DE69832706T2 - Immunschützendes influenzaantigen und dessen verwendung zur impfung - Google Patents
Immunschützendes influenzaantigen und dessen verwendung zur impfung Download PDFInfo
- Publication number
- DE69832706T2 DE69832706T2 DE69832706T DE69832706T DE69832706T2 DE 69832706 T2 DE69832706 T2 DE 69832706T2 DE 69832706 T DE69832706 T DE 69832706T DE 69832706 T DE69832706 T DE 69832706T DE 69832706 T2 DE69832706 T2 DE 69832706T2
- Authority
- DE
- Germany
- Prior art keywords
- influenza
- antigen
- protein
- vaccine
- expression
- 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 - Lifetime
Links
- 238000002255 vaccination Methods 0.000 title description 7
- 239000000427 antigen Substances 0.000 claims abstract description 86
- 108091007433 antigens Proteins 0.000 claims abstract description 86
- 102000036639 antigens Human genes 0.000 claims abstract description 86
- 239000012634 fragment Substances 0.000 claims abstract description 85
- 206010022000 influenza Diseases 0.000 claims abstract description 65
- 238000000034 method Methods 0.000 claims abstract description 46
- 229960005486 vaccine Drugs 0.000 claims abstract description 43
- 230000004927 fusion Effects 0.000 claims abstract description 32
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 22
- 108010052285 Membrane Proteins Proteins 0.000 claims abstract description 15
- 102000018697 Membrane Proteins Human genes 0.000 claims abstract description 13
- 229920001059 synthetic polymer Polymers 0.000 claims abstract description 3
- 230000014509 gene expression Effects 0.000 claims description 103
- 108090000623 proteins and genes Proteins 0.000 claims description 95
- 210000004027 cell Anatomy 0.000 claims description 60
- 102000004169 proteins and genes Human genes 0.000 claims description 35
- 208000002672 hepatitis B Diseases 0.000 claims description 32
- 238000002360 preparation method Methods 0.000 claims description 27
- 238000004519 manufacturing process Methods 0.000 claims description 25
- 108020004414 DNA Proteins 0.000 claims description 24
- 239000001963 growth medium Substances 0.000 claims description 17
- 101710132601 Capsid protein Proteins 0.000 claims description 16
- 239000002671 adjuvant Substances 0.000 claims description 16
- 208000037797 influenza A Diseases 0.000 claims description 16
- 239000012528 membrane Substances 0.000 claims description 16
- 241000712431 Influenza A virus Species 0.000 claims description 14
- 108091026890 Coding region Proteins 0.000 claims description 12
- 101710154606 Hemagglutinin Proteins 0.000 claims description 6
- 241001465754 Metazoa Species 0.000 claims description 6
- 108010006232 Neuraminidase Proteins 0.000 claims description 6
- 102000005348 Neuraminidase Human genes 0.000 claims description 6
- 101710093908 Outer capsid protein VP4 Proteins 0.000 claims description 6
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 claims description 6
- 101710176177 Protein A56 Proteins 0.000 claims description 6
- 239000000185 hemagglutinin Substances 0.000 claims description 6
- 108010041986 DNA Vaccines Proteins 0.000 claims description 5
- 229940021995 DNA vaccine Drugs 0.000 claims description 5
- 230000001105 regulatory effect Effects 0.000 claims description 5
- 230000002163 immunogen Effects 0.000 claims description 4
- 230000002103 transcriptional effect Effects 0.000 claims description 4
- 241000194036 Lactococcus Species 0.000 claims description 3
- 206010046865 Vaccinia virus infection Diseases 0.000 claims description 3
- 230000005847 immunogenicity Effects 0.000 claims description 3
- 230000008569 process Effects 0.000 claims description 3
- 208000007089 vaccinia Diseases 0.000 claims description 3
- 102000011931 Nucleoproteins Human genes 0.000 claims description 2
- 108010061100 Nucleoproteins Proteins 0.000 claims description 2
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 claims description 2
- 210000002443 helper t lymphocyte Anatomy 0.000 claims description 2
- 230000001939 inductive effect Effects 0.000 claims description 2
- 239000000816 peptidomimetic Substances 0.000 claims description 2
- 230000024932 T cell mediated immunity Effects 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 210000000170 cell membrane Anatomy 0.000 claims 1
- 230000002787 reinforcement Effects 0.000 claims 1
- 108010044241 tetanus toxin fragment C Proteins 0.000 claims 1
- 239000000546 pharmaceutical excipient Substances 0.000 abstract description 3
- 101001039853 Sonchus yellow net virus Matrix protein Proteins 0.000 description 94
- 239000013612 plasmid Substances 0.000 description 77
- 244000057717 Streptococcus lactis Species 0.000 description 59
- 241000699670 Mus sp. Species 0.000 description 51
- 108020001507 fusion proteins Proteins 0.000 description 41
- 102000037865 fusion proteins Human genes 0.000 description 40
- 239000000463 material Substances 0.000 description 33
- 235000018102 proteins Nutrition 0.000 description 32
- 239000013598 vector Substances 0.000 description 30
- 230000003053 immunization Effects 0.000 description 29
- 238000002649 immunization Methods 0.000 description 28
- 241000894006 Bacteria Species 0.000 description 27
- 108020004705 Codon Proteins 0.000 description 27
- 241000588724 Escherichia coli Species 0.000 description 27
- 241000700605 Viruses Species 0.000 description 27
- 210000002966 serum Anatomy 0.000 description 27
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 22
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 22
- 241000701447 unidentified baculovirus Species 0.000 description 22
- 150000001413 amino acids Chemical class 0.000 description 20
- 238000004458 analytical method Methods 0.000 description 19
- 238000001262 western blot Methods 0.000 description 18
- 235000001014 amino acid Nutrition 0.000 description 17
- 229940024606 amino acid Drugs 0.000 description 17
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 17
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 17
- 238000002965 ELISA Methods 0.000 description 16
- 238000006243 chemical reaction Methods 0.000 description 16
- 108091034117 Oligonucleotide Proteins 0.000 description 15
- 108010076504 Protein Sorting Signals Proteins 0.000 description 15
- 239000000499 gel Substances 0.000 description 15
- 241000699666 Mus <mouse, genus> Species 0.000 description 14
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 14
- 230000028327 secretion Effects 0.000 description 14
- 238000002474 experimental method Methods 0.000 description 13
- 230000004224 protection Effects 0.000 description 13
- 108090001005 Interleukin-6 Proteins 0.000 description 12
- 239000000872 buffer Substances 0.000 description 12
- 210000004379 membrane Anatomy 0.000 description 12
- 239000000203 mixture Substances 0.000 description 12
- 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 11
- 101710141347 Major envelope glycoprotein Proteins 0.000 description 11
- 102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 description 11
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 10
- 241000238631 Hexapoda Species 0.000 description 10
- 241000282412 Homo Species 0.000 description 10
- 102000004889 Interleukin-6 Human genes 0.000 description 10
- 238000012408 PCR amplification Methods 0.000 description 10
- 230000003321 amplification Effects 0.000 description 10
- 238000010790 dilution Methods 0.000 description 10
- 239000012895 dilution Substances 0.000 description 10
- 238000003199 nucleic acid amplification method Methods 0.000 description 10
- 235000019687 Lamb Nutrition 0.000 description 9
- 101150115929 Usp45 gene Proteins 0.000 description 9
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 9
- 239000002245 particle Substances 0.000 description 9
- 238000011238 DNA vaccination Methods 0.000 description 8
- 108090000204 Dipeptidase 1 Proteins 0.000 description 8
- 101000937544 Homo sapiens Beta-2-microglobulin Proteins 0.000 description 8
- 108010002350 Interleukin-2 Proteins 0.000 description 8
- 102000000588 Interleukin-2 Human genes 0.000 description 8
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 8
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 8
- 230000000692 anti-sense effect Effects 0.000 description 8
- 102000006635 beta-lactamase Human genes 0.000 description 8
- 102000047279 human B2M Human genes 0.000 description 8
- 208000015181 infectious disease Diseases 0.000 description 8
- 239000007924 injection Substances 0.000 description 8
- 238000002347 injection Methods 0.000 description 8
- 229940100601 interleukin-6 Drugs 0.000 description 8
- 239000002773 nucleotide Substances 0.000 description 8
- 125000003729 nucleotide group Chemical group 0.000 description 8
- 239000006228 supernatant Substances 0.000 description 8
- 102100034343 Integrase Human genes 0.000 description 7
- 101710182846 Polyhedrin Proteins 0.000 description 7
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 7
- 108020005091 Replication Origin Proteins 0.000 description 7
- 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 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 210000004369 blood Anatomy 0.000 description 7
- 239000008280 blood Substances 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 239000011780 sodium chloride Substances 0.000 description 7
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
- 102000000989 Complement System Proteins Human genes 0.000 description 6
- 108010069112 Complement System Proteins Proteins 0.000 description 6
- 102000053602 DNA Human genes 0.000 description 6
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 241000282326 Felis catus Species 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 101100445533 Staphylococcus epidermidis ermM gene Proteins 0.000 description 6
- 235000014897 Streptococcus lactis Nutrition 0.000 description 6
- 238000013459 approach Methods 0.000 description 6
- HPNMFZURTQLUMO-UHFFFAOYSA-N diethylamine Chemical compound CCNCC HPNMFZURTQLUMO-UHFFFAOYSA-N 0.000 description 6
- 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 6
- 239000002609 medium Substances 0.000 description 6
- 210000001322 periplasm Anatomy 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 230000004083 survival effect Effects 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- QRXMUCSWCMTJGU-UHFFFAOYSA-L (5-bromo-4-chloro-1h-indol-3-yl) phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP([O-])(=O)[O-])=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-L 0.000 description 5
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 5
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 5
- 108010078791 Carrier Proteins Proteins 0.000 description 5
- 102000014914 Carrier Proteins Human genes 0.000 description 5
- 241000282414 Homo sapiens Species 0.000 description 5
- 108010063738 Interleukins Proteins 0.000 description 5
- 230000005875 antibody response Effects 0.000 description 5
- -1 bla = β-Laktamase Proteins 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 230000001086 cytosolic effect Effects 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 229960003276 erythromycin Drugs 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- JPXMTWWFLBLUCD-UHFFFAOYSA-N nitro blue tetrazolium(2+) Chemical compound COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 JPXMTWWFLBLUCD-UHFFFAOYSA-N 0.000 description 5
- 239000008188 pellet Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 230000035755 proliferation Effects 0.000 description 5
- 238000012546 transfer Methods 0.000 description 5
- 230000003612 virological effect Effects 0.000 description 5
- 102000015696 Interleukins Human genes 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- 241001529936 Murinae Species 0.000 description 4
- 101001043827 Mus musculus Interleukin-2 Proteins 0.000 description 4
- 239000000020 Nitrocellulose Substances 0.000 description 4
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 4
- 108010073443 Ribi adjuvant Proteins 0.000 description 4
- 108010055044 Tetanus Toxin Proteins 0.000 description 4
- 229920004890 Triton X-100 Polymers 0.000 description 4
- 239000013504 Triton X-100 Substances 0.000 description 4
- 238000002835 absorbance Methods 0.000 description 4
- 230000006978 adaptation Effects 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 239000005018 casein Substances 0.000 description 4
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 4
- 235000021240 caseins Nutrition 0.000 description 4
- 210000002421 cell wall Anatomy 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 210000004408 hybridoma Anatomy 0.000 description 4
- 229940047122 interleukins Drugs 0.000 description 4
- 231100000518 lethal Toxicity 0.000 description 4
- 231100000636 lethal dose Toxicity 0.000 description 4
- 230000001665 lethal effect Effects 0.000 description 4
- 229920001220 nitrocellulos Polymers 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 238000002741 site-directed mutagenesis Methods 0.000 description 4
- 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 4
- 238000012360 testing method Methods 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 241000712461 unidentified influenza virus Species 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 3
- 108700010070 Codon Usage Proteins 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 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
- 241000984622 Leucodon Species 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 101150061732 M2L gene Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102000016943 Muramidase Human genes 0.000 description 3
- 108010014251 Muramidase Proteins 0.000 description 3
- 101001076414 Mus musculus Interleukin-6 Proteins 0.000 description 3
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 101000582398 Staphylococcus aureus Replication initiation protein Proteins 0.000 description 3
- 241000282887 Suidae Species 0.000 description 3
- 108020002494 acetyltransferase Proteins 0.000 description 3
- 102000005421 acetyltransferase Human genes 0.000 description 3
- 238000000137 annealing Methods 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 238000004166 bioassay Methods 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000012228 culture supernatant Substances 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 101150036274 kil gene Proteins 0.000 description 3
- 210000004072 lung Anatomy 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 239000004325 lysozyme Substances 0.000 description 3
- 229960000274 lysozyme Drugs 0.000 description 3
- 235000010335 lysozyme Nutrition 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 229940118376 tetanus toxin Drugs 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 2
- 206010002091 Anaesthesia Diseases 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 206010011224 Cough Diseases 0.000 description 2
- 241000701022 Cytomegalovirus Species 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 101001033280 Homo sapiens Cytokine receptor common subunit beta Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 241001483952 Peach chlorotic mottle virus Species 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- 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 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 241000221988 Russula cyanoxantha Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 239000012506 Sephacryl® Substances 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 2
- 239000007984 Tris EDTA buffer Substances 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000037005 anaesthesia Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 2
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 244000309466 calf Species 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000003433 contraceptive agent Substances 0.000 description 2
- 230000002254 contraceptive effect Effects 0.000 description 2
- 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 2
- 239000007771 core particle Substances 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- IPCSVZSSVZVIGE-UHFFFAOYSA-N hexadecanoic acid Chemical compound CCCCCCCCCCCCCCCC(O)=O IPCSVZSSVZVIGE-UHFFFAOYSA-N 0.000 description 2
- 102000055647 human CSF2RB Human genes 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 230000002480 immunoprotective effect Effects 0.000 description 2
- 208000037799 influenza C Diseases 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- PHTQWCKDNZKARW-UHFFFAOYSA-N isoamylol Chemical compound CC(C)CCO PHTQWCKDNZKARW-UHFFFAOYSA-N 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 108010009719 mutanolysin Proteins 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 230000003204 osmotic effect Effects 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 230000009993 protective function Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 238000003757 reverse transcription PCR Methods 0.000 description 2
- 101150098466 rpsL gene Proteins 0.000 description 2
- 230000035939 shock Effects 0.000 description 2
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000011282 treatment Methods 0.000 description 2
- YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 1
- 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 1
- BHNQPLPANNDEGL-UHFFFAOYSA-N 2-(4-octylphenoxy)ethanol Chemical compound CCCCCCCCC1=CC=C(OCCO)C=C1 BHNQPLPANNDEGL-UHFFFAOYSA-N 0.000 description 1
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- LVSPDZAGCBEQAV-UHFFFAOYSA-N 4-chloronaphthalen-1-ol Chemical compound C1=CC=C2C(O)=CC=C(Cl)C2=C1 LVSPDZAGCBEQAV-UHFFFAOYSA-N 0.000 description 1
- 101100295756 Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) omp38 gene Proteins 0.000 description 1
- DLQPMEMYCIGJIM-UHFFFAOYSA-N Adjuvant peptide Natural products CC(NC(=O)CCOC1C(O)C(CO)OC(O)C1NC(=O)C)C(=O)NC(CCC(=O)O)C(=O)N DLQPMEMYCIGJIM-UHFFFAOYSA-N 0.000 description 1
- 240000006108 Allium ampeloprasum Species 0.000 description 1
- 235000005254 Allium ampeloprasum Nutrition 0.000 description 1
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 1
- 229920000298 Cellophane Polymers 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 108010076804 DNA Restriction Enzymes Proteins 0.000 description 1
- 101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 102100020743 Dipeptidase 1 Human genes 0.000 description 1
- 241000701832 Enterobacteria phage T3 Species 0.000 description 1
- 238000000729 Fisher's exact test Methods 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 102100036263 Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Human genes 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108060003393 Granulin Proteins 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 101001001786 Homo sapiens Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Proteins 0.000 description 1
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 241001500351 Influenzavirus A Species 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 108090000862 Ion Channels Proteins 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- 240000006024 Lactobacillus plantarum Species 0.000 description 1
- 235000013965 Lactobacillus plantarum Nutrition 0.000 description 1
- 239000012741 Laemmli sample buffer Substances 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 101710085938 Matrix protein Proteins 0.000 description 1
- 101100364971 Mus musculus Scai gene Proteins 0.000 description 1
- 208000000112 Myalgia Diseases 0.000 description 1
- XUYPXLNMDZIRQH-LURJTMIESA-N N-acetyl-L-methionine Chemical compound CSCC[C@@H](C(O)=O)NC(C)=O XUYPXLNMDZIRQH-LURJTMIESA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 235000021314 Palmitic acid Nutrition 0.000 description 1
- 108010090127 Periplasmic Proteins Proteins 0.000 description 1
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 101710132653 Protein M2 Proteins 0.000 description 1
- 108010019653 Pwo polymerase Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 1
- 241001282153 Scopelogadus mizolepis Species 0.000 description 1
- VMLONWHIORGALA-SRVKXCTJSA-N Ser-Leu-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]([NH3+])CO VMLONWHIORGALA-SRVKXCTJSA-N 0.000 description 1
- 108091081024 Start codon 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
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 101710137500 T7 RNA polymerase Proteins 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 108091034135 Vault RNA Proteins 0.000 description 1
- 108010015780 Viral Core Proteins Proteins 0.000 description 1
- 108020000999 Viral RNA Proteins 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 230000003302 anti-idiotype Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 239000000074 antisense oligonucleotide Substances 0.000 description 1
- 238000012230 antisense oligonucleotides Methods 0.000 description 1
- 101150042295 arfA gene Proteins 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000010241 blood sampling Methods 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 238000012754 cardiac puncture Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000012501 chromatography medium Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 210000005220 cytoplasmic tail Anatomy 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000008260 defense mechanism Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000000635 electron micrograph Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 101150045500 galK gene Proteins 0.000 description 1
- 101150041954 galU gene Proteins 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 101150096208 gtaB gene Proteins 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 208000021760 high fever Diseases 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 101150085823 hsdR gene Proteins 0.000 description 1
- 102000055277 human IL2 Human genes 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 208000037798 influenza B Diseases 0.000 description 1
- 229960003971 influenza vaccine Drugs 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000009413 insulation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- 229940072205 lactobacillus plantarum Drugs 0.000 description 1
- 231100000225 lethality Toxicity 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 101150079876 mcrB gene Proteins 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- BSOQXXWZTUDTEL-QAQREVAFSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-QAQREVAFSA-N 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 238000010606 normalization Methods 0.000 description 1
- 101150087557 omcB gene Proteins 0.000 description 1
- 101150115693 ompA gene Proteins 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000003161 ribonuclease inhibitor Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 206010041232 sneezing Diseases 0.000 description 1
- 229940054269 sodium pyruvate Drugs 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 229940031439 squalene Drugs 0.000 description 1
- TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000012096 transfection reagent Substances 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/16—Antivirals for RNA viruses for influenza or rhinoviruses
-
- 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
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/472—Complement proteins, e.g. anaphylatoxin, C3a, C5a
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- 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
- C12N2730/00—Reverse transcribing DNA viruses
- C12N2730/00011—Details
- C12N2730/10011—Hepadnaviridae
- C12N2730/10111—Orthohepadnavirus, e.g. hepatitis B virus
- C12N2730/10122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N2760/16111—Influenzavirus A, i.e. influenza A virus
- C12N2760/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Virology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Pulmonology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP97202434 | 1997-08-05 | ||
| EP97202434 | 1997-08-05 | ||
| PCT/EP1998/005106 WO1999007839A2 (en) | 1997-08-05 | 1998-08-05 | Immunoprotective influenza antigen and its use in vaccination |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE69832706D1 DE69832706D1 (de) | 2006-01-12 |
| DE69832706T2 true DE69832706T2 (de) | 2006-08-10 |
Family
ID=8228624
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE69832706T Expired - Lifetime DE69832706T2 (de) | 1997-08-05 | 1998-08-05 | Immunschützendes influenzaantigen und dessen verwendung zur impfung |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US7732130B2 (enExample) |
| EP (1) | EP0996717B1 (enExample) |
| JP (2) | JP5132851B2 (enExample) |
| AT (1) | ATE312172T1 (enExample) |
| AU (1) | AU745951B2 (enExample) |
| CA (1) | CA2297786C (enExample) |
| DE (1) | DE69832706T2 (enExample) |
| DK (1) | DK0996717T3 (enExample) |
| ES (1) | ES2255181T3 (enExample) |
| WO (1) | WO1999007839A2 (enExample) |
Families Citing this family (62)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7731972B1 (en) | 2000-02-04 | 2010-06-08 | Vlaams Interuniversitair Instituut Voor Biotechnologie | Immunoprotective influenza antigen and its use in vaccination |
| ES2255181T3 (es) | 1997-08-05 | 2006-06-16 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw. | Antigeno inmunoprotector contra la gripe y su uso en vacunacion. |
| WO2000032227A2 (en) | 1998-11-30 | 2000-06-08 | Cytos Biotechnology Ag | Ordered molecular presentation of antigens, method of preparation and use |
| GB0008582D0 (en) * | 2000-04-08 | 2000-05-31 | Adprotech Plc | DNA immunization vectors |
| AU5533601A (en) * | 2000-04-14 | 2001-10-30 | Wisconsin Alumni Res Found | Viruses comprising mutation ion channel protein |
| EP1282640A2 (en) * | 2000-05-01 | 2003-02-12 | Powderject Vaccines, Inc. | Nucleic acid immunization |
| CA2407897A1 (en) | 2000-05-05 | 2001-11-15 | Cytos Biotechnology Ag | Molecular antigen arrays and vaccines |
| GB0025229D0 (en) * | 2000-10-14 | 2000-11-29 | Adprotech Ltd | Veterinary immunisation vectors |
| US7320793B2 (en) | 2001-01-19 | 2008-01-22 | Cytos Biotechnology Ag | Molecular antigen array |
| US7094409B2 (en) | 2001-01-19 | 2006-08-22 | Cytos Biotechnology Ag | Antigen arrays for treatment of allergic eosinophilic diseases |
| US7128911B2 (en) | 2001-01-19 | 2006-10-31 | Cytos Biotechnology Ag | Antigen arrays for treatment of bone disease |
| US7361352B2 (en) | 2001-08-15 | 2008-04-22 | Acambis, Inc. | Influenza immunogen and vaccine |
| ES2335979T3 (es) | 2001-09-14 | 2010-04-07 | Cytos Biotechnology Ag | Empaquetamiento de cpg inmunoestimuladores en particulas similares a virus: metodo de preparacion y su uso. |
| US7115266B2 (en) | 2001-10-05 | 2006-10-03 | Cytos Biotechnology Ag | Angiotensin peptide-carrier conjugates and uses thereof |
| US7351413B2 (en) | 2002-02-21 | 2008-04-01 | Lorantis, Limited | Stabilized HBc chimer particles as immunogens for chronic hepatitis |
| GB0204154D0 (en) * | 2002-02-22 | 2002-04-10 | Adprotech Ltd | Cat immunisation vectors |
| TW200407161A (en) * | 2002-03-13 | 2004-05-16 | Gemini Science Inc | Human monoclonal antibodies to influenza M2 protein and method of making and using same |
| CN102061288A (zh) | 2002-07-17 | 2011-05-18 | 希托斯生物技术股份公司 | 使用衍生自ap205外壳蛋白的病毒样颗粒的分子抗原阵列 |
| IN2008CN05409A (enExample) | 2002-07-18 | 2015-10-02 | Cytos Biotechnology Ag | |
| CA2492930C (en) | 2002-07-19 | 2013-01-08 | Cytos Biotechnology Ag | Vaccine compositions containing amyloid beta1-6 antigen arrays |
| CA2522081C (en) * | 2003-04-23 | 2013-01-29 | Wisconsin Alumni Research Foundation | Recombinant influenza viruses holding a mutation in a transmembrane protein gene |
| ATE414535T1 (de) * | 2003-06-23 | 2008-12-15 | Baxter Int | Trägerproteine für impfstoffe |
| KR20070086344A (ko) | 2004-11-19 | 2007-08-27 | 위스콘신 얼럼나이 리서어치 화운데이션 | 탠덤 전사 유닛을 갖는 재조합 인플루엔자 벡터 |
| AU2005313026B2 (en) | 2004-12-06 | 2011-09-08 | Kyowa Hakko Kirin Co., Ltd. | Human monoclonal antibodies to influenza M2 protein and methods of making and using same |
| US20090162400A1 (en) * | 2004-12-21 | 2009-06-25 | Powell Thomas J | Compositions of influenza viral proteins and methods of use thereof |
| WO2007056266A2 (en) * | 2005-11-07 | 2007-05-18 | Sidney Kimmel Cancer Center | Cd40 ligand fusion protein vaccine |
| CA2632483C (en) | 2005-12-06 | 2014-11-25 | Yeda Research And Development Co. Ltd. At The Weizmann Institute Of Science | Improved influenza vaccine |
| EP1991264B1 (en) | 2006-03-07 | 2015-01-07 | Vaxinnate Corporation | Compositions that include hemagglutinin, methods of making and methods of use thereof |
| EP2010557B1 (en) | 2006-03-31 | 2014-02-26 | Wisconsin Alumni Research Foundation | High titer recombinant influenza viruses for vaccines |
| EP2043681B1 (en) | 2006-07-14 | 2015-10-07 | Sanofi Pasteur Biologics, LLC | Construction of recombinant virus vaccines by direct transposon-mediated insertion of foreign immunologic determinants into vector virus proteins |
| WO2008100290A2 (en) | 2006-09-29 | 2008-08-21 | Sanofi Pasteur Biologics Co | Recombinant rhinovirus vectors |
| WO2008058396A1 (en) * | 2006-11-15 | 2008-05-22 | Folia Biotech Inc. | Papaya mosaic virus-based vaccines for influenza |
| US9474798B2 (en) | 2007-06-18 | 2016-10-25 | Wisconsin Alumni Research Foundation | Influenza M2 protein mutant viruses as live influenza attenuated vaccines |
| MX2010001284A (es) | 2007-08-02 | 2010-08-31 | Biondvax Pharmaceuticals Ltd | Vacunas contra la influenza con multiepitope multimerico. |
| WO2009073330A2 (en) * | 2007-11-12 | 2009-06-11 | The Trustees Of The University Of Pennsylvania | Novel vaccines against multiple subtypes of influenza virus |
| SG190562A1 (en) * | 2008-04-18 | 2013-06-28 | Vaxinnate Corp | Deletion mutants of flagellin and methods of use |
| CA2742288A1 (en) * | 2008-07-30 | 2010-02-04 | Folia Biotech Inc. | Multivalent vaccines based on papaya mosaic virus and uses thereof |
| EP2168987A1 (en) * | 2008-09-22 | 2010-03-31 | Mucosis B.V. | Multifunctional linker protein containing an antibody against hemagglutinin, a conserved influenza antigen and an immunostimulating carrier binding domain |
| BR112012008060A2 (pt) | 2009-07-31 | 2016-11-22 | Paxvax Inc | vetores baseados em adenovírus |
| JP5730204B2 (ja) | 2009-08-28 | 2015-06-03 | 一般財団法人化学及血清療法研究所 | インフルエンザｍ２由来の改変ペプチドワクチン |
| US20110097358A1 (en) * | 2009-10-12 | 2011-04-28 | Techno Vax, Inc. | RESPIRATORY SYNCYTIAL VIRUS (RSV) VIRUS-LIKE PARTICLES (VLPs) |
| US9109013B2 (en) | 2009-10-26 | 2015-08-18 | Wisconsin Alumni Research Foundation | High titer recombinant influenza viruses with enhanced replication in vero cells |
| WO2011054995A2 (es) | 2009-11-06 | 2011-05-12 | Chimera Pharma, S. L. U. | VACUNAS PROFILACTICAS DE GRIPE A PARTIR DE CAPSIDAS VIRALES DE BIRNAVIRUS CONTENIENDO EL ANTIGENO M2e DEL VIRUS DE LA GRIPE |
| US10130697B2 (en) | 2010-03-23 | 2018-11-20 | Wisconsin Alumni Research Foundation (Warf) | Vaccines comprising mutant attenuated influenza viruses |
| CA2828068C (en) | 2011-02-22 | 2019-03-19 | Biondvax Pharmaceuticals Ltd. | Multimeric multiepitope polypeptides in improved seasonal and pandemic influenza vaccines |
| WO2013032942A1 (en) | 2011-08-26 | 2013-03-07 | Yoshihiro Kawaoka | Influenza viruses with mutant pb2 gene segment as live attenuated vaccines |
| US8932598B2 (en) | 2012-08-28 | 2015-01-13 | Vaxinnate Corporation | Fusion proteins and methods of use |
| EP3022296B1 (en) | 2013-07-15 | 2022-12-28 | Wisconsin Alumni Research Foundation | High titer recombinant influenza viruses with enhanced replication in mdck or vero cells or eggs |
| WO2015196150A2 (en) | 2014-06-20 | 2015-12-23 | Wisconsin Alumni Research Foundation (Warf) | Mutations that confer genetic stability to additional genes in influenza viruses |
| US10633422B2 (en) | 2015-06-01 | 2020-04-28 | Wisconsin Alumni Research Foundation (Warf) | Influenza virus replication by inhibiting microRNA lec7C binding to influenza viral cRNA and mRNA |
| EP3103474A1 (en) * | 2015-06-12 | 2016-12-14 | Institut Pasteur | Live recombinant measles-m2 virus and its use in eliciting immunity against influenza viruses |
| WO2017007839A1 (en) | 2015-07-06 | 2017-01-12 | Wisconsin Alumni Research Foundation (Warf) | Improved influenza virus replication for vaccine development |
| EP3417056A1 (en) | 2016-02-19 | 2018-12-26 | Wisconsin Alumni Research Foundation (WARF) | Improved influenza b virus replication for vaccine development |
| JP2021500891A (ja) | 2017-10-25 | 2021-01-14 | ウィスコンシン アルムニ リサーチ ファンデイション | 卵における複製のための安定化されたｈａを有する組換えインフルエンザウイルス |
| US12343390B2 (en) | 2018-08-07 | 2025-07-01 | Wisconsin Alumni Research Foundation (Warf) | Recombinant biologically contained filovirus vaccine |
| JP7655849B2 (ja) | 2018-08-20 | 2025-04-02 | ウィスコンシン アルムニ リサーチ ファンデイション | ヘマグルチニン（ｈａ）タンパク質内の非ドミナントエピトープに対する免疫応答を誘起するためのベクター |
| US11241492B2 (en) | 2019-01-23 | 2022-02-08 | Wisconsin Alumni Research Foundation (Warf) | Mutations that confer genetic stability to genes in influenza viruses |
| EP3921413A1 (en) | 2019-02-08 | 2021-12-15 | Wisconsin Alumni Research Foundation (WARF) | Humanized cell line |
| US11390649B2 (en) | 2019-05-01 | 2022-07-19 | Wisconsin Alumni Research Foundation (Warf) | Influenza virus replication for vaccine development |
| WO2021041624A2 (en) | 2019-08-27 | 2021-03-04 | Yoshihiro Kawaoka | Recombinant influenza viruses with stabilized ha for replication in eggs |
| JP2023511444A (ja) | 2020-01-24 | 2023-03-17 | ウィスコンシン アルムニ リサーチ ファンデイション | 安定化されたｎａを有する組換えインフルエンザウイルス |
| US12290562B2 (en) | 2020-03-25 | 2025-05-06 | Wisconsin Alumni Research Foundation (Warf) | Recombinant multivalent influenza viruses |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3919044A (en) * | 1973-03-28 | 1975-11-11 | Armour Pharma | Processes for concentrating and purifying viruses and viral antigens |
| NZ219516A (en) * | 1987-02-10 | 1991-02-26 | Wellcome Found | Fusion proteins of hbcag (hepatitis b virus core antigen) |
| EP0590055B1 (en) * | 1991-06-19 | 1997-12-03 | New York Medical College | M-protein peptides of influenza virus as antiviral agents |
| FR2695563B1 (fr) | 1992-09-11 | 1994-12-02 | Pasteur Institut | Microparticules portant des antigènes et leur utilisation pour l'induction de réponses humorales ou cellulaires. |
| ES2180576T3 (es) * | 1993-04-27 | 2003-02-16 | United Biomedical Inc | Construcciones peptidicas de lhrh inmunogenicas y estimuladores de inmunidad universales sinteticos para vacunas. |
| US5759551A (en) | 1993-04-27 | 1998-06-02 | United Biomedical, Inc. | Immunogenic LHRH peptide constructs and synthetic universal immune stimulators for vaccines |
| WO1995004151A2 (en) * | 1993-07-30 | 1995-02-09 | Medeva Holdings B.V. | Vaccine compositions containing recombinant tetc-fusion proteins |
| US5691189A (en) * | 1994-01-19 | 1997-11-25 | Bristol-Myers Squibb Company | Saccharomyces cerevisiae expressing M2 protein of influenza A virus |
| GB9424631D0 (en) * | 1994-12-06 | 1995-01-25 | Lynxvale Ltd | Modulating the immune response |
| GB9521568D0 (en) * | 1995-10-20 | 1995-12-20 | Lynxvale Ltd | Delivery of biologically active polypeptides |
| EP0941315B1 (en) | 1996-11-26 | 2006-03-01 | Stressgen Biotechnologies Corporation | Fusion proteins containing stress proteins for inducing immune responses |
| ES2255181T3 (es) | 1997-08-05 | 2006-06-16 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw. | Antigeno inmunoprotector contra la gripe y su uso en vacunacion. |
| US6169175B1 (en) * | 1997-08-06 | 2001-01-02 | Centers For Disease Control And Prevention | Preparation and use of recombinant influenza A virus M2 construct vaccines |
| US20020015951A1 (en) | 2000-01-06 | 2002-02-07 | Bader Joel S. | Method of analyzing a nucleic acid |
-
1998
- 1998-08-05 ES ES98946321T patent/ES2255181T3/es not_active Expired - Lifetime
- 1998-08-05 AU AU93416/98A patent/AU745951B2/en not_active Expired
- 1998-08-05 AT AT98946321T patent/ATE312172T1/de active
- 1998-08-05 JP JP2000506324A patent/JP5132851B2/ja not_active Expired - Lifetime
- 1998-08-05 WO PCT/EP1998/005106 patent/WO1999007839A2/en not_active Ceased
- 1998-08-05 DK DK98946321T patent/DK0996717T3/da active
- 1998-08-05 EP EP98946321A patent/EP0996717B1/en not_active Revoked
- 1998-08-05 CA CA2297786A patent/CA2297786C/en not_active Expired - Lifetime
- 1998-08-05 DE DE69832706T patent/DE69832706T2/de not_active Expired - Lifetime
-
2006
- 2006-03-14 US US11/374,922 patent/US7732130B2/en active Active
-
2009
- 2009-10-16 JP JP2009239092A patent/JP2010059164A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| JP2010059164A (ja) | 2010-03-18 |
| JP5132851B2 (ja) | 2013-01-30 |
| DE69832706D1 (de) | 2006-01-12 |
| EP0996717B1 (en) | 2005-12-07 |
| CA2297786A1 (en) | 1999-02-18 |
| ES2255181T3 (es) | 2006-06-16 |
| US7732130B2 (en) | 2010-06-08 |
| WO1999007839A3 (en) | 1999-05-14 |
| AU745951B2 (en) | 2002-04-11 |
| US20060246092A1 (en) | 2006-11-02 |
| WO1999007839A2 (en) | 1999-02-18 |
| ATE312172T1 (de) | 2005-12-15 |
| AU9341698A (en) | 1999-03-01 |
| EP0996717A2 (en) | 2000-05-03 |
| CA2297786C (en) | 2011-06-14 |
| JP2001512748A (ja) | 2001-08-28 |
| DK0996717T3 (da) | 2006-04-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DE69832706T2 (de) | Immunschützendes influenzaantigen und dessen verwendung zur impfung | |
| DE69021575T4 (de) | Expressionssysteme für rekombinante negativstrang-rna-viren und impfstoffe | |
| DE69032284T2 (de) | Expression von exogenen polynukleotidsequenzen in wirbeltieren | |
| DE69534449T2 (de) | Vektor und methode zur herstellung von influenza hämagglutinin | |
| DE69519041T2 (de) | Dna-impfstoffe gegen rotavirusinfektionen | |
| DE69932425T2 (de) | Attenuierte salmonella mutanten, welche das vi-antigen konstant exprimieren | |
| EP2102345B1 (de) | Rsv f-protein und seine verwendung | |
| CA2323634A1 (en) | Lactobacilli harboring aggregation and mucin binding genes as vaccine delivery vehicles | |
| US7993652B2 (en) | Immunoprotective influenza antigen and its use in vaccination | |
| DE60125528T2 (de) | Isolierung und charakterisierung des csa-operons (etec-cs4 pili) und verfahren zu dessen anwendung | |
| DE68923286T2 (de) | Impfstoffe und testsätze für haemophilus influenzae. | |
| DE69828414T2 (de) | Mukosale zytotoxische t-lymphozytenantwort | |
| EP2844759A1 (de) | Vakzinierung mittels rekombinanter hefe durch erzeugung einer protektiven humoralen immunantwort gegen definierte antigene | |
| DE68928529T2 (de) | Expression der bindenden Untereinheit des Choleratoxins mit Hilfe von fremden Promotoren und/oder Leadersequenzen | |
| US5330753A (en) | Cholera vaccines | |
| EP0696322A1 (en) | METHODS AND COMPOSITIONS FOR $i(SALMONELLA)-BASED VACCINES | |
| DE69633179T2 (de) | Transferrinrezeptorgene | |
| DE60319741T2 (de) | Einschlusskörper für die mündliche impfung von tieren | |
| DE60016806T2 (de) | Selfantigen-impfstoffe zur behandlung von b-zell lymphomen und sonstigen krebsen | |
| AT409863B (de) | Hoch effiziente expression eines polypeptids, das eine modifizierte pres1-region des grossen hepatitis b-virus-antigens enthält | |
| DE69325294T2 (de) | Keuchhusten-Impfstoff | |
| US5472871A (en) | Isolation and characterization of the nematode HER-1 Gene and protein product | |
| DE69535716T2 (de) | Methode für die Produktion von multivalenten Influenza Hämagglutinin Vakzinen | |
| DE60036563T2 (de) | Nucleoprotein des toscanavirus | |
| WO1988008431A1 (en) | Cholera vaccines |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| 8363 | Opposition against the patent |