NO315050B1 - Kapsiddannende og cysteinmodifisert kim¶rt MS2-kappeprotein - Google Patents
Kapsiddannende og cysteinmodifisert kim¶rt MS2-kappeprotein Download PDFInfo
- Publication number
- NO315050B1 NO315050B1 NO19934842A NO934842A NO315050B1 NO 315050 B1 NO315050 B1 NO 315050B1 NO 19934842 A NO19934842 A NO 19934842A NO 934842 A NO934842 A NO 934842A NO 315050 B1 NO315050 B1 NO 315050B1
- Authority
- NO
- Norway
- Prior art keywords
- coat protein
- modified
- protein according
- cysteine
- cysteine residue
- Prior art date
Links
- 101710132601 Capsid protein Proteins 0.000 title claims abstract description 65
- 101710094648 Coat protein Proteins 0.000 title claims abstract description 65
- 101710125418 Major capsid protein Proteins 0.000 title claims abstract description 65
- 101710141454 Nucleoprotein Proteins 0.000 title claims abstract description 65
- 101710083689 Probable capsid protein Proteins 0.000 title claims abstract description 65
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 title claims abstract description 63
- 210000000234 capsid Anatomy 0.000 claims abstract description 39
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims abstract description 37
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 25
- 235000018102 proteins Nutrition 0.000 claims abstract description 24
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 24
- 238000003780 insertion Methods 0.000 claims abstract description 9
- 230000037431 insertion Effects 0.000 claims abstract description 9
- 239000000203 mixture Substances 0.000 claims description 15
- 239000002299 complementary DNA Substances 0.000 claims description 12
- 238000000034 method Methods 0.000 claims description 10
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 9
- 235000018417 cysteine Nutrition 0.000 claims description 9
- 241000588724 Escherichia coli Species 0.000 claims description 8
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 8
- 125000006850 spacer group Chemical group 0.000 claims description 7
- 238000002741 site-directed mutagenesis Methods 0.000 claims description 6
- 108091005573 modified proteins Proteins 0.000 claims description 5
- 102000035118 modified proteins Human genes 0.000 claims description 5
- 230000008685 targeting Effects 0.000 claims description 5
- 229960005486 vaccine Drugs 0.000 claims description 5
- 239000004471 Glycine Substances 0.000 claims description 4
- 239000013604 expression vector Substances 0.000 claims description 4
- 108020004414 DNA Proteins 0.000 claims description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 3
- 230000000890 antigenic effect Effects 0.000 claims description 3
- 229930182830 galactose Natural products 0.000 claims description 3
- 238000002360 preparation method Methods 0.000 claims description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims description 3
- JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 claims description 2
- BQWBEDSJTMWJAE-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 4-[(2-iodoacetyl)amino]benzoate Chemical compound C1=CC(NC(=O)CI)=CC=C1C(=O)ON1C(=O)CCC1=O BQWBEDSJTMWJAE-UHFFFAOYSA-N 0.000 claims description 2
- DIYPCWKHSODVAP-UHFFFAOYSA-N 1-[3-(2,5-dioxopyrrol-1-yl)benzoyl]oxy-2,5-dioxopyrrolidine-3-sulfonic acid Chemical compound O=C1C(S(=O)(=O)O)CC(=O)N1OC(=O)C1=CC=CC(N2C(C=CC2=O)=O)=C1 DIYPCWKHSODVAP-UHFFFAOYSA-N 0.000 claims description 2
- 239000003431 cross linking reagent Substances 0.000 claims description 2
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 108020004635 Complementary DNA Proteins 0.000 claims 1
- 230000001588 bifunctional effect Effects 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 2
- 239000000872 buffer Substances 0.000 description 14
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 13
- 108090000765 processed proteins & peptides Proteins 0.000 description 11
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 239000012634 fragment Substances 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
- KIUMMUBSPKGMOY-UHFFFAOYSA-N 3,3'-Dithiobis(6-nitrobenzoic acid) Chemical compound C1=C([N+]([O-])=O)C(C(=O)O)=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C(O)=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- 150000001413 amino acids Chemical group 0.000 description 6
- 150000002256 galaktoses Chemical class 0.000 description 6
- 229920000136 polysorbate Polymers 0.000 description 6
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 6
- 101100386050 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-14 gene Proteins 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 4
- 229960000723 ampicillin Drugs 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 229940098773 bovine serum albumin Drugs 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 239000004971 Cross linker Substances 0.000 description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
- 101710154606 Hemagglutinin Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 3
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 3
- 101710176177 Protein A56 Proteins 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 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 3
- 230000000694 effects Effects 0.000 description 3
- 239000000185 hemagglutinin Substances 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 101710091045 Envelope protein Proteins 0.000 description 2
- 241000724791 Filamentous phage Species 0.000 description 2
- 108700012941 GNRH1 Proteins 0.000 description 2
- 239000000579 Gonadotropin-Releasing Hormone Substances 0.000 description 2
- 102100034349 Integrase Human genes 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 101710188315 Protein X Proteins 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000013256 coordination polymer Substances 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 238000005538 encapsulation Methods 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000001965 increasing effect Effects 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
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000001338 self-assembly Methods 0.000 description 2
- GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 150000003573 thiols Chemical class 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 241000712461 unidentified influenza virus Species 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- RBNSZWOCWHGHMR-UHFFFAOYSA-N (2-iodoacetyl) 2-iodoacetate Chemical compound ICC(=O)OC(=O)CI RBNSZWOCWHGHMR-UHFFFAOYSA-N 0.000 description 1
- LBWHYNPDTSNGQD-NSHCULHESA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[2-[[(2s)-2-[[2-[[(2s)-6-amino-2-[[(2s,3r)-2-[[(2s)-2,6-diaminohexanoyl]amino]-3-hydroxybutanoyl]amino]hexanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino] Chemical compound C([C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)C1=CC=CC=C1 LBWHYNPDTSNGQD-NSHCULHESA-N 0.000 description 1
- MIAKOEWBCMPCQR-YBXAARCKSA-N (2s,3r,4s,5r,6r)-2-(4-aminophenoxy)-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound C1=CC(N)=CC=C1O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MIAKOEWBCMPCQR-YBXAARCKSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- DJQYYYCQOZMCRC-UHFFFAOYSA-N 2-aminopropane-1,3-dithiol Chemical group SCC(N)CS DJQYYYCQOZMCRC-UHFFFAOYSA-N 0.000 description 1
- KIUMMUBSPKGMOY-UHFFFAOYSA-L 5-[(3-carboxylato-4-nitrophenyl)disulfanyl]-2-nitrobenzoate Chemical compound C1=C([N+]([O-])=O)C(C(=O)[O-])=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C([O-])=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-L 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 102000053642 Catalytic RNA Human genes 0.000 description 1
- 108090000994 Catalytic RNA Proteins 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 241000709747 Enterobacteria phage R17 Species 0.000 description 1
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108010003533 Viral Envelope Proteins Proteins 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000011246 composite particle Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229910052736 halogen Inorganic materials 0.000 description 1
- -1 halogen-activated galactose Chemical class 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000008073 immune recognition Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 125000005439 maleimidyl group Chemical group C1(C=CC(N1*)=O)=O 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 108091092562 ribozyme Proteins 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000012868 site-directed mutagenesis technique Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 235000010265 sodium sulphite Nutrition 0.000 description 1
- HAEPBEMBOAIUPN-UHFFFAOYSA-L sodium tetrathionate Chemical compound O.O.[Na+].[Na+].[O-]S(=O)(=O)SSS([O-])(=O)=O HAEPBEMBOAIUPN-UHFFFAOYSA-L 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000010809 targeting technique Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
- A61K47/549—Sugars, nucleosides, nucleotides or nucleic acids
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Virology (AREA)
- Zoology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Hydrogenated Pyridines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB919114003A GB9114003D0 (en) | 1991-06-28 | 1991-06-28 | Chimaeric protein |
PCT/GB1992/001159 WO1993000434A1 (en) | 1991-06-28 | 1992-06-26 | Capsid forming and cystein modified chimaeric ms2-coat protein |
Publications (3)
Publication Number | Publication Date |
---|---|
NO934842D0 NO934842D0 (no) | 1993-12-27 |
NO934842L NO934842L (no) | 1994-02-28 |
NO315050B1 true NO315050B1 (no) | 2003-06-30 |
Family
ID=10697502
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19934842A NO315050B1 (no) | 1991-06-28 | 1993-12-27 | Kapsiddannende og cysteinmodifisert kim¶rt MS2-kappeprotein |
Country Status (15)
Country | Link |
---|---|
US (1) | US5698424A (ja) |
EP (1) | EP0591369B1 (ja) |
JP (1) | JP3514755B2 (ja) |
KR (1) | KR100222163B1 (ja) |
AT (1) | ATE205880T1 (ja) |
AU (1) | AU657560B2 (ja) |
CA (1) | CA2111683A1 (ja) |
DE (1) | DE69232069T2 (ja) |
FI (1) | FI110613B (ja) |
GB (2) | GB9114003D0 (ja) |
IE (1) | IE922085A1 (ja) |
NO (1) | NO315050B1 (ja) |
NZ (1) | NZ243330A (ja) |
WO (1) | WO1993000434A1 (ja) |
ZA (1) | ZA924774B (ja) |
Families Citing this family (35)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB9213601D0 (en) * | 1992-06-26 | 1992-08-12 | Mastico Robert A | Protein based delivery system |
DE19618797C2 (de) * | 1996-05-10 | 2000-03-23 | Bertling Wolf | Vehikel zum Transport molekularer Substanz |
AU770802B2 (en) * | 1998-10-21 | 2004-03-04 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Virus-like particles for the induction of autoantibodies |
CN100534529C (zh) * | 1998-11-30 | 2009-09-02 | 希托斯生物技术股份公司 | 抗原的有序分子呈递,制备及使用的方法 |
DE19916224C1 (de) | 1999-04-10 | 2000-06-21 | November Ag Molekulare Medizin | Synthetisches biologisch aktives Molekül |
WO2001005950A2 (en) * | 1999-07-20 | 2001-01-25 | Morphosys Ag | Methods for displaying (poly)peptides/proteins on bacteriophage particles via disulfide bonds |
AU2001252458A1 (en) | 2000-05-05 | 2001-11-20 | Martin Bachmann | Molecular antigen arrays and vaccines |
US7128911B2 (en) * | 2001-01-19 | 2006-10-31 | Cytos Biotechnology Ag | Antigen arrays for treatment of bone disease |
US7094409B2 (en) * | 2001-01-19 | 2006-08-22 | Cytos Biotechnology Ag | Antigen arrays for treatment of allergic eosinophilic diseases |
US7320793B2 (en) * | 2001-01-19 | 2008-01-22 | Cytos Biotechnology Ag | Molecular antigen array |
AU2007202761B2 (en) * | 2001-01-19 | 2010-01-21 | Kuros Biosciences Ag | Molecular antigen array |
DE60234375D1 (de) * | 2001-09-14 | 2009-12-24 | Cytos Biotechnology Ag | VERPACKUNG VON IMMUNSTIMULIERENDEM CpG IN VIRUSÄHNLICHEN PARTIKELN: HERSTELLUNGSVERFAHREN UND VERWENDUNG |
CA2492823A1 (en) * | 2001-09-14 | 2003-03-27 | Martin F. Bachmann | In vivo activation of antigen presenting cells for enhancement of immune responses induced by virus like particles |
BR0213117A (pt) | 2001-10-05 | 2004-09-21 | Cytos Biotechnology Ag | Conjugados peptìdeo angiotensina-veìculo e seus usos |
US7115266B2 (en) * | 2001-10-05 | 2006-10-03 | Cytos Biotechnology Ag | Angiotensin peptide-carrier conjugates and uses thereof |
RU2322258C2 (ru) * | 2001-11-07 | 2008-04-20 | Цитос Байотекнолоджи Аг | Антигенные матрицы для лечения заболевания костей |
US20030219459A1 (en) * | 2002-01-18 | 2003-11-27 | Cytos Biotechnology Ag | Prion protein carrier-conjugates |
EP1513552B1 (en) * | 2002-06-20 | 2010-12-01 | Cytos Biotechnology AG | Packaged virus-like particles in combination with cpg for use as adjuvants with allergens : method of preparation and use |
MXPA05000277A (es) * | 2002-07-17 | 2005-03-31 | Cytos Biotechnology Ag | Configuraciones de antigenos moleculares de usan una particula tipo virus derivada de la proteina de recurimiento ap205. |
KR101228376B1 (ko) | 2002-07-18 | 2013-01-31 | 사이토스 바이오테크놀로지 아게 | 합텐-캐리어 컨쥬게이트 및 그의 용도 |
WO2004016282A1 (en) * | 2002-07-19 | 2004-02-26 | Cytos Biotechnology Ag | Vaccine compositions containing amyloid beta1-6 antigen arrays |
EP1605972A2 (en) * | 2003-03-26 | 2005-12-21 | Cytos Biotechnology AG | Hiv-peptide-carrier-conjugates |
US20060210588A1 (en) * | 2003-03-26 | 2006-09-21 | Cytos Biotechnology Ag | Hiv-peptide-carrier-conjugates |
US7537767B2 (en) * | 2003-03-26 | 2009-05-26 | Cytis Biotechnology Ag | Melan-A- carrier conjugates |
US20050191317A1 (en) * | 2004-01-20 | 2005-09-01 | Cytos Biotechnology Ag | Ghrelin-carrier conjugates |
EP1750761A1 (en) * | 2004-06-02 | 2007-02-14 | Cytos Biotechnology AG | Medical uses of carrier conjugates of non-human tnf-peptides |
CA2588274A1 (en) * | 2004-10-05 | 2006-04-13 | Cytos Biotechnology Ag | Vlp-antigen conjugates and their uses as vaccines |
US7572451B2 (en) * | 2004-10-25 | 2009-08-11 | Cytos Biotechnology Ag | Gastric inhibitory polypeptide (GIP) antigen arrays and uses thereof |
GB0424563D0 (en) * | 2004-11-05 | 2004-12-08 | Novartis Ag | Organic compounds |
WO2006095345A2 (en) * | 2005-03-08 | 2006-09-14 | Ramot At Tel-Aviv University Ltd. | Targeted drug-carrying bacteriophages |
US7767212B2 (en) * | 2005-03-18 | 2010-08-03 | Cytos Biotechnology Ag | CAT allergen conjugates and uses thereof |
KR20080047564A (ko) | 2005-09-28 | 2008-05-29 | 사이토스 바이오테크놀로지 아게 | 인터루킨-1 컨쥬게이트 및 그의 용도 |
CA2636139A1 (en) | 2005-12-14 | 2007-06-21 | Cytos Biotechnology Ag | Immunostimulatory nucleic acid packaged particles for the treatment of hypersensitivity |
ES2427994T3 (es) | 2006-06-12 | 2013-11-05 | Cytos Biotechnology Ag | Procesos para empaquetar oligonucleótidos en partículas de tipo viral de bacteriófagos de ARN |
EP2190987B1 (en) * | 2007-08-21 | 2012-11-14 | MorphoSys AG | Methods for the formation of disulphide bonds |
Family Cites Families (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB9101550D0 (en) * | 1991-01-24 | 1991-03-06 | Mastico Robert A | Antigen-presenting chimaeric protein |
-
1991
- 1991-06-28 GB GB919114003A patent/GB9114003D0/en active Pending
-
1992
- 1992-06-26 ZA ZA924774A patent/ZA924774B/xx unknown
- 1992-06-26 CA CA002111683A patent/CA2111683A1/en not_active Abandoned
- 1992-06-26 KR KR1019930703986A patent/KR100222163B1/ko not_active IP Right Cessation
- 1992-06-26 GB GB9213644A patent/GB2257431B/en not_active Revoked
- 1992-06-26 NZ NZ243330A patent/NZ243330A/en unknown
- 1992-06-26 EP EP92913894A patent/EP0591369B1/en not_active Expired - Lifetime
- 1992-06-26 AT AT92913894T patent/ATE205880T1/de not_active IP Right Cessation
- 1992-06-26 JP JP50123093A patent/JP3514755B2/ja not_active Expired - Fee Related
- 1992-06-26 US US08/167,982 patent/US5698424A/en not_active Expired - Fee Related
- 1992-06-26 AU AU21955/92A patent/AU657560B2/en not_active Ceased
- 1992-06-26 DE DE69232069T patent/DE69232069T2/de not_active Expired - Fee Related
- 1992-06-26 WO PCT/GB1992/001159 patent/WO1993000434A1/en active IP Right Grant
- 1992-07-01 IE IE208592A patent/IE922085A1/en not_active Application Discontinuation
-
1993
- 1993-12-27 FI FI935877A patent/FI110613B/fi active
- 1993-12-27 NO NO19934842A patent/NO315050B1/no not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
NO934842D0 (no) | 1993-12-27 |
GB9213644D0 (en) | 1992-08-12 |
ZA924774B (en) | 1993-04-22 |
FI110613B (fi) | 2003-02-28 |
JPH06509223A (ja) | 1994-10-20 |
EP0591369B1 (en) | 2001-09-19 |
EP0591369A1 (en) | 1994-04-13 |
ATE205880T1 (de) | 2001-10-15 |
AU657560B2 (en) | 1995-03-16 |
IE922085A1 (en) | 1992-12-30 |
WO1993000434A1 (en) | 1993-01-07 |
CA2111683A1 (en) | 1993-01-07 |
FI935877A0 (fi) | 1993-12-27 |
GB2257431B (en) | 1995-04-19 |
AU2195592A (en) | 1993-01-25 |
KR940701447A (ko) | 1994-05-28 |
KR100222163B1 (ko) | 1999-10-01 |
DE69232069T2 (de) | 2002-01-31 |
GB9114003D0 (en) | 1991-08-14 |
GB2257431A (en) | 1993-01-13 |
NZ243330A (en) | 1994-06-27 |
US5698424A (en) | 1997-12-16 |
NO934842L (no) | 1994-02-28 |
DE69232069D1 (de) | 2001-10-25 |
JP3514755B2 (ja) | 2004-03-31 |
FI935877A (fi) | 1993-12-27 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO315050B1 (no) | Kapsiddannende og cysteinmodifisert kim¶rt MS2-kappeprotein | |
JP3634358B2 (ja) | タンパク質に基づく輸送系 | |
JP2974028B2 (ja) | アドヒシン抗原類 | |
KR100197819B1 (ko) | 융합 ms2 코트 단백질을 포함하는 항원제공 캡시드 | |
JP2768928B2 (ja) | ウシ乳頭腫ウィルスのdna断片 | |
EA006207B1 (ru) | ИММУНОГЕННЫЕ ХИМЕРНЫЕ ЧАСТИЦЫ НВс, ОБЛАДАЮЩИЕ ПОВЫШЕННОЙ СТАБИЛЬНОСТЬЮ | |
JPH06507551A (ja) | 組換えdna由来コレラトキシンサブユニット類似体 | |
KR910002693B1 (ko) | 면역 강화 | |
DE69327553T2 (de) | E.Coli P-Fimbriae als immunogener Träger gegen GnRH | |
CN113121704B (zh) | 基于纳米颗粒的冠状病毒疫苗 | |
WO1995032731A2 (en) | Immunogenic pharmaceuticals | |
WO1991006653A1 (en) | Recombinant vaccine for porcine pleuropneumonia | |
EP1042467B1 (en) | Non-identical genes and their application in improved molecular adjuvants | |
JPS61111695A (ja) | B型肝炎ビールス又はb型肝炎ビールス成分からのdnaフラグメント、ポリペプチド及びオリゴペプチド、組み換えdna分子、dnaベクター、エシエリヒア・コリk12変異体、ポリペプチドの製法、b型肝炎ビールス疾患に対する接種物質、モノクロナール抗体ma18/7、マウス雑種細胞go1a18/7‐1並びにモノクロナール抗体ma18/7の製法 | |
JP3135060B2 (ja) | ヘモフィルスインフルエンザb型菌の外皮膜タンパク質P2の部分断片を用いた接合体 | |
EP0247904A1 (en) | Method of preparation and use for feline leukemia virus antigens | |
CA2271699A1 (en) | Chimeric ltb vaccines | |
KR0178110B1 (ko) | 대장균에서 발현된 인간유래 한탄바이러스의 뉴클레오캡시드 단백질을 이용한 백신 | |
US5916562A (en) | Membrane proteins and peptides of haemophilus influenzae type B | |
EP0551689A2 (en) | Cyclic HIV principal neutralizing determinant (PNP) peptides | |
HU205372B (en) | Process for producing vaccines against cholera | |
Val et al. | 56 THOMAS HOHN AND BARBARA HOHN | |
JPH03501684A (ja) | Hiv抗原の製法およびその系 | |
MXPA00002973A (en) | Fusion proteins comprising hiv-1 tat and/or nef proteins | |
NO176996B (no) | Fremgangsmåte for fremstilling av en farmasöytisk sammensetning for beskyttelse av felin leukemivirus (FeLV) |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MM1K | Lapsed by not paying the annual fees |