method for plate culture count analyze bacteriostatic activity
Method flow is as follows：
(1) staphylococcus aureus, Escherichia coli, beta streptococcus, vibrio alginolyticus are activated in a small amount, i.e. 1mL nutrient meats
+ 50 μ L bacterium solutions of soup, are placed in 37 DEG C of constant-temperature table culture 6-12h.
(2) bacterium solution after activating is seeded to using oese on LB agar slant culture-mediums, is put into constant incubator, 37 DEG C
Lower 6-12h.
(3) increase slant medium lawn under the sterile washing of 3mL after bacterium, pour into the triangular flask equipped with 97mL sterile waters
In, mixing is diluted to 10-2Times；1mL dilution bacterium solutions are therefrom taken with equipped with 9mL sterile water test tube mixings, being diluted to 10-3Times.With
This analogizes, and four kinds of pathogenic bacteria are by required concentration dilution to corresponding multiple.
(4) 50 μ L of bacterium solution and 50 μ L mixings of different component polypeptide solution after diluting, using sterile water as negative control, ammonia benzyl are taken
Penicillin is positive control.
(5) bacteriostasis rate (%)=(negative control clump count-experimental group clump count)/negative control clump count × 100 are calculated.
As a result represented with " mean+SD ".
2.3 interpretation of result
2.3.1 the bacteriostatic activity analysis of antibacterial peptide G1
2.3.1.1 synthesis polypeptide G1 analyzes staphylococcus aureus bacteriostatic activity
The method of plate culture count is taken to analyze G1 to staphylococcus aureus bacteriostatic activity, as a result as shown in table 2, Fig. 1：
2 G1 of table is to the bacteriostasis rate of staphylococcus aureus
Synthesis polypeptide G1 has apparent antibacterial effect, minimum inhibitory concentration 0.004mg/ to staphylococcus aureus
ML, bacteriostasis rate are 56.45 ± 5.55%；And ampicillin is 0.25mg/ to the minimum inhibitory concentration of staphylococcus aureus
ML, bacteriostasis rate are 43.64 ± 2.42%.2.3.1.2 synthesis polypeptide G1 analyzes Escherichia coli bacteriostatic activity
The method of plate culture count is taken to analyze G1 to Escherichia coli bacteriostatic activity, as a result as shown in table 3, Fig. 2：
3 G1 of table is to the bacteriostasis rate of Escherichia coli
Synthesis polypeptide G1 has Escherichia coli apparent antibacterial effect, and minimum inhibitory concentration 0.004mg/mL is antibacterial
Rate is 54.17 ± 0.83%；And ampicillin is 0.0625mg/mL to the minimum inhibitory concentration of Escherichia coli, bacteriostasis rate is
31.39 ± 0.28%.
2.3.1.3 synthesis polypeptide G1 analyzes vibrio alginolyticus bacteriostatic activity
The method of plate culture count is taken to analyze G1 to vibrio alginolyticus bacteriostatic activity, as a result as shown in table 4, Fig. 3：
4 G1 of table is to the bacteriostasis rate of vibrio alginolyticus
Synthesis polypeptide G1 has vibrio alginolyticus apparent antibacterial effect, and minimum inhibitory concentration 0.002mg/mL is antibacterial
Rate is 41.38 ± 31.03%；And ampicillin is 0.016mg/mL to the minimum inhibitory concentration of vibrio alginolyticus, bacteriostasis rate is
68.97 ± 1.15%.
2.3.1.4 synthesis polypeptide G1 analyzes beta streptococcus bacteriostatic activity
The method of plate culture count is taken to analyze G1 to beta streptococcus bacteriostatic activity, as a result as shown in table 5, Fig. 4：
5 G1 of table is to the bacteriostasis rate of beta streptococcus
Synthesis polypeptide G1 has vibrio alginolyticus apparent antibacterial effect, and minimum inhibitory concentration 0.016mg/mL is antibacterial
Rate is 75 ± 0.52%；And ampicillin is 0.25mg/mL to the minimum inhibitory concentration of beta streptococcus, bacteriostasis rate 8.31
± 2.11%.
2.3.1.5 synthesis polypeptide G1 fungistatic effects are summarized
To sum up, synthesis polypeptide G1 is (golden yellow to Gram-negative bacteria (Escherichia coli, vibrio alginolyticus), gram-positive bacteria
Staphylococcus, beta streptococcus) all there is antibacterial effect.To negative bacterium, such as Escherichia coli and vibrio alginolyticus, minimum inhibitory concentration
Respectively 0.004mg/mL and 0.002mg/mL, bacteriostasis rate reach 40%-60%.And the minimum inhibitory concentration of its ampicillin
Respectively 0.063mg/mL and 0.016mg/mL；It is minimum antibacterial dense such as staphylococcus aureus, beta streptococcus to positive bacteria
Degree is respectively 0.004mg/mL and 0.016mg/mL, and bacteriostasis rate reaches 50%-75%, the minimum inhibitory concentration of ampicillin
It is 0.25mg/mL.I.e. for antibiotic, synthesis polypeptide G1 can press down pathogenic bacteria with relatively small concentration
System.Thus synthesis polypeptide G1 can be explained to there is a possibility that antibiotic can be replaced.It is but so strong for fungistatic effect, it is also possible to
There is a possibility that it is larger not only kill bacterium but also kill cell, need to further be studied.
The structure prediction of 3 synthesis polypeptide G1 of embodiment and analysis
3.1 antibacterial peptide G1 surface affinities and secondary structure prediction
Pass through NetSurfP ver.1.1-Protein Surface Accessibility and Secondary
Structure Predictions(http://www.cbs.dtu.dk/services/NetSurfP/) online software prediction.
3.1.1 the surface affinity and secondary structure prediction of antibacterial peptide G1
The surface affinity and secondary structure prediction value of 6 antibacterial peptide G1 of table
As can be seen from Table 6, the existing hydrophilic amino acids of G1 have hydrophobic amino acid again, this has amphiphilic with antibacterial peptide
Feature is consistent.Wherein there are 8 surface affinities to be less than 0.5, hydrophobicity is stronger, easily interacts with bacterial cell membrane, has
Stronger bacteriostatic activity.From structure, formed beta sheet possibility be more than form alpha-helix.
The 3D models of 3.2 I-TASSER prediction antibacterial peptides G1
3.2.1 method
To antibacterial peptide G1 (FLKLGRKSRYGMLKL) I-TASSER (http://
Zhanglab.ccmb.med.umich.edu/I-TA SSER/) online software is to beta-1,3-dextran binding protein amino acid sequence
Row are calculated, and are finally shown with Pymol softwares.
3.2.2 antibacterial peptide 3D models are predicted
3.2.2.1 the 3D models of antibacterial peptide G1 are predicted
As shown in figure 5, antibacterial peptide G1 may be β-pleated sheet structure.
The 3D models of 3.3 SWISS-Model prediction antibacterial peptides G1
3.3.1 method
To antibacterial peptide G1 (FLKLGRKSRYGMLKL) SWISS-Model (https://
Swissmodel.expasy.org/interactive) online software carries out 3D model predictions to antibacterial peptide fragment G1, finally uses
Pymol softwares are shown.
3.3.2 the 3D model predictions of antibacterial peptide G1
The antibacterial peptide G1 predicted with SWISS-MODEL is similar to model 1fug.1.B, similarity 45.16%,
Middle 1fug.1.B is S-adenosylmethionine synzyme (S-Adenosylmethionine Synthetase, SAMS), there is research
Show that SAMS can improve the resistance of plant.
The physicochemical property of 3.4 antibacterial peptide G1
3.4.1 method
With HeliQuest (http://heliquest.ipmc.cnrs.fr/) online software is to the physics and chemistry of antibacterial peptide G1
Property predicted, as shown in Figure 7.
3.4.2 the analysis of physical and chemical property of antibacterial peptide G1
The physicochemical property of 7 antibacterial peptide G1 of table
As shown in table 7, the hydrophobicity of antibacterial peptide G1 is 0.383；Net charge is 5；Polar residues 8, wherein serine 1
A, glycine 2, lysine 3, arginase 12；Non-polar residue 7, wherein tryptophan 1, phenylalanine 1.
3.4.4 interpretation of result
The primary structure of antibacterial peptide has similitude：N-terminal is to add lysine rich in hydrophilic alkaline amino acid residue；C
It holds as rich in hydrophobic amino acid.
Antibacterial peptide G1 may be β-pleated sheet structure, and net charge has 5, be cationic antibacterial peptide.Most of antibacterial peptide contains 2-7
A positive charge, positive charge are conducive to antibacterial peptide in the surface aggregation of film so as to reach effective bacteriocidal concentration.The quantity shadow of positive charge
Ring bacteriostatic activity.Hydrophobicity has the activity of cell membrane influence, and hydrophobicity is excessively high to cause antibacterial peptide surface aggregation so as to heavy
Precipitation goes out, and bacteriostatic activity reduces；Hydrophobicity is too low to cause antibacterial peptide to reduce the insertion ability of film, and then bacteriostatic activity drops
It is low.
The above is only present pre-ferred embodiments, therefore cannot limit the scope implemented of the present invention according to this, i.e., according to
The equivalent changes and modifications that the scope of the claims of the present invention and description are made all should still belong in the range of the present invention covers.
Sequence table
<110>Collects The American University
<120>A kind of litopenaeus vannamei beta-1,3-dextran binding protein antibacterial peptide and its application
<130> 2017
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 15
<212> PRT
<213>Artificial sequence (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 (5)
1. a kind of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide, it is characterised in that：Its amino acid sequence such as sequence
Table SEQ ID NO:Shown in 1.
2. a kind of litopenaeus vannamei β -1 as described in claim 1,3- glucan-binding protein antibacterial peptides, it is characterised in that：Institute
The molecular weight for stating antibacterial peptide is 1810Da.
3. a kind of application of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide, it is characterised in that：Prepare treatment or
Prevent the application in the drug of Gram-negative bacteria or gram-positive bacteria.
4. a kind of application of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide, it is characterised in that：The gram-negative
Property bacterium bag includes Escherichia coli, vibrio alginolyticus.
5. a kind of application of litopenaeus vannamei β -1,3- glucan-binding protein antibacterial peptide, it is characterised in that：The gram sun
Property bacterium bag includes staphylococcus aureus, beta streptococcus.
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Cited By (6)
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| CN111333716A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea hemoglobin antibacterial peptide and application thereof |
| CN111333700A (en) * | 2020-03-23 | 2020-06-26 | 集美大学 | Pseudosciaena crocea whey acidic protein 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 |
| CN112898386A (en) * | 2021-03-02 | 2021-06-04 | 集美大学 | Large yellow croaker myosin heavy chain antibacterial peptide LCMHC and application thereof |
| CN113087771A (en) * | 2021-04-25 | 2021-07-09 | 集美大学 | Nanmeibai-DNA-conjugated antibacterial peptide VPDB40 and application thereof |
| CN114315972A (en) * | 2021-12-30 | 2022-04-12 | 集美大学 | Litopenaeus vannamei calcium ion chelating antibacterial peptide PV13 and application thereof |
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