KR101986358B1 - 병원균을 조절하기 위한 아미노산 서열 - Google Patents
병원균을 조절하기 위한 아미노산 서열 Download PDFInfo
- Publication number
- KR101986358B1 KR101986358B1 KR1020147009805A KR20147009805A KR101986358B1 KR 101986358 B1 KR101986358 B1 KR 101986358B1 KR 1020147009805 A KR1020147009805 A KR 1020147009805A KR 20147009805 A KR20147009805 A KR 20147009805A KR 101986358 B1 KR101986358 B1 KR 101986358B1
- Authority
- KR
- South Korea
- Prior art keywords
- peptide
- amino acid
- group
- seq
- acid sequence
- 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.)
- Active
Links
- 125000003275 alpha amino acid group Chemical group 0.000 title claims 15
- 244000052769 pathogen Species 0.000 title abstract description 21
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 113
- 102000044503 Antimicrobial Peptides Human genes 0.000 claims abstract description 54
- 108700042778 Antimicrobial Peptides Proteins 0.000 claims abstract description 54
- 230000000845 anti-microbial effect Effects 0.000 claims abstract description 19
- 241000894006 Bacteria Species 0.000 claims abstract description 18
- 239000000203 mixture Substances 0.000 claims abstract description 16
- 239000003910 polypeptide antibiotic agent Substances 0.000 claims abstract description 15
- 230000014509 gene expression Effects 0.000 claims abstract description 12
- 229960005486 vaccine Drugs 0.000 claims abstract description 11
- 239000002671 adjuvant Substances 0.000 claims abstract description 9
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 7
- 238000003786 synthesis reaction Methods 0.000 claims abstract description 5
- 241000251468 Actinopterygii Species 0.000 claims description 35
- 238000002649 immunization Methods 0.000 claims description 17
- 230000003053 immunization Effects 0.000 claims description 16
- 108020004414 DNA Proteins 0.000 claims description 11
- 102000053602 DNA Human genes 0.000 claims description 11
- 239000000427 antigen Substances 0.000 claims description 10
- 102000036639 antigens Human genes 0.000 claims description 10
- 108091007433 antigens Proteins 0.000 claims description 10
- 238000000034 method Methods 0.000 claims description 9
- 230000001580 bacterial effect Effects 0.000 claims description 7
- 238000007654 immersion Methods 0.000 claims description 6
- 239000003674 animal food additive Substances 0.000 claims description 5
- 238000005516 engineering process Methods 0.000 claims description 5
- 230000028993 immune response Effects 0.000 claims description 4
- 239000007924 injection Substances 0.000 claims description 4
- 238000002347 injection Methods 0.000 claims description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 3
- 241000124008 Mammalia Species 0.000 claims description 2
- 239000004599 antimicrobial Substances 0.000 claims description 2
- 244000052616 bacterial pathogen Species 0.000 claims description 2
- 125000004122 cyclic group Chemical group 0.000 claims description 2
- 239000008194 pharmaceutical composition Substances 0.000 claims description 2
- 230000003612 virological effect Effects 0.000 claims description 2
- 239000004480 active ingredient Substances 0.000 claims 1
- 244000053095 fungal pathogen Species 0.000 claims 1
- 239000012646 vaccine adjuvant Substances 0.000 claims 1
- 229940124931 vaccine adjuvant Drugs 0.000 claims 1
- 244000052613 viral pathogen Species 0.000 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 58
- 241000276707 Tilapia Species 0.000 abstract description 16
- 241000700605 Viruses Species 0.000 abstract description 12
- 241000233866 Fungi Species 0.000 abstract description 9
- 239000000284 extract Substances 0.000 abstract description 4
- 241000276719 Oreochromis Species 0.000 abstract 1
- 238000009472 formulation Methods 0.000 abstract 1
- 238000001823 molecular biology technique Methods 0.000 abstract 1
- 241001465754 Metazoa Species 0.000 description 49
- 239000002953 phosphate buffered saline Substances 0.000 description 42
- 108010058846 Ovalbumin Proteins 0.000 description 41
- 229940092253 ovalbumin Drugs 0.000 description 41
- 235000019688 fish Nutrition 0.000 description 39
- 150000001413 amino acids Chemical class 0.000 description 24
- 108090000623 proteins and genes Proteins 0.000 description 22
- 102000004169 proteins and genes Human genes 0.000 description 22
- 241000699670 Mus sp. Species 0.000 description 21
- 210000004027 cell Anatomy 0.000 description 21
- 208000015181 infectious disease Diseases 0.000 description 21
- 235000018102 proteins Nutrition 0.000 description 21
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 18
- 238000012360 testing method Methods 0.000 description 18
- 241000276703 Oreochromis niloticus Species 0.000 description 16
- 241000607528 Aeromonas hydrophila Species 0.000 description 15
- 229940027941 immunoglobulin g Drugs 0.000 description 14
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 12
- 239000007928 intraperitoneal injection Substances 0.000 description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 241000235058 Komagataella pastoris Species 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 230000037396 body weight Effects 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000002158 endotoxin Substances 0.000 description 8
- 229920006008 lipopolysaccharide Polymers 0.000 description 8
- 230000004083 survival effect Effects 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 239000012228 culture supernatant Substances 0.000 description 7
- 239000002904 solvent Substances 0.000 description 7
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 239000013642 negative control Substances 0.000 description 6
- 150000007523 nucleic acids Chemical class 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 231100000673 dose–response relationship Toxicity 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 231100000636 lethal dose Toxicity 0.000 description 5
- 210000004379 membrane Anatomy 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 238000003752 polymerase chain reaction Methods 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 125000003345 AMP group Chemical group 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 229920006227 ethylene-grafted-maleic anhydride Polymers 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 230000028996 humoral immune response Effects 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 230000001717 pathogenic effect Effects 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 210000004988 splenocyte Anatomy 0.000 description 4
- 238000007619 statistical method Methods 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 3
- 102000004388 Interleukin-4 Human genes 0.000 description 3
- 108090000978 Interleukin-4 Proteins 0.000 description 3
- 241000589516 Pseudomonas Species 0.000 description 3
- 238000000540 analysis of variance Methods 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 125000002091 cationic group Chemical group 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 3
- 230000001747 exhibiting effect Effects 0.000 description 3
- 210000002816 gill Anatomy 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000010839 reverse transcription Methods 0.000 description 3
- 229920002477 rna polymer Polymers 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 238000013207 serial dilution Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 230000035899 viability Effects 0.000 description 3
- 238000005303 weighing Methods 0.000 description 3
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 2
- 241000607534 Aeromonas Species 0.000 description 2
- 101710150620 Anionic peptide Proteins 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000252233 Cyprinus carpio Species 0.000 description 2
- 241000192125 Firmicutes Species 0.000 description 2
- TVUWMSBGMVAHSJ-KBPBESRZSA-N Gly-Leu-Phe Chemical compound NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 TVUWMSBGMVAHSJ-KBPBESRZSA-N 0.000 description 2
- 241000701372 Iridovirus Species 0.000 description 2
- 239000012097 Lipofectamine 2000 Substances 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 108010038807 Oligopeptides Proteins 0.000 description 2
- 102000015636 Oligopeptides Human genes 0.000 description 2
- HTXVATDVCRFORF-MGHWNKPDSA-N Phe-Ile-His Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](CC2=CC=CC=C2)N HTXVATDVCRFORF-MGHWNKPDSA-N 0.000 description 2
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 241000191967 Staphylococcus aureus Species 0.000 description 2
- 230000024932 T cell mediated immunity Effects 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 238000009360 aquaculture Methods 0.000 description 2
- 244000144974 aquaculture Species 0.000 description 2
- 238000010804 cDNA synthesis Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 108010026364 glycyl-glycyl-leucine Proteins 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 210000005007 innate immune system Anatomy 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000002955 isolation 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
- 238000012454 limulus amebocyte lysate test Methods 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 238000003359 percent control normalization Methods 0.000 description 2
- 108010051242 phenylalanylserine Proteins 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DSLBDPPHINVUID-REOHCLBHSA-N (2s)-2-aminobutanediamide Chemical compound NC(=O)[C@@H](N)CC(N)=O DSLBDPPHINVUID-REOHCLBHSA-N 0.000 description 1
- XJOTXKZIRSHZQV-RXHOOSIZSA-N (3S)-3-amino-4-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S,3S)-1-[[(1R,6R,12R,17R,20S,23S,26R,31R,34R,39R,42S,45S,48S,51S,59S)-51-(4-aminobutyl)-31-[[(2S)-6-amino-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxohexan-2-yl]carbamoyl]-20-benzyl-23-[(2S)-butan-2-yl]-45-(3-carbamimidamidopropyl)-48-(hydroxymethyl)-42-(1H-imidazol-4-ylmethyl)-59-(2-methylsulfanylethyl)-7,10,19,22,25,33,40,43,46,49,52,54,57,60,63,64-hexadecaoxo-3,4,14,15,28,29,36,37-octathia-8,11,18,21,24,32,41,44,47,50,53,55,58,61,62,65-hexadecazatetracyclo[32.19.8.26,17.212,39]pentahexacontan-26-yl]amino]-3-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-4-oxobutanoic acid Chemical compound CC[C@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1cnc[nH]1)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)[C@@H](C)O)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@@H]2CSSC[C@@H]3NC(=O)[C@@H]4CSSC[C@H](NC(=O)[C@H](Cc5ccccc5)NC(=O)[C@@H](NC1=O)[C@@H](C)CC)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](Cc1cnc[nH]1)NC3=O)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N2)C(=O)NCC(=O)N4)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XJOTXKZIRSHZQV-RXHOOSIZSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 241001578974 Achlya <moth> Species 0.000 description 1
- 101710186708 Agglutinin Proteins 0.000 description 1
- QCTFKEJEIMPOLW-JURCDPSOSA-N Ala-Ile-Phe Chemical compound C[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 QCTFKEJEIMPOLW-JURCDPSOSA-N 0.000 description 1
- XPSGESXVBSQZPL-SRVKXCTJSA-N Arg-Arg-Arg Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O XPSGESXVBSQZPL-SRVKXCTJSA-N 0.000 description 1
- RGKKALNPOYURGE-ZKWXMUAHSA-N Asp-Ala-Val Chemical compound N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)O RGKKALNPOYURGE-ZKWXMUAHSA-N 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000222122 Candida albicans Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 102000000541 Defensins Human genes 0.000 description 1
- 108010002069 Defensins Proteins 0.000 description 1
- 208000035240 Disease Resistance Diseases 0.000 description 1
- 241000607471 Edwardsiella tarda Species 0.000 description 1
- 241000305071 Enterobacterales Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- MADFVRSKEIEZHZ-DCAQKATOSA-N Gln-Gln-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CCC(=O)N)N MADFVRSKEIEZHZ-DCAQKATOSA-N 0.000 description 1
- QITBQGJOXQYMOA-ZETCQYMHSA-N Gly-Gly-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)CNC(=O)CN QITBQGJOXQYMOA-ZETCQYMHSA-N 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 241000606790 Haemophilus Species 0.000 description 1
- 241000148627 Hirame novirhabdovirus Species 0.000 description 1
- SYMSVYVUSPSAAO-IHRRRGAJSA-N His-Arg-Leu Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(O)=O SYMSVYVUSPSAAO-IHRRRGAJSA-N 0.000 description 1
- YADRBUZBKHHDAO-XPUUQOCRSA-N His-Gly-Ala Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)NCC(=O)N[C@@H](C)C(O)=O YADRBUZBKHHDAO-XPUUQOCRSA-N 0.000 description 1
- RGPWUJOMKFYFSR-QWRGUYRKSA-N His-Gly-Leu Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)NCC(=O)N[C@@H](CC(C)C)C(O)=O RGPWUJOMKFYFSR-QWRGUYRKSA-N 0.000 description 1
- NDKSHNQINMRKHT-PEXQALLHSA-N His-Ile-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)NCC(=O)O)NC(=O)[C@H](CC1=CN=CN1)N NDKSHNQINMRKHT-PEXQALLHSA-N 0.000 description 1
- 101000928314 Homo sapiens Aldehyde oxidase Proteins 0.000 description 1
- 101710146024 Horcolin Proteins 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- HLYBGMZJVDHJEO-CYDGBPFRSA-N Ile-Arg-Arg Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N HLYBGMZJVDHJEO-CYDGBPFRSA-N 0.000 description 1
- UASTVUQJMLZWGG-PEXQALLHSA-N Ile-His-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)NCC(=O)O)N UASTVUQJMLZWGG-PEXQALLHSA-N 0.000 description 1
- YNMQUIVKEFRCPH-QSFUFRPTSA-N Ile-Ile-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)O)N YNMQUIVKEFRCPH-QSFUFRPTSA-N 0.000 description 1
- HZVRQFKRALAMQS-SLBDDTMCSA-N Ile-Trp-Asp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)N[C@@H](CC(=O)O)C(=O)O)N HZVRQFKRALAMQS-SLBDDTMCSA-N 0.000 description 1
- 241000711804 Infectious hematopoietic necrosis virus Species 0.000 description 1
- 241000710921 Infectious pancreatic necrosis virus Species 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 238000012313 Kruskal-Wallis test Methods 0.000 description 1
- 239000012480 LAL reagent Substances 0.000 description 1
- 101710189395 Lectin Proteins 0.000 description 1
- VZBIUJURDLFFOE-IHRRRGAJSA-N Leu-His-Arg Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O VZBIUJURDLFFOE-IHRRRGAJSA-N 0.000 description 1
- NFLFJGGKOHYZJF-BJDJZHNGSA-N Lys-Ala-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCCN NFLFJGGKOHYZJF-BJDJZHNGSA-N 0.000 description 1
- GKFNXYMAMKJSKD-NHCYSSNCSA-N Lys-Asp-Val Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O GKFNXYMAMKJSKD-NHCYSSNCSA-N 0.000 description 1
- WOEDRPCHKPSFDT-MXAVVETBSA-N Lys-His-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CC1=CN=CN1)NC(=O)[C@H](CCCCN)N WOEDRPCHKPSFDT-MXAVVETBSA-N 0.000 description 1
- ZMMDPRTXLAEMOD-BZSNNMDCSA-N Lys-His-Phe Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O ZMMDPRTXLAEMOD-BZSNNMDCSA-N 0.000 description 1
- 101710179758 Mannose-specific lectin Proteins 0.000 description 1
- 101710150763 Mannose-specific lectin 1 Proteins 0.000 description 1
- 101710150745 Mannose-specific lectin 2 Proteins 0.000 description 1
- 241000863434 Myxococcales Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 101100342977 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) leu-1 gene Proteins 0.000 description 1
- 241000187654 Nocardia Species 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 239000012979 RPMI medium Substances 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 241000269435 Rana <genus> Species 0.000 description 1
- 241000467915 Rana grylio iridovirus Species 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 241000233667 Saprolegnia Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- BTKUIVBNGBFTTP-WHFBIAKZSA-N Ser-Ala-Gly Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C)C(=O)NCC(O)=O BTKUIVBNGBFTTP-WHFBIAKZSA-N 0.000 description 1
- JZRYFUGREMECBH-XPUUQOCRSA-N Ser-Val-Gly Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O JZRYFUGREMECBH-XPUUQOCRSA-N 0.000 description 1
- 241001479108 Snakehead virus Species 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 238000003639 Student–Newman–Keuls (SNK) method Methods 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- IDKGBVZGNTYYCC-QXEWZRGKSA-N Val-Asn-Pro Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(O)=O IDKGBVZGNTYYCC-QXEWZRGKSA-N 0.000 description 1
- 241000607598 Vibrio Species 0.000 description 1
- 241000607284 Vibrio sp. Species 0.000 description 1
- 206010058874 Viraemia Diseases 0.000 description 1
- 241000711825 Viral hemorrhagic septicemia virus Species 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 210000000683 abdominal cavity Anatomy 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000004721 adaptive immunity Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 239000000910 agglutinin Substances 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- 208000007502 anemia Diseases 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 229940095731 candida albicans Drugs 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000001332 colony forming effect Effects 0.000 description 1
- 230000003750 conditioning effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000000120 cytopathologic effect Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000008260 defense mechanism Effects 0.000 description 1
- 230000001687 destabilization Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- FFYPMLJYZAEMQB-UHFFFAOYSA-N diethyl pyrocarbonate Chemical compound CCOC(=O)OC(=O)OCC FFYPMLJYZAEMQB-UHFFFAOYSA-N 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000007598 dipping method Methods 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- 229940125532 enzyme inhibitor Drugs 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 208000010932 epithelial neoplasm Diseases 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000005189 flocculation Methods 0.000 description 1
- 230000016615 flocculation Effects 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 239000013505 freshwater Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000004943 gill filament Anatomy 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010015792 glycyllysine Proteins 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 230000012447 hatching Effects 0.000 description 1
- 230000002008 hemorrhagic effect Effects 0.000 description 1
- 102000018511 hepcidin Human genes 0.000 description 1
- 108060003558 hepcidin Proteins 0.000 description 1
- 229940066919 hepcidin Drugs 0.000 description 1
- 108010028295 histidylhistidine Proteins 0.000 description 1
- 108010092114 histidylphenylalanine Proteins 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000005965 immune activity Effects 0.000 description 1
- 230000008076 immune mechanism Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 229940028885 interleukin-4 Drugs 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 210000003097 mucus Anatomy 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 229940107700 pyruvic acid Drugs 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 230000002245 ribonucleolytic effect Effects 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 239000013535 sea water Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 235000015170 shellfish Nutrition 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 230000009469 supplementation Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 108010073969 valyllysine Proteins 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/39—Medicinal preparations containing antigens or antibodies characterised by the immunostimulating additives, e.g. chemical adjuvants
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1706—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/10—Antimycotics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/461—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Polymers & Plastics (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Gastroenterology & Hepatology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Animal Husbandry (AREA)
- Food Science & Technology (AREA)
- Epidemiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Marine Sciences & Fisheries (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Virology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Fodder In General (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CU2011-0181 | 2011-09-30 | ||
| CU20110181A CU24076B1 (es) | 2011-09-30 | 2011-09-30 | Composición para el control de patógenos |
| PCT/CU2012/000005 WO2013044890A1 (es) | 2011-09-30 | 2012-10-01 | Secuencias de aminoácidos para el control de patógenos |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR20140070597A KR20140070597A (ko) | 2014-06-10 |
| KR101986358B1 true KR101986358B1 (ko) | 2019-06-05 |
Family
ID=47143463
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1020147009805A Active KR101986358B1 (ko) | 2011-09-30 | 2012-10-01 | 병원균을 조절하기 위한 아미노산 서열 |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US9549978B2 (enExample) |
| EP (1) | EP2767290B1 (enExample) |
| JP (1) | JP6034385B2 (enExample) |
| KR (1) | KR101986358B1 (enExample) |
| CN (1) | CN103874502B (enExample) |
| AR (1) | AR088176A1 (enExample) |
| AU (1) | AU2012315083B2 (enExample) |
| BR (1) | BR112014007491B1 (enExample) |
| CA (1) | CA2849040C (enExample) |
| CL (1) | CL2014000760A1 (enExample) |
| CU (1) | CU24076B1 (enExample) |
| ES (1) | ES2600903T3 (enExample) |
| MX (1) | MX348934B (enExample) |
| RU (1) | RU2636001C2 (enExample) |
| WO (1) | WO2013044890A1 (enExample) |
| ZA (1) | ZA201402171B (enExample) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104262485B (zh) * | 2014-04-15 | 2017-01-18 | 四川农业大学 | 罗非鱼sIgM截短重链恒定区蛋白多克隆抗体及其制备方法 |
| CN105061575B (zh) * | 2015-02-03 | 2020-08-04 | 浙江海洋学院 | 一种金枪鱼肝脏抗菌肽及其制备方法和用途 |
| CN109350731A (zh) * | 2018-12-18 | 2019-02-19 | 汕尾市维明生物科技股份有限公司 | 一种罗非鱼蛋白肽在制备免疫制剂中的应用 |
| CN112979763A (zh) * | 2021-03-03 | 2021-06-18 | 山东大学 | 一种基于可溶性疏水载体抗菌肽Oreoch-2的液相合成方法 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030105281A1 (en) | 2000-08-15 | 2003-06-05 | Noga Edward J. | Antimicrobial peptides isolated from mast cells |
| US20060093596A1 (en) | 2002-08-22 | 2006-05-04 | Susan Douglas | Genomic approach to identification of novel broad-spectrum antimicrobial peptides from bony fish |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030056244A1 (en) * | 2000-05-02 | 2003-03-20 | Ning Huang | Feed additive compositions and methods |
| US6753407B2 (en) * | 2000-08-15 | 2004-06-22 | North Carolina State University | Antimicrobial peptides isolated from fish |
| EP1838331A4 (en) * | 2004-12-15 | 2012-12-26 | Univ Colorado | ANTIMICROBIAL PEPTIDES AND METHOD OF USE |
| RU2302467C1 (ru) * | 2005-12-01 | 2007-07-10 | Институт биоорганической химии им. академиков М.М. Шемякина и Ю.А. Овчинникова Российской академии наук | Пептиды латарцины, проявляющие антимикробную активность |
| US20090186047A1 (en) * | 2006-04-25 | 2009-07-23 | Intercell Ag | HCV Vaccinations |
| TWI299335B (en) * | 2006-12-05 | 2008-08-01 | Academia Sinica | Anti-microbal peptides and uses thereof |
| WO2009149554A1 (en) * | 2008-06-11 | 2009-12-17 | National Research Council Of Canada | Antimicrobial components of the mucus and extruded slime of hagfish (myxine glutinosa) |
| CN103665170A (zh) * | 2008-12-05 | 2014-03-26 | 安吉奥开米公司 | 肽治疗剂轭合物及其应用 |
| US20100184684A1 (en) * | 2009-01-06 | 2010-07-22 | C3 Jian, Inc. | Antibacterial and antifungal peptides |
| US8389679B2 (en) * | 2009-02-05 | 2013-03-05 | The Regents Of The University Of California | Targeted antimicrobial moieties |
| CN101559214A (zh) * | 2009-05-27 | 2009-10-21 | 珍奥集团股份有限公司 | 具有增强免疫功能作用的组合物及其用途 |
| CN102021172A (zh) * | 2010-06-23 | 2011-04-20 | 广西壮族自治区水产研究所 | 罗非鱼白细胞 cAMP 诱导早期抑制因子基因序列及用途 |
| EP2661451B1 (en) * | 2011-01-07 | 2019-10-09 | Valiant Biopharma SDN BHD | Antimicrobial fusion compounds and uses thereof |
-
2011
- 2011-09-30 CU CU20110181A patent/CU24076B1/es active IP Right Grant
-
2012
- 2012-09-27 AR ARP120103606A patent/AR088176A1/es unknown
- 2012-10-01 CN CN201280050943.4A patent/CN103874502B/zh active Active
- 2012-10-01 EP EP12783080.0A patent/EP2767290B1/en not_active Not-in-force
- 2012-10-01 JP JP2014532244A patent/JP6034385B2/ja active Active
- 2012-10-01 CA CA2849040A patent/CA2849040C/en active Active
- 2012-10-01 WO PCT/CU2012/000005 patent/WO2013044890A1/es not_active Ceased
- 2012-10-01 RU RU2014117659A patent/RU2636001C2/ru active
- 2012-10-01 AU AU2012315083A patent/AU2012315083B2/en active Active
- 2012-10-01 MX MX2014003892A patent/MX348934B/es active IP Right Grant
- 2012-10-01 KR KR1020147009805A patent/KR101986358B1/ko active Active
- 2012-10-01 BR BR112014007491-7A patent/BR112014007491B1/pt active IP Right Grant
- 2012-10-01 ES ES12783080.0T patent/ES2600903T3/es active Active
- 2012-10-01 US US14/346,562 patent/US9549978B2/en active Active
-
2014
- 2014-03-24 ZA ZA2014/02171A patent/ZA201402171B/en unknown
- 2014-03-27 CL CL2014000760A patent/CL2014000760A1/es unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030105281A1 (en) | 2000-08-15 | 2003-06-05 | Noga Edward J. | Antimicrobial peptides isolated from mast cells |
| US20060093596A1 (en) | 2002-08-22 | 2006-05-04 | Susan Douglas | Genomic approach to identification of novel broad-spectrum antimicrobial peptides from bony fish |
Non-Patent Citations (3)
| Title |
|---|
| GeneBank: GR604642 (2010. 5.22.)* |
| GeneBank: GR645750 (2010. 5.22.)* |
| GeneBank: GR647541 (2010. 5.22.)* |
Also Published As
| Publication number | Publication date |
|---|---|
| ZA201402171B (en) | 2015-12-23 |
| CU24076B1 (es) | 2015-01-29 |
| CA2849040C (en) | 2019-11-26 |
| ES2600903T3 (es) | 2017-02-13 |
| KR20140070597A (ko) | 2014-06-10 |
| AR088176A1 (es) | 2014-05-14 |
| RU2014117659A (ru) | 2015-11-10 |
| CA2849040A1 (en) | 2013-04-04 |
| CL2014000760A1 (es) | 2014-08-22 |
| CU20110181A7 (es) | 2013-05-31 |
| US9549978B2 (en) | 2017-01-24 |
| US20140294871A1 (en) | 2014-10-02 |
| MX348934B (es) | 2017-07-03 |
| EP2767290A1 (en) | 2014-08-20 |
| WO2013044890A1 (es) | 2013-04-04 |
| AU2012315083A1 (en) | 2014-05-08 |
| AU2012315083B2 (en) | 2016-02-25 |
| BR112014007491A2 (pt) | 2017-04-04 |
| CN103874502B (zh) | 2015-11-25 |
| CN103874502A (zh) | 2014-06-18 |
| EP2767290B1 (en) | 2016-09-14 |
| BR112014007491B1 (pt) | 2022-03-03 |
| JP6034385B2 (ja) | 2016-11-30 |
| RU2636001C2 (ru) | 2017-11-17 |
| MX2014003892A (es) | 2014-07-09 |
| JP2014533931A (ja) | 2014-12-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US11603391B2 (en) | CATH2 derivatives | |
| Wang et al. | Functions of antimicrobial peptides in gut homeostasis | |
| KR101986358B1 (ko) | 병원균을 조절하기 위한 아미노산 서열 | |
| Sathyamoorthi et al. | Therapeutic cationic antimicrobial peptide (CAP) derived from fish aspartic proteinase Cathepsin D and its antimicrobial mechanism | |
| Li et al. | Antimicrobial peptides: sources, expression systems, and applications | |
| Wang et al. | Molecular characterization, phylogenetic analysis and adjuvant effect of channel catfish interleukin-1βs against Streptococcus iniae | |
| CA2873599A1 (en) | Peptides inducing an immune response against copepods and/or the development of a mucous shield in fish; vaccines, uses and methods for modulating the fish immune response and/or for inducing development of a mucous shield in fish | |
| KR101384577B1 (ko) | 황다랑어 유래의 새로운 항미생물성 펩타이드 및 이의 용도 | |
| CN112778424A (zh) | 嵌合肽r7及其应用 | |
| JP6921387B2 (ja) | 抗微生物ポリペプチド | |
| Wilson et al. | Milk-derived antimicrobial peptides to protect against Neonatal Diarrheal Disease: An alternative to antibiotics | |
| Blumhardt | Antimicrobial peptides: immunomodulatory and therapeutic potential for use in Atlantic salmon (Salmo salar) | |
| Chanu et al. | Structure activity relationship of buffalo antibacterial hepcidin analogs | |
| KR101919314B1 (ko) | 구제역 바이러스 백신 조성물 | |
| KR101754756B1 (ko) | 재조합 백시니아바이러스를 이용한 탄저/두창 2가 백신후보주 | |
| CN117279934A (zh) | 用于抑制猪链球菌的cath2及其衍生物 | |
| Douglas | Marine Flatfish-Derived Bioactive Peptides: From the |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PA0105 | International application |
Patent event date: 20140414 Patent event code: PA01051R01D Comment text: International Patent Application |
|
| PG1501 | Laying open of application | ||
| A201 | Request for examination | ||
| PA0201 | Request for examination |
Patent event code: PA02012R01D Patent event date: 20170626 Comment text: Request for Examination of Application |
|
| E902 | Notification of reason for refusal | ||
| PE0902 | Notice of grounds for rejection |
Comment text: Notification of reason for refusal Patent event date: 20180810 Patent event code: PE09021S01D |
|
| E701 | Decision to grant or registration of patent right | ||
| PE0701 | Decision of registration |
Patent event code: PE07011S01D Comment text: Decision to Grant Registration Patent event date: 20190326 |
|
| GRNT | Written decision to grant | ||
| PR0701 | Registration of establishment |
Comment text: Registration of Establishment Patent event date: 20190530 Patent event code: PR07011E01D |
|
| PR1002 | Payment of registration fee |
Payment date: 20190531 End annual number: 3 Start annual number: 1 |
|
| PG1601 | Publication of registration | ||
| PR1001 | Payment of annual fee |
Payment date: 20220428 Start annual number: 4 End annual number: 4 |
|
| PR1001 | Payment of annual fee |
Payment date: 20240307 Start annual number: 6 End annual number: 6 |
|
| PR1001 | Payment of annual fee |
Payment date: 20250326 Start annual number: 7 End annual number: 7 |