CN104017087B - One boar derived antimicrobial peptide and preparation method thereof - Google Patents
One boar derived antimicrobial peptide and preparation method thereof Download PDFInfo
- Publication number
- CN104017087B CN104017087B CN201410284682.3A CN201410284682A CN104017087B CN 104017087 B CN104017087 B CN 104017087B CN 201410284682 A CN201410284682 A CN 201410284682A CN 104017087 B CN104017087 B CN 104017087B
- Authority
- CN
- China
- Prior art keywords
- antibacterial peptide
- fusion
- antibacterial
- preparation
- recombinant dna
- 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.)
- Expired - Fee Related
Links
- 239000003910 polypeptide antibiotic agent Substances 0.000 title claims abstract description 89
- 238000002360 preparation method Methods 0.000 title claims abstract description 17
- 108700042778 Antimicrobial Peptides Proteins 0.000 title abstract description 7
- 102000044503 Antimicrobial Peptides Human genes 0.000 title abstract description 7
- 230000004927 fusion Effects 0.000 claims abstract description 43
- 239000013604 expression vector Substances 0.000 claims abstract description 10
- 239000000654 additive Substances 0.000 claims abstract description 8
- 108020004705 Codon Proteins 0.000 claims abstract description 6
- 230000000844 anti-bacterial effect Effects 0.000 claims description 16
- 108020004511 Recombinant DNA Proteins 0.000 claims description 14
- 238000013461 design Methods 0.000 claims description 10
- 230000036039 immunity Effects 0.000 claims description 6
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 4
- 239000013598 vector Substances 0.000 claims description 4
- 239000003814 drug Substances 0.000 claims description 3
- 241000894006 Bacteria Species 0.000 abstract description 11
- 230000000845 anti-microbial effect Effects 0.000 abstract description 8
- 108010066857 PMAP-36 Proteins 0.000 abstract description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 abstract description 6
- 108050004290 Cecropin Proteins 0.000 abstract description 5
- 241000588724 Escherichia coli Species 0.000 abstract description 5
- 241000191967 Staphylococcus aureus Species 0.000 abstract description 4
- 201000010099 disease Diseases 0.000 abstract description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 4
- 230000000968 intestinal effect Effects 0.000 abstract description 4
- 244000144972 livestock Species 0.000 abstract description 4
- 230000003385 bacteriostatic effect Effects 0.000 abstract description 2
- 238000000338 in vitro Methods 0.000 abstract description 2
- 238000000746 purification Methods 0.000 abstract description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 13
- 238000000034 method Methods 0.000 description 8
- 229920001184 polypeptide Polymers 0.000 description 8
- 102000004196 processed proteins & peptides Human genes 0.000 description 8
- 239000000047 product Substances 0.000 description 7
- FRXSZNDVFUDTIR-UHFFFAOYSA-N 6-methoxy-1,2,3,4-tetrahydroquinoline Chemical compound N1CCCC2=CC(OC)=CC=C21 FRXSZNDVFUDTIR-UHFFFAOYSA-N 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 2
- 108010042407 Endonucleases Proteins 0.000 description 2
- 102000004533 Endonucleases Human genes 0.000 description 2
- 102100029727 Enteropeptidase Human genes 0.000 description 2
- 108010013369 Enteropeptidase Proteins 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000862 Ion Channels Proteins 0.000 description 2
- 102000004310 Ion Channels Human genes 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- 108010066849 PMAP-37 Proteins 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 238000000137 annealing Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000004087 circulation Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 239000003292 glue Substances 0.000 description 2
- 150000002460 imidazoles Chemical class 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- 230000001665 lethal effect Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000003204 osmotic effect Effects 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 101710145659 Antibacterial peptide PMAP-36 Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 206010010356 Congenital anomaly Diseases 0.000 description 1
- 241000446313 Lamella Species 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- NPYPAHLBTDXSSS-UHFFFAOYSA-N Potassium ion Chemical compound [K+] NPYPAHLBTDXSSS-UHFFFAOYSA-N 0.000 description 1
- 101100298055 Sus scrofa PMAP36 gene Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 230000000721 bacterilogical effect Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000012295 chemical reaction liquid Substances 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000001143 conditioned effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 230000001186 cumulative effect Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000012969 defense response to bacterium Effects 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 230000000855 fungicidal effect Effects 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 231100000225 lethality Toxicity 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- ZPWVBRGFVGXRKZ-DMZHRTQBSA-N pmap-23 Chemical compound C([C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCNC(N)=N)[C@@H](C)CC)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(N)=O)C1=CC=CC=C1 ZPWVBRGFVGXRKZ-DMZHRTQBSA-N 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 108010027884 porcine myeloid antibacterial peptide 23 Proteins 0.000 description 1
- 229910001414 potassium ion Inorganic materials 0.000 description 1
- 238000012797 qualification Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000002525 ultrasonication Methods 0.000 description 1
Landscapes
- Peptides Or Proteins (AREA)
- Fodder In General (AREA)
Abstract
Description
Primer numbers | Sequence |
S1-SEQ ID 4 | 5’-agggtaccgttggtcgtttccgtcgtctgcgtaaaaaaacccgtaaacgtctgaa-3’ |
A1-SEQ ID 5 | 5’-aacgatcggcgggatccatttcagaactttaccgatttttttcagacgtttacggg-3’ |
F1-SEQ ID 6 | 5’-ggatcccgccgatcgttggttctatcccgctgggttgcggtccggaaggtatcgct-3’ |
R1-SEQ ID 7 | 5’-tactcgagttaacgcggaccaccctggatagcgatagcgataccttccggac-3’ |
Claims (8)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201410284682.3A CN104017087B (en) | 2014-06-24 | 2014-06-24 | One boar derived antimicrobial peptide and preparation method thereof |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201410284682.3A CN104017087B (en) | 2014-06-24 | 2014-06-24 | One boar derived antimicrobial peptide and preparation method thereof |
Publications (2)
Publication Number | Publication Date |
---|---|
CN104017087A CN104017087A (en) | 2014-09-03 |
CN104017087B true CN104017087B (en) | 2016-03-09 |
Family
ID=51434121
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201410284682.3A Expired - Fee Related CN104017087B (en) | 2014-06-24 | 2014-06-24 | One boar derived antimicrobial peptide and preparation method thereof |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN104017087B (en) |
Families Citing this family (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN104448006B (en) * | 2014-12-13 | 2015-11-18 | 青岛宏昊生物科技有限公司 | A kind of heterozygous antibacterial peptide CE-PR and application thereof |
CN105153281B (en) * | 2015-09-18 | 2018-04-03 | 广州傲农生物科技有限公司 | Antibacterial peptide HP10 and its preparation method and application |
CN105777889B (en) * | 2016-03-25 | 2019-02-01 | 东北农业大学 | A kind of heterozygosis α screw type pig derived antimicrobial peptide and its preparation method and application |
CN107090473A (en) * | 2017-05-19 | 2017-08-25 | 华南农业大学 | Antibacterial peptide PR39 and PG1 coexpression vector and turn PR39 and PG1 DNA murine preparation methods |
CN108570103B (en) * | 2018-04-03 | 2019-07-30 | 东北农业大学 | One kind is rich in tryptophan antibacterial peptide WK12 and its preparation method and application |
CN108314722B (en) * | 2018-04-27 | 2020-08-11 | 九江牧威利元科技中心(普通合伙) | Antibacterial peptide and application thereof |
CN110283253B (en) * | 2019-07-12 | 2020-04-10 | 东北农业大学 | Pig-derived hybrid antibacterial peptide MDP-2 and preparation method and application thereof |
CN113024653B (en) * | 2021-03-30 | 2022-06-17 | 山东中科康源生物科技有限公司 | Pig-derived antibacterial peptide PMAP-23 variant and application thereof in preparation of feed |
Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101509007A (en) * | 2008-12-10 | 2009-08-19 | 东北农业大学 | Synthesis of LfcinB15-Mag12 encoding gene and expression method in colon bacillus |
CN102220255A (en) * | 2010-04-14 | 2011-10-19 | 深圳市圣西马生物技术有限公司 | Recombinant antimicrobial peptide (AMP) as well as genetic engineering preparation method and application thereof |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101717737B (en) * | 2009-12-11 | 2012-05-30 | 中国科学院亚热带农业生态研究所 | Antibiotic peptide buforin II and porcine INF-alpha fusion expression pichia pastoris, and preparation method and applications thereof |
CN103435701B (en) * | 2013-07-24 | 2014-09-17 | 山西农业大学 | Pig antibacterial peptide cystatin11 fusion protein, and encoding gene and application thereof |
-
2014
- 2014-06-24 CN CN201410284682.3A patent/CN104017087B/en not_active Expired - Fee Related
Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101509007A (en) * | 2008-12-10 | 2009-08-19 | 东北农业大学 | Synthesis of LfcinB15-Mag12 encoding gene and expression method in colon bacillus |
CN102220255A (en) * | 2010-04-14 | 2011-10-19 | 深圳市圣西马生物技术有限公司 | Recombinant antimicrobial peptide (AMP) as well as genetic engineering preparation method and application thereof |
Also Published As
Publication number | Publication date |
---|---|
CN104017087A (en) | 2014-09-03 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN104017087B (en) | One boar derived antimicrobial peptide and preparation method thereof | |
JP6594293B2 (en) | Purification of triple helix proteins | |
Ramos et al. | Recombinant expression and purification of the antimicrobial peptide magainin‐2 | |
CN105219779B (en) | Red claw crayfish coagulogen and preparation method and application | |
CN104017086B (en) | A kind of fusion antibacterial peptide and preparation method thereof | |
Yu et al. | Secretory production of antimicrobial peptides in Escherichia coli using the catalytic domain of a cellulase as fusion partner | |
Yue et al. | Separation and purification of a keratinase as pesticide against root-knot nematodes | |
CN104017085A (en) | PAMP37-PR39 fused antibacterial peptide and preparation method thereof | |
CN103621795A (en) | Application of hybrid antibacterial peptide as the feed supplement | |
CN103833839B (en) | C-type agglutinin and its preparation method and application | |
CN101948839B (en) | Antimicrobial peptide gene from pinctada fucata and application | |
CN101319216B (en) | Preparation for recombined cultivated silkworm antimicrobial peptide CM4 and purification process | |
CN103641901A (en) | Antibacterial peptide | |
CN107475222B (en) | Genetically engineered heat-resistant human lysozyme | |
WO2007033529A1 (en) | A gene encoding antibacterial protein of fenneropenaeus chinensis and its recombination expression method and uses | |
CN106478812B (en) | Serine protease inhibitor-3, and function, preparation method and application thereof | |
CN101265291A (en) | Recombination pig origin antibiotic peptide PG4 and its biological synthesis method and application | |
Yang et al. | Efficient extracellular expression of phospholipase D in Escherichia coli with an optimized signal peptide | |
CN102094024A (en) | Plutella xylostella cecropin gene, encoded protein, corresponding expression system and application | |
CN102532325A (en) | Method for preparing cecropins AD and frog Buforin II fusion antimicrobial peptide by using hydroxylamine cutting method, and uses thereof | |
CN102276729A (en) | Antibacterial peptide bovine lactoferricin-thanatin (LF-TH) and Escherichia coli recombination preparation method thereof | |
CN101914546B (en) | Amphioxus saccharide pattern-recognition molecule Bjfcn1 gene and application thereof | |
CN116143903B (en) | Peptidoglycan recognition protein-3, preparation method and application thereof | |
JP2021185912A (en) | Novel chitosanase chi1 as well as coding gene and application thereof | |
CN103194442A (en) | Novel polypeptide and hydrolyzed antibacterial peptide and preparation method thereof |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
ASS | Succession or assignment of patent right |
Owner name: KEMEI BORUI TECHNOLOGY (BEIJING) CO., LTD. Free format text: FORMER OWNER: REN JIANTING Effective date: 20150320 |
|
C41 | Transfer of patent application or patent right or utility model | ||
TA01 | Transfer of patent application right |
Effective date of registration: 20150320 Address after: 100085 No. 1, building 5, building ten, No. 8, 805 street, Beijing, Haidian District Applicant after: Kemei Borui Technology (Beijing) Co.,Ltd. Address before: 100085 splendid international ten, 5-805 street, Beijing, Haidian District Applicant before: Ren Jianting |
|
C14 | Grant of patent or utility model | ||
GR01 | Patent grant | ||
CB03 | Change of inventor or designer information |
Inventor after: Yang Xiaolan Inventor before: Ren Jianting |
|
CB03 | Change of inventor or designer information | ||
TR01 | Transfer of patent right | ||
TR01 | Transfer of patent right |
Effective date of registration: 20180521 Address after: 100096 Changping District 11, 3, unit 11, No. 30 building, No. 30, Yu Zhi Dong Road, Beijing. Patentee after: Beijing Botai Rui Kang Technology Co., Ltd. Address before: 100085, 5 floor 8, 1 Street, ten Street, Haidian District, Beijing. Patentee before: Kemei Borui Technology (Beijing) Co.,Ltd. |
|
CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20160309 Termination date: 20190624 |
|
CF01 | Termination of patent right due to non-payment of annual fee | ||
RR01 | Reinstatement of patent right |
Former decision: termination of patent right due to unpaid annual fee Former decision publication date: 20200623 |
|
RR01 | Reinstatement of patent right | ||
CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20160309 Termination date: 20210624 |
|
CF01 | Termination of patent right due to non-payment of annual fee |