CN101250222A - Ascidian antibacterial peptide, precursor peptide, coding gene and use thereof - Google Patents
Ascidian antibacterial peptide, precursor peptide, coding gene and use thereof Download PDFInfo
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- CN101250222A CN101250222A CNA2008100657658A CN200810065765A CN101250222A CN 101250222 A CN101250222 A CN 101250222A CN A2008100657658 A CNA2008100657658 A CN A2008100657658A CN 200810065765 A CN200810065765 A CN 200810065765A CN 101250222 A CN101250222 A CN 101250222A
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Abstract
The invention relates to a sea squirt antibacterial peptide, a relative precursor peptide, a relative encoding gene and an application, wherein the sea squirt antibacterial peptide is sea squirt antibacterial peptide Clavanin H, relative conservative variation polypeptide, relative active derivative or the polypeptide derived from the sea squirt antibacterial peptide Clavanin H with antibacterial function whose one or several amino acid residues are substituted, deleted or added. The precurose peptide of the sea squirt antibacterial peptide is provided with the amino acid sequence represented by SEQ ID NO: 2 in the sequence list. The inventive sea squirt antibacterial peptide can be used to prepare anti-virus product as forge additive, veterinary drug, preservative, pharmaceutical product as antibiotics.
Description
Technical field
The present invention relates to bioengineering field, be specifically related to the application of a kind of Ascidian antibacterial peptide, its precursor peptide, encoding gene and Ascidian antibacterial peptide.
Background technology
Antibacterial peptide (antimicrobial peptides) is the natural small molecular protein that a class has anti-microbial activity.From Sweden scientist Boman in 1975 etc. separate on one's body from silkworm chrysalis obtain first antibacterial peptide cecropin (Cecropin) since, people are again insect, batrachians, aquatic animal, and comprise that people's Mammals even plant and bacterium etc. have found at least 900 surplus kinds of antibacterial peptides in the biological spectrum widely.This endogenic antibacterial peptide synthesizes through inducing, and playing an important role aspect the invasion of body opposing cause of disease, is the important component part of body non-specific immunity.
The resistance spectrum of antibacterial peptide is very extensive.Great majority especially have stronger killing action to drug tolerant bacteria to bacterium, and some then also has killing action to some fungi, protozoon.In recent years research finds that also some antibacterial peptide can also be selected killing tumor cell, suppresses duplicating of HBV, HIV, thereby has caused the concern that people are bigger.The mechanism of action of antibacterial peptide is special, the popular viewpoint is at present: at first, positively charged antibacterial peptide molecule contacts with electronegative target cell membrane, to form the antibacterial peptide dimer injection cytolemma of hydrophobic surface subsequently by the electromotive force that target cell membrane produced, last a plurality of dimer or polymer form the ionic channel of striding film together, thereby upset the permeability and the cellular energy state of cytolemma, cause the cytolemma depolarize, respiration is suppressed and cell ATP content seriously descends, and finally makes target cell death.The antivirus action of antibacterial peptide then is to cause virus to lose biological activity by combining with virus capsid protein.This special role mechanism makes microorganism be difficult for it is produced resistance.
Ascidian is a kind of marine invertebrate, belongs to Chordata, is in again between invertebrates and the vertebrates as ancient protochordate.Ascidian is the fabulous material that research vertebrates innate immunity is evolved, depend on innate immune system owing to ascidian lacks the immunoglobulin (Ig) and the TXi Baoshouti that exist in high-grade vertebrates more, so their hemocyte there is important effect in host defense.In recent years, many antibacterial peptides from the hemocyte of Ascidian, have been extracted.
At present, people have found multiple antibacterial peptide from Ascidian.Difference according to the Ascidian antibacterial peptide primary structure can be divided into the three major types type.(1) the both sexes antibacterial peptide molecule of linear spirane structure comprises Clavanins, styelins, clavaspirin; (2) contain the antibacterial peptide molecule of DOPA residue, comprise plicatamide, haloxyamine; (3) contain the antibacterial peptide molecule of disulfide linkage, comprise halocidin and dycynthaurin etc.
Lee etc. isolate one group of Clavanins A of family that is made up of 4 alpha-helix antibacterial peptides, B, C, and D from the hemocyte of Styela clava (Styela clava).After this from the cDNA library of Styela clava pharynx tissue construction, filter out a kind of new Clavanins family member Clavanin E again.By studies show that Clavanins A-E is rich in Histidine, comprise 23 residues, the amidated antibacterial peptide of C-terminal.
The anti-microbial activity of Clavanins is discovered that they equally with other antibacterial peptides show germ-killing efficiency fast under low-down concentration.After 5 minutes hatching, the Clavanin A of 1.6ug/ml makes the quantity of E.coli ML-35P reduce half; The sterilizing ability of finding ClavaninC/D simultaneously is roughly higher 3 ~ 5 times than Clavanin A/B.Studies show that afterwards they all have significant anti-microbial effect to other several Gram-positives and negative bacteria, and several fungies such as C.albicans are had the inhibition effect.Under low pH (pH=5.5) and high salt (300mmol/LNaCl) condition, wherein several microorganisms are still kept suitable activity.
Summary of the invention
First purpose of the present invention is to provide a kind of Ascidian antibacterial peptide and precursor peptide thereof.
Second purpose of the present invention is to provide the encoding gene of Ascidian antibacterial peptide of the present invention.
The 3rd purpose of the present invention is Ascidian antibacterial peptide of the present invention is applied to prepare disease-resistant becteriums product.
The selected Ascidian of the present invention belongs to South China Sea entomophagy Styela clava (Styela clava), picks up from the South China Sea Xisha Islands.
The present invention clones from South China Sea Styela clava pharynx tissue and obtains antibacterial peptide Clavanin family member with the method in construction cDNA library.
The structure in South China Sea Ascidian pharynx tissue cDNA library: at first separate Ascidian pharynx tissue, extract total RNA.Get total RNA and carry out the synthetic cDNA first chain product of reverse transcription.Get cDNA again and be used for ligation, conversion fluid is coated plate respectively, and all the other are used to shake total storehouse bacterium liquid, and the picking mono-clonal is protected kind from the flat board.
The present invention passes through the extensive sequencing of above recombinant clone, obtain 8 est sequence coding South China Sea Styela clava antibacterial peptide Clavanin family members, applicant general's called after Ascidian antibacterial peptide Clavanin H, Ascidian antibacterial peptide Clavanin H is a mature peptide, be made up of 23 amino acid, molecular weight is 2.71 kilodaltons, and Ascidian antibacterial peptide Clavanin H has the feature of typical antibacterial peptide primary structure, its aminoacid sequence is shown in SEQ ID NO:3 in the sequence table, and is specific as follows:
Val?Phe?Arg?Tyr?Leu?Gly?Lys?Ile?Ile?His?His?Val?Gly?Asn?Phe
1 5 10 15
Val?His?Gly?Phe?Ser?His?Val?Phe
20
This mature peptide can obtain by separation and purification, and HPLC identifies that its purity reaches 96.5%, and MALDI-TOF identifies that its molecular weight is correct.
Ascidian antibacterial peptide of the present invention is following (a) or (b) or (c) or (d) described polypeptide:
(a) have the described aminoacid sequence of SEQ ID NO:3 in the sequence table, i.e. Ascidian antibacterial peptide Clavanin H;
(b) (a) conservative property of described aminoacid sequence variation polypeptide;
(c) (a) reactive derivative of described aminoacid sequence;
(d) aminoacid sequence in (a) is formed through replacement, disappearance or the interpolation of one or more amino-acid residues have antibacterial by (a) polypeptides derived.
Above-mentioned (c) described Ascidian antibacterial peptide, the C-terminal amidation modifier of preferred Ascidian antibacterial peptide Clavanin H.
Ascidian antibacterial peptide of the present invention can be the product that obtains by chemosynthesis, dna recombinant expression.
The precursor peptide of Ascidian antibacterial peptide Clavanin H of the present invention, its aminoacid sequence is shown in SEQ ID NO:2 in the sequence table, and is specific as follows:
Met?Lys?Thr?Thr?Ile?Leu?Ile?Leu?Leu?Ile?Leu?Gly?Leu?Gly?Ile
1 5 10 15
Asn?Ala?Lys?Ser?Leu?Glu?Glu?Arg?Lys?Ser?Glu?Glu?Glu?Lys?Val
20 25 30
Phe?Arg?Tyr?Leu?Gly?Lys?Ile?Ile?His?His?Val?Gly?Asn?Phe?Val
35 40 45
His?Gly?Phe?Ser?His?Val?Phe?Gly?Asp?Asp?Gln?Gln?Asp?Asn?Gly
50 55 60
Lys?Phe?Tyr?Gly?His?Tyr?Ala?Glu?Asp?Asn?Gly?Lys?His?Trp?Tyr
65 70 75
Asp?Thr?Gly?Asp?Gln
80
The polynucleotide sequence of the precursor peptide of coding Ascidian antibacterial peptide Clavanin H is shown in SEQ ID NO:1 in the sequence table, and is specific as follows:
atgaaaacaa?caattttgat?tcttctcata?ctgggacttg?gcatcaatgc?aaaatctctg?60
gaggaaagaa?aatcggagga?agagaaagta?ttccgctacc?ttggcaaaat?tattcatcat?120
gttggcaatt?ttgtacatgg?ttttagccac?gtgttcggcg?acgaccaaca?agataatgga?180
aagttttatg?gccactacgc?agaagacaat?ggcaagcatt?ggtatgatac?cggggatcaa?240
taa 243
Polynucleotide of the present invention are following (a) or (b) described nucleotide sequence:
(a) polynucleotide of the precursor peptide of coding Ascidian antibacterial peptide Clavanin H;
(b) with polynucleotide (a) complementary polynucleotide.
Polynucleotide of the present invention preferably have the polynucleotide of the described nucleotide sequence of SEQ ID N0:1 in the sequence table.
The South China Sea Styela clava antibacterial peptide Clavanin H biologically active that the present invention obtains has anti-microbial effect.The Clavanin H of separation and purification can suppress part malignant bacteria and fungi when 50nM.Therefore, Ascidian antibacterial peptide of the present invention can be applicable to prepare disease-resistant becteriums product, and disease-resistant becteriums product comprises fodder additives, veterinary drug, sanitas, pharmaceutical prod such as antibacterials etc.
Description of drawings
Fig. 1 is the est sequence length distribution statistical graph in South China Sea Ascidian pharynx tissue cDNA library.
Fig. 2 is the molecular sieving collection of illustrative plates of South China Sea Styela clava antibacterial peptide Clavanin H of the present invention;
Fig. 3 is anion exchange separation figure behind the South China Sea Styela clava antibacterial peptide Clavanin H molecular sieving;
Fig. 4 is that South China Sea Styela clava antibacterial peptide Clavanin H negatively charged ion separates back HPLC separation graph;
Fig. 5 is that MALDI-TOF identifies figure behind the South China Sea Styela clava antibacterial peptide Clavanin H purifying.
Fig. 6 is the experimental result that South China Sea Styela clava antibacterial peptide Clavanin H suppresses mammitis of cow pathogenic bacterium growth experiment.
Embodiment
Embodiment one: the structure and the est sequence analysis in South China Sea Ascidian pharynx tissue cDNA library
The extraction of total RNA is synthetic with cDNA: separates South China Sea Ascidian pharynx tissue, carry out poison with reference to the TRIZOL LS reagent specification sheets of GibcoBRL company and manage total RNA extraction.Library construction adopts the Clontech Smart cDNA Library Construction Kit of company test kit, and utilizes the incidental primer of test kit itself, carrier, restriction enzyme etc. to experimentize.Get 1 μ g Ascidian pharynx total tissue RNA with SMART III oligonucleotide segment (5 '-AAGCAGTGGTATCAACGCAGAGTGGCCATTATGGCCGGG-3 ') and CDSIII/3 ' PCR primer (5 '-ATTCTAGAGGCCGAGGCGGCCGACATG-d (T)
30N
-1N-3 ') carries out synthetic first chain of reverse transcription, obtain 10 μ l cDNA, the first chain product.
The structure and the evaluation in Ascidian pharynx tissue cDNA library: get cDNA 1.5 μ l and be used for ligation, reaction system 5 μ l transform wherein 1 μ l, get 5ul conversion fluid coated plate respectively, get the 300ul conversion fluid and are used to shake total storehouse bacterium colony.The dull and stereotyped single colony number of next day numeration is respectively: 805,695 and 1052.Therefore the obtainable cDNA library clone of double-stranded cDNA7ul number is: (805+695+1052) * 1050*7*5/3*5*1.5=4.170*10
6(individual).46 mono-clonals of picking utilize the T7 and the amplification of SP6 primer PCR at carrier multiple clone site two ends at random, and the result shows that recombination fraction surpasses 98% (45/46), and most insertion fragment is greater than 500bp (41/46), and on average inserting fragment length is 700bp.Picking six plate mono-clonals shake bacterium at random, the guarantor plants, extracts plasmid, the unidirectional order-checking of T7 primer from flat board, and manual BLASTN of use and the online homology of BLASTX are compared SEQTOOL, ClustalX 1.83 programanalysis sequencing results.Sequencing result shows that it is 544bp that Styela clava on average inserts fragment length.
Above result shows that the aspects such as subnumber, recombination fraction and insertion clip size of recombinating in the library, Ascidian pharynx tissue cDNA library that the applicant makes up all meet the quality standard in good library.At 500-600bp, there are abundant est sequence in 700-800bp and 800-900bp place as can be seen from Fig. 1, and the est sequence length of the South Sea Styela clava antifungal genes Clavanin H that the present invention cloned is sitting between the 500-600bp.
Embodiment two: the mensuration and the analysis of Ascidian antifungal genes Clavanin H sequence
The sequence of South Sea Styela clava antifungal genes Clavanin H is from 8 height homologous est sequences of being cloned in the embodiment one South China Sea Ascidian pharynx tissue cDNA library, Ascidian antifungal genes Clavanin H belongs to cance high-expression gene, account for 4% of all est sequences, with No. 5 plate D12 number clone is that example is carried out bioinformatic analysis to it, and the result shows that its cDNA sequence length is 523bp.Utilize tool software SEQTOOL that its base sequence is analyzed, and obtain its maximum opening code-reading frame, length 240bp (not comprising terminator codon), the precursor peptide of 80 amino-acid residues of coding, its nucleotide sequence is as described in the SEQ ID NO:1 in the sequence table, and the aminoacid sequence of the precursor peptide of 80 amino-acid residues is as described in the SEQ IDNO:2 in the sequence table.Further analyze and show, the 1-29 amino acids residue of this precursor peptide is its signal peptide zone, its the 29th residue is Methionin, can think standard protein hydrolysis signal, the leading peptide and the mature peptide of precursor peptide are partly separated, so determine that the aminoacid sequence of Clavanin H mature peptide is VFRYLGKIIHHVGNFVHGFSHVF, i.e. the described aminoacid sequence of SEQ IDNO:3 in the sequence table.Because there are tangible similarity in signal peptide district and mature peptide district and antibacterial peptide Clavanin family that all have been reported in the Clavanin H precursor peptide, so Ascidian antibacterial peptide Clavanin H is new Clavanin family member.
Embodiment three: the separation and purification of Ascidian antibacterial peptide Clavanin H
Get Ascidian pharynx tissue, shred back 50mmol/L Tris-Cl, the pH8.6+100mmol/LNaCl extraction separates with G25Fine (i.d2.6*100cm), and with the extraction buffer solution elution, 280nm detects, and visible four ultraviolet absorption peaks as shown in Figure 2; Collect QSepharose fast flow separation on the 2nd peak, the NaCl gradient elution obtains 5 elution peaks as shown in Figure 3.Collect on the 1st peak C18 reversed-phase column and separate, the acetonitrile gradient wash-out, the peak of collecting retention time and be 45.7min is as shown in Figure 4.The antibiotic Clavanin H of the Ascidian of separation and purification, through flying time mass spectrum analysis, molecular weight be 2.71 kilodaltons as shown in Figure 5.These theoretical molecular 2.71 kilodaltons with the expressed sequence VFRYLGKIIHHVGNFVHGFSHVF that infers according to institute's cloned genes are consistent.
Embodiment four: Ascidian antibacterial peptide gene C lavanin H's is recombinant expressed
This experiment adopts histidine defect type pichia spp GS115 as the host bacterium, adopts secretion expression's carrier pPICZ α A to make up recombinant expression system.Select SacI restriction endonuclease linearizing recombinant vectors pPICZ α A, the antibacterial peptide Clavanin H gene that will have corresponding restriction enzyme site then is connected with linearized vector by the T4DNA ligase enzyme, again it is transformed in the bacillus coli DH 5 alpha, utilizes the less salt LB plate screening positive transformant of Zeocin resistance.Choose single colony inoculation and cultivate, the extracting plasmid carries out enzyme and cuts checking and order-checking.
The competent cell of preparation Pichi strain GS115.Get the linearizing recombinant expression plasmid mixing of 80ml competent cell and 10ug SacI single endonuclease digestion, the conversion of shocking by electricity.Behind 30 ℃ of incubation 1h, bacterium liquid is coated in contains on the antibiotic YPD solid medium of the 100ug/ml Zeocin flat board.30 ℃ of constant temperature culture 2 ~ 4 days filter out positive bacterium colony.Simultaneously, with the blank plasmid transformed yeast of the linearizing pPICZ α of Sacl A GS115 bacterial strain as blank.
The positive recombination microzyme that evaluation is obtained joins respectively in the 10ml YPDA substratum, 30 ℃ of constant temperature culture, and then utilizes methyl alcohol as inductor, and reorganization target protein Clavanin H is carried out abduction delivering, and through ultrafiltration and cation-exchange chromatography purifying.
Embodiment five: the bacteriostatic activity experiment of Ascidian antibacterial peptide Clavanin H
Ascidian antibacterial peptide Clavanin H suppresses the experiment of mammitis of cow pathogenic bacterium.Select the inflammation enlargement of newborn chamber, skin rubefaction, warm, not smooth, the thin dairy cow milk of being with yellow and being mixed with the obvious mammitis of cow symptoms of performance such as floss and curd pieces of milk discharge in the test.Experimental group is the above-mentioned dairy cow milk of 5ml with concentration is that the Ascidian antibacterial peptide Clavanin H equal-volume concussion of 0.5mg/ml mixed 30 minutes, and control group is that the above-mentioned dairy cow milk of 5ml shakes with the sterile saline equal-volume and mixed 30 minutes.Above-mentioned mixing solutions separate application to the LB solid medium, is observed mammitis of cow pathogenic bacterium growing state.As can be seen from Figure 6, adding has in the dairy cow milk of antibacterial peptide, and the mastitis pathogenic bacterium are growth (left side flat board) not, and control group (right side flat board) then has a large amount of mastitis pathogenic bacterium growths.Illustrate that antibacterial peptide has the effect of killing the mastitis pathogenic bacterium.
Ascidian antibacterial peptide Clavanin H of the present invention can suppress part malignant bacteria and fungi.Therefore, Ascidian antibacterial peptide of the present invention can be applicable to prepare disease-resistant becteriums product, as: fodder additives, veterinary drug, sanitas, antibacterials etc.
Sequence table
Claims (6)
1. Ascidian antibacterial peptide is following (a) or (b) or (c) or (d) described polypeptide:
(a) has the described aminoacid sequence of SEQ ID NO:3 in the sequence table;
(b) (a) conservative property of described aminoacid sequence variation polypeptide;
(c) (a) reactive derivative of described aminoacid sequence;
(d) aminoacid sequence in (a) is formed through replacement, disappearance or the interpolation of one or more amino-acid residues have antibacterial by (a) polypeptides derived.
2. Ascidian antibacterial peptide according to claim 1 is characterized in that: be the C-terminal amidation modifier of (a) described polypeptide.
3. the precursor peptide of an Ascidian antibacterial peptide has the described aminoacid sequence of SEQ ID NO:2 in the sequence table;
4. polynucleotide are following (a) or (b) described nucleotide sequence:
(a) polynucleotide of the described polypeptide of coding claim 3;
(b) with polynucleotide (a) complementary polynucleotide.
5. polynucleotide according to claim 4 is characterized in that: have the described nucleotide sequence of SEQ ID NO:1 in the sequence table.
6. claim 1 or the 2 described Ascidian antibacterial peptides application on the disease-resistant becteriums product of preparation, described disease-resistant becteriums product comprises fodder additives, veterinary drug, sanitas and pharmaceutical prod.
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| CN102174096A (en) * | 2010-12-24 | 2011-09-07 | 中国科学院海洋研究所 | Ciona intestinalis polypeptide and preparation method thereof |
| CN102597249A (en) * | 2009-09-04 | 2012-07-18 | 弗雷德里克·诺伦 | A system to produce feedstock for biogas production |
| CN103360467A (en) * | 2013-07-16 | 2013-10-23 | 青岛科技大学 | Preparation method of broad-spectrum antibacterial polypeptide |
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| CN104185425A (en) * | 2011-12-16 | 2014-12-03 | 卑尔根技术交易股份公司 | Tunicate extract for use in animal feeds |
| CN110810672A (en) * | 2019-11-28 | 2020-02-21 | 威海长青海洋科技股份有限公司 | Abalone feed compound additive and manufacturing and using methods thereof |
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| CN102597249A (en) * | 2009-09-04 | 2012-07-18 | 弗雷德里克·诺伦 | A system to produce feedstock for biogas production |
| CN102174096A (en) * | 2010-12-24 | 2011-09-07 | 中国科学院海洋研究所 | Ciona intestinalis polypeptide and preparation method thereof |
| CN104185425A (en) * | 2011-12-16 | 2014-12-03 | 卑尔根技术交易股份公司 | Tunicate extract for use in animal feeds |
| CN103360467A (en) * | 2013-07-16 | 2013-10-23 | 青岛科技大学 | Preparation method of broad-spectrum antibacterial polypeptide |
| CN103382219A (en) * | 2013-07-16 | 2013-11-06 | 青岛科技大学 | Preparation method of antitumor polypeptide |
| CN103360467B (en) * | 2013-07-16 | 2015-06-03 | 青岛科技大学 | Preparation method of broad-spectrum antibacterial polypeptide |
| CN110810672A (en) * | 2019-11-28 | 2020-02-21 | 威海长青海洋科技股份有限公司 | Abalone feed compound additive and manufacturing and using methods thereof |
| CN114569699A (en) * | 2022-03-18 | 2022-06-03 | 山东大学齐鲁医院(青岛) | Medicinal preparation for vascular endothelial cell aging |
| CN114569699B (en) * | 2022-03-18 | 2022-10-28 | 山东大学齐鲁医院(青岛) | Medicinal preparation for vascular endothelial cell aging |
| CN117285611A (en) * | 2023-11-24 | 2023-12-26 | 中国海洋大学 | Novel anti-inflammatory oligopeptide from sea squirt and application of novel anti-inflammatory oligopeptide in preparation of medicines |
| CN117285611B (en) * | 2023-11-24 | 2024-02-09 | 中国海洋大学 | Anti-inflammatory oligopeptide from sea squirt and application of anti-inflammatory oligopeptide in preparation of medicines |
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Open date: 20080827 |