JP2008506364A - 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド - Google Patents
型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド Download PDFInfo
- Publication number
- JP2008506364A JP2008506364A JP2007512595A JP2007512595A JP2008506364A JP 2008506364 A JP2008506364 A JP 2008506364A JP 2007512595 A JP2007512595 A JP 2007512595A JP 2007512595 A JP2007512595 A JP 2007512595A JP 2008506364 A JP2008506364 A JP 2008506364A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- nucleic acid
- present
- sequence
- seq
- 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.)
- Withdrawn
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 124
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 121
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 117
- 241000606768 Haemophilus influenzae Species 0.000 title abstract description 10
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 97
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 91
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 91
- 238000000034 method Methods 0.000 claims abstract description 41
- 206010033078 Otitis media Diseases 0.000 claims abstract description 17
- 206010022000 influenza Diseases 0.000 claims abstract description 15
- 208000015181 infectious disease Diseases 0.000 claims abstract description 12
- 201000010099 disease Diseases 0.000 claims abstract description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract description 8
- 239000003814 drug Substances 0.000 claims abstract description 5
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 4
- 239000000203 mixture Substances 0.000 claims description 86
- 150000001413 amino acids Chemical class 0.000 claims description 41
- 239000002773 nucleotide Substances 0.000 claims description 25
- 125000003729 nucleotide group Chemical group 0.000 claims description 25
- 239000012634 fragment Substances 0.000 claims description 14
- 238000004519 manufacturing process Methods 0.000 claims description 7
- 201000009906 Meningitis Diseases 0.000 claims description 6
- 206010035664 Pneumonia Diseases 0.000 claims description 6
- 206010010741 Conjunctivitis Diseases 0.000 claims description 4
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 4
- 206010053555 Arthritis bacterial Diseases 0.000 claims description 3
- 208000031729 Bacteremia Diseases 0.000 claims description 3
- 206010007882 Cellulitis Diseases 0.000 claims description 3
- 206010014568 Empyema Diseases 0.000 claims description 3
- 206010031252 Osteomyelitis Diseases 0.000 claims description 3
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 3
- 206010006451 bronchitis Diseases 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 208000001606 epiglottitis Diseases 0.000 claims description 3
- 208000008494 pericarditis Diseases 0.000 claims description 3
- 201000009890 sinusitis Diseases 0.000 claims description 3
- 208000019206 urinary tract infection Diseases 0.000 claims description 3
- 239000012646 vaccine adjuvant Substances 0.000 claims description 2
- 229940124931 vaccine adjuvant Drugs 0.000 claims description 2
- 108090000623 proteins and genes Proteins 0.000 abstract description 67
- 102000004169 proteins and genes Human genes 0.000 abstract description 62
- 229940047650 haemophilus influenzae Drugs 0.000 abstract description 4
- 235000018102 proteins Nutrition 0.000 description 61
- 239000000427 antigen Substances 0.000 description 45
- 108091007433 antigens Proteins 0.000 description 41
- 102000036639 antigens Human genes 0.000 description 41
- 239000002671 adjuvant Substances 0.000 description 32
- 235000001014 amino acid Nutrition 0.000 description 26
- 230000000295 complement effect Effects 0.000 description 26
- 239000013615 primer Substances 0.000 description 24
- 229940024606 amino acid Drugs 0.000 description 23
- 150000001875 compounds Chemical class 0.000 description 20
- 229960005486 vaccine Drugs 0.000 description 18
- 230000008569 process Effects 0.000 description 17
- 210000004027 cell Anatomy 0.000 description 16
- 229930182490 saponin Natural products 0.000 description 16
- 150000007949 saponins Chemical class 0.000 description 16
- 235000017709 saponins Nutrition 0.000 description 16
- 108091034117 Oligonucleotide Proteins 0.000 description 14
- 108020004414 DNA Proteins 0.000 description 12
- 238000009472 formulation Methods 0.000 description 12
- 239000002245 particle Substances 0.000 description 12
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 11
- -1 aromatic amino acids Chemical class 0.000 description 11
- 238000009396 hybridization Methods 0.000 description 11
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 11
- DRHZYJAUECRAJM-DWSYSWFDSA-N (2s,3s,4s,5r,6r)-6-[[(3s,4s,4ar,6ar,6bs,8r,8ar,12as,14ar,14br)-8a-[(2s,3r,4s,5r,6r)-3-[(2s,3r,4s,5r,6s)-5-[(2s,3r,4s,5r)-4-[(2s,3r,4r)-3,4-dihydroxy-4-(hydroxymethyl)oxolan-2-yl]oxy-3,5-dihydroxyoxan-2-yl]oxy-3,4-dihydroxy-6-methyloxan-2-yl]oxy-5-[(3s,5s, Chemical compound O([C@H]1[C@H](O)[C@H](O[C@H]([C@@H]1O[C@H]1[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O1)O)O[C@H]1CC[C@]2(C)[C@H]3CC=C4[C@@H]5CC(C)(C)CC[C@@]5([C@@H](C[C@@]4(C)[C@]3(C)CC[C@H]2[C@@]1(C=O)C)O)C(=O)O[C@@H]1O[C@H](C)[C@@H]([C@@H]([C@H]1O[C@H]1[C@@H]([C@H](O)[C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@](O)(CO)CO3)O)[C@H](O)CO2)O)[C@H](C)O1)O)O)OC(=O)C[C@@H](O)C[C@H](OC(=O)C[C@@H](O)C[C@@H]([C@@H](C)CC)O[C@H]1[C@@H]([C@@H](O)[C@H](CO)O1)O)[C@@H](C)CC)C(O)=O)[C@@H]1OC[C@@H](O)[C@H](O)[C@H]1O DRHZYJAUECRAJM-DWSYSWFDSA-N 0.000 description 10
- 239000012528 membrane Substances 0.000 description 10
- 108091028043 Nucleic acid sequence Proteins 0.000 description 9
- 230000003053 immunization Effects 0.000 description 9
- 238000002649 immunization Methods 0.000 description 9
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 9
- 239000000523 sample Substances 0.000 description 9
- 238000003786 synthesis reaction Methods 0.000 description 9
- 238000012360 testing method Methods 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 201000005702 Pertussis Diseases 0.000 description 8
- 230000001580 bacterial effect Effects 0.000 description 8
- 238000002347 injection Methods 0.000 description 8
- 239000007924 injection Substances 0.000 description 8
- 239000003053 toxin Substances 0.000 description 8
- 231100000765 toxin Toxicity 0.000 description 8
- 108700012359 toxins Proteins 0.000 description 8
- 238000011282 treatment Methods 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 239000002158 endotoxin Substances 0.000 description 7
- 230000002163 immunogen Effects 0.000 description 7
- 229920006008 lipopolysaccharide Polymers 0.000 description 7
- 231100000252 nontoxic Toxicity 0.000 description 7
- 230000003000 nontoxic effect Effects 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 230000003321 amplification Effects 0.000 description 6
- 230000003115 biocidal effect Effects 0.000 description 6
- 239000012472 biological sample Substances 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 6
- 239000000839 emulsion Substances 0.000 description 6
- 230000028993 immune response Effects 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 230000001717 pathogenic effect Effects 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- 108091081024 Start codon Proteins 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 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 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 230000003308 immunostimulating effect Effects 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 229920000642 polymer Polymers 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 239000004094 surface-active agent Substances 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- NYHBQMYGNKIUIF-UUOKFMHZSA-N Guanosine Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O NYHBQMYGNKIUIF-UUOKFMHZSA-N 0.000 description 4
- 241000606790 Haemophilus Species 0.000 description 4
- 101710116435 Outer membrane protein Proteins 0.000 description 4
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 4
- 206010043376 Tetanus Diseases 0.000 description 4
- 239000003242 anti bacterial agent Substances 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 206010013023 diphtheria Diseases 0.000 description 4
- 210000000959 ear middle Anatomy 0.000 description 4
- 239000007850 fluorescent dye Substances 0.000 description 4
- 150000004676 glycans Chemical class 0.000 description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 238000000338 in vitro Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- GZQKNULLWNGMCW-PWQABINMSA-N lipid A (E. coli) Chemical class O1[C@H](CO)[C@@H](OP(O)(O)=O)[C@H](OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC)[C@@H](NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC)[C@@H]1OC[C@@H]1[C@@H](O)[C@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OP(O)(O)=O)O1 GZQKNULLWNGMCW-PWQABINMSA-N 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 210000001322 periplasm Anatomy 0.000 description 4
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 4
- 229920001282 polysaccharide Polymers 0.000 description 4
- 239000005017 polysaccharide Substances 0.000 description 4
- 229920000053 polysorbate 80 Polymers 0.000 description 4
- 239000002987 primer (paints) Substances 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 239000000277 virosome Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 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 3
- 208000035143 Bacterial infection Diseases 0.000 description 3
- 108010039939 Cell Wall Skeleton Proteins 0.000 description 3
- 238000002965 ELISA Methods 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 3
- 229930182558 Sterol Natural products 0.000 description 3
- 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 3
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 3
- 208000022362 bacterial infectious disease Diseases 0.000 description 3
- 239000000227 bioadhesive Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 210000004520 cell wall skeleton Anatomy 0.000 description 3
- 235000012000 cholesterol Nutrition 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 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 3
- 230000006870 function Effects 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 239000002955 immunomodulating agent Substances 0.000 description 3
- 229940121354 immunomodulator Drugs 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 208000022760 infectious otitis media Diseases 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 239000002502 liposome Substances 0.000 description 3
- 238000002493 microarray Methods 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000011859 microparticle Substances 0.000 description 3
- 238000012544 monitoring process Methods 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 150000003904 phospholipids Chemical class 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 229920000056 polyoxyethylene ether Polymers 0.000 description 3
- 229920000136 polysorbate Polymers 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 229940031439 squalene Drugs 0.000 description 3
- 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 3
- 235000003702 sterols Nutrition 0.000 description 3
- 238000013519 translation 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
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 101710132601 Capsid protein Proteins 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 102000053642 Catalytic RNA Human genes 0.000 description 2
- 108090000994 Catalytic RNA Proteins 0.000 description 2
- 102100038385 Coiled-coil domain-containing protein R3HCC1L Human genes 0.000 description 2
- MIKUYHXYGGJMLM-GIMIYPNGSA-N Crotonoside Natural products C1=NC2=C(N)NC(=O)N=C2N1[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O MIKUYHXYGGJMLM-GIMIYPNGSA-N 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 150000008574 D-amino acids Chemical class 0.000 description 2
- NYHBQMYGNKIUIF-UHFFFAOYSA-N D-guanosine Natural products C1=2NC(N)=NC(=O)C=2N=CN1C1OC(CO)C(O)C1O NYHBQMYGNKIUIF-UHFFFAOYSA-N 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 241000700721 Hepatitis B virus Species 0.000 description 2
- 101000743767 Homo sapiens Coiled-coil domain-containing protein R3HCC1L Proteins 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- 108010065805 Interleukin-12 Proteins 0.000 description 2
- 241000588747 Klebsiella pneumoniae Species 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 241000588655 Moraxella catarrhalis Species 0.000 description 2
- 108700020354 N-acetylmuramyl-threonyl-isoglutamine Proteins 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 101710163270 Nuclease Proteins 0.000 description 2
- 108700006640 OspA Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 108091093037 Peptide nucleic acid Proteins 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 241000219287 Saponaria Species 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- 241000194017 Streptococcus Species 0.000 description 2
- 241000193985 Streptococcus agalactiae Species 0.000 description 2
- 241000193998 Streptococcus pneumoniae Species 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 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
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 108010067390 Viral Proteins Proteins 0.000 description 2
- 239000003463 adsorbent Substances 0.000 description 2
- NWMHDZMRVUOQGL-CZEIJOLGSA-N almurtide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)CO[C@@H]([C@H](O)[C@H](O)CO)[C@@H](NC(C)=O)C=O NWMHDZMRVUOQGL-CZEIJOLGSA-N 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
- AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 2
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 229960003983 diphtheria toxoid Drugs 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 229930182470 glycoside Natural products 0.000 description 2
- 229940029575 guanosine Drugs 0.000 description 2
- 229930186900 holotoxin Natural products 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 239000007972 injectable composition Substances 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 230000009545 invasion Effects 0.000 description 2
- 230000029226 lipidation Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000006193 liquid solution Substances 0.000 description 2
- 239000006194 liquid suspension Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000003232 mucoadhesive effect Effects 0.000 description 2
- 125000001446 muramyl group Chemical group N[C@@H](C=O)[C@@H](O[C@@H](C(=O)*)C)[C@H](O)[C@H](O)CO 0.000 description 2
- 229920002113 octoxynol Polymers 0.000 description 2
- 229940066429 octoxynol Drugs 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 150000002482 oligosaccharides Chemical class 0.000 description 2
- UNEIHNMKASENIG-UHFFFAOYSA-N para-chlorophenylpiperazine Chemical compound C1=CC(Cl)=CC=C1N1CCNCC1 UNEIHNMKASENIG-UHFFFAOYSA-N 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 235000021317 phosphate Nutrition 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 230000037452 priming Effects 0.000 description 2
- 238000011321 prophylaxis Methods 0.000 description 2
- 230000002685 pulmonary effect Effects 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 108091092562 ribozyme Proteins 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 238000010845 search algorithm Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 150000003432 sterols Chemical class 0.000 description 2
- 229940031000 streptococcus pneumoniae Drugs 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- XETCRXVKJHBPMK-MJSODCSWSA-N trehalose 6,6'-dimycolate Chemical compound C([C@@H]1[C@H]([C@H](O)[C@@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](COC(=O)C(CCCCCCCCCCC3C(C3)CCCCCCCCCCCCCCCCCC)C(O)CCCCCCCCCCCCCCCCCCCCCCCCC)O2)O)O1)O)OC(=O)C(C(O)CCCCCCCCCCCCCCCCCCCCCCCCC)CCCCCCCCCCC1CC1CCCCCCCCCCCCCCCCCC XETCRXVKJHBPMK-MJSODCSWSA-N 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 1
- NNWQLZWAZSJGLY-VKHMYHEASA-N (2s)-2-azaniumyl-4-azidobutanoate Chemical compound OC(=O)[C@@H](N)CCN=[N+]=[N-] NNWQLZWAZSJGLY-VKHMYHEASA-N 0.000 description 1
- YHQZWWDVLJPRIF-JLHRHDQISA-N (4R)-4-[[(2S,3R)-2-[acetyl-[(3R,4R,5S,6R)-3-amino-4-[(1R)-1-carboxyethoxy]-5-hydroxy-6-(hydroxymethyl)oxan-2-yl]amino]-3-hydroxybutanoyl]amino]-5-amino-5-oxopentanoic acid Chemical compound C(C)(=O)N([C@@H]([C@H](O)C)C(=O)N[C@H](CCC(=O)O)C(N)=O)C1[C@H](N)[C@@H](O[C@@H](C(=O)O)C)[C@H](O)[C@H](O1)CO YHQZWWDVLJPRIF-JLHRHDQISA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
- PFCLMNDDPTZJHQ-XLPZGREQSA-N 2-amino-7-[(2r,4s,5r)-4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]-1h-pyrrolo[2,3-d]pyrimidin-4-one Chemical compound C1=CC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](CO)O1 PFCLMNDDPTZJHQ-XLPZGREQSA-N 0.000 description 1
- RHKWIGHJGOEUSM-UHFFFAOYSA-N 3h-imidazo[4,5-h]quinoline Chemical class C1=CN=C2C(N=CN3)=C3C=CC2=C1 RHKWIGHJGOEUSM-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 description 1
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 description 1
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000031504 Asymptomatic Infections Diseases 0.000 description 1
- 108010071134 CRM197 (non-toxic variant of diphtheria toxin) Proteins 0.000 description 1
- 108090000565 Capsid Proteins Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical compound [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 description 1
- 241000700112 Chinchilla Species 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- YVGGHNCTFXOJCH-UHFFFAOYSA-N DDT Chemical compound C1=CC(Cl)=CC=C1C(C(Cl)(Cl)Cl)C1=CC=C(Cl)C=C1 YVGGHNCTFXOJCH-UHFFFAOYSA-N 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 240000006541 Dactyloctenium aegyptium Species 0.000 description 1
- 206010011878 Deafness Diseases 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000305071 Enterobacterales Species 0.000 description 1
- 101710146739 Enterotoxin Proteins 0.000 description 1
- 101710204837 Envelope small membrane protein Proteins 0.000 description 1
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- JZNWSCPGTDBMEW-UHFFFAOYSA-N Glycerophosphorylethanolamin Natural products NCCOP(O)(=O)OCC(O)CO JZNWSCPGTDBMEW-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 240000003824 Gypsophila paniculata Species 0.000 description 1
- 206010061190 Haemophilus infection Diseases 0.000 description 1
- 241001235200 Haemophilus influenzae Rd KW20 Species 0.000 description 1
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 1
- 108010004889 Heat-Shock Proteins Proteins 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 241000709721 Hepatovirus A Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 241000701806 Human papillomavirus Species 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 108090000978 Interleukin-4 Proteins 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- 108010002586 Interleukin-7 Proteins 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 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
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 229920002884 Laureth 4 Polymers 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 206010024971 Lower respiratory tract infections Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 101710145006 Lysis protein Proteins 0.000 description 1
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 201000005505 Measles Diseases 0.000 description 1
- 241000712079 Measles morbillivirus Species 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108090000301 Membrane transport proteins Proteins 0.000 description 1
- 102000003939 Membrane transport proteins Human genes 0.000 description 1
- 241001300083 Milax Species 0.000 description 1
- 241001092142 Molina Species 0.000 description 1
- 208000005647 Mumps Diseases 0.000 description 1
- 108700015872 N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine Proteins 0.000 description 1
- PYUSHNKNPOHWEZ-YFKPBYRVSA-N N-formyl-L-methionine Chemical group CSCC[C@@H](C(O)=O)NC=O PYUSHNKNPOHWEZ-YFKPBYRVSA-N 0.000 description 1
- 241001644525 Nastus productus Species 0.000 description 1
- 241000588650 Neisseria meningitidis Species 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 241000714209 Norwalk virus Species 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010090127 Periplasmic Proteins Proteins 0.000 description 1
- 108010081690 Pertussis Toxin Proteins 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 241000702670 Rotavirus Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000710960 Sindbis virus Species 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- PRXRUNOAOLTIEF-ADSICKODSA-N Sorbitan trioleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](OC(=O)CCCCCCC\C=C/CCCCCCCC)[C@H]1OC[C@H](O)[C@H]1OC(=O)CCCCCCC\C=C/CCCCCCCC PRXRUNOAOLTIEF-ADSICKODSA-N 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 241000193996 Streptococcus pyogenes Species 0.000 description 1
- 230000029662 T-helper 1 type immune response Effects 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-N Thiophosphoric acid Chemical class OP(O)(S)=O RYYWUUFWQRZTIU-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
- 102000008235 Toll-Like Receptor 9 Human genes 0.000 description 1
- 108010060818 Toll-Like Receptor 9 Proteins 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 230000000240 adjuvant effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000005907 alkyl ester group Chemical group 0.000 description 1
- 150000005215 alkyl ethers Chemical class 0.000 description 1
- 229940061720 alpha hydroxy acid Drugs 0.000 description 1
- 150000001280 alpha hydroxy acids Chemical class 0.000 description 1
- 125000000266 alpha-aminoacyl group Chemical group 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 229940047712 aluminum hydroxyphosphate Drugs 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000010913 antigen-directed enzyme pro-drug therapy Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000000074 antisense oligonucleotide Substances 0.000 description 1
- 238000012230 antisense oligonucleotides Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000013528 artificial neural network Methods 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000008952 bacterial invasion Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 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
- 159000000007 calcium salts Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000003093 cationic surfactant Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000013553 cell monolayer Substances 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical class NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001784 detoxification Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000006196 drop Substances 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000000147 enterotoxin Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 210000002388 eustachian tube Anatomy 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000010419 fine particle Substances 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000012268 genome sequencing Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000010370 hearing loss Effects 0.000 description 1
- 231100000888 hearing loss Toxicity 0.000 description 1
- 208000016354 hearing loss disease Diseases 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229960003160 hyaluronic acid Drugs 0.000 description 1
- 150000004679 hydroxides Chemical class 0.000 description 1
- 229940124669 imidazoquinoline Drugs 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000002584 immunomodulator Effects 0.000 description 1
- 229960001438 immunostimulant agent Drugs 0.000 description 1
- 239000003022 immunostimulating agent Substances 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 150000002484 inorganic compounds Chemical class 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000008140 language development Effects 0.000 description 1
- 229940062711 laureth-9 Drugs 0.000 description 1
- 150000002611 lead compounds Chemical class 0.000 description 1
- 230000013016 learning Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- JMUHBNWAORSSBD-WKYWBUFDSA-N mifamurtide Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@@H](OC(=O)CCCCCCCCCCCCCCC)COP(O)(=O)OCCNC(=O)[C@H](C)NC(=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 JMUHBNWAORSSBD-WKYWBUFDSA-N 0.000 description 1
- 229960005225 mifamurtide Drugs 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- ZLVYMPOQNJTFSG-QMMMGPOBSA-N monoiodotyrosine Chemical compound OC(=O)[C@@H](NI)CC1=CC=C(O)C=C1 ZLVYMPOQNJTFSG-QMMMGPOBSA-N 0.000 description 1
- 208000010805 mumps infectious disease Diseases 0.000 description 1
- SCIFESDRCALIIM-UHFFFAOYSA-N n-methylphenylalanine Chemical compound CNC(C(O)=O)CC1=CC=CC=C1 SCIFESDRCALIIM-UHFFFAOYSA-N 0.000 description 1
- 230000017066 negative regulation of growth Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 239000007764 o/w emulsion Substances 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 229940099789 ospa protein Drugs 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 108010021711 pertactin Proteins 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 108700010839 phage proteins Proteins 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 150000008104 phosphatidylethanolamines Chemical class 0.000 description 1
- 150000008300 phosphoramidites Chemical class 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- ONJQDTZCDSESIW-UHFFFAOYSA-N polidocanol Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO ONJQDTZCDSESIW-UHFFFAOYSA-N 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920001606 poly(lactic acid-co-glycolic acid) Polymers 0.000 description 1
- 239000002745 poly(ortho ester) Substances 0.000 description 1
- 229920002627 poly(phosphazenes) Polymers 0.000 description 1
- 239000004584 polyacrylic acid Substances 0.000 description 1
- 229920001610 polycaprolactone Polymers 0.000 description 1
- 239000004632 polycaprolactone Substances 0.000 description 1
- 108010094020 polyglycine Proteins 0.000 description 1
- 229920000232 polyglycine polymer Polymers 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229940051841 polyoxyethylene ether Drugs 0.000 description 1
- 229950008882 polysorbate Drugs 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 150000003230 pyrimidines Chemical class 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 201000005404 rubella Diseases 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000004960 subcellular localization Effects 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 101150118483 tmk gene Proteins 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 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
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 238000010396 two-hybrid screening Methods 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 210000000689 upper leg Anatomy 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000001018 virulence Effects 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/285—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Pasteurellaceae (F), e.g. Haemophilus influenza
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/102—Pasteurellales, e.g. Actinobacillus, Pasteurella; Haemophilus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/02—Nasal agents, e.g. decongestants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/04—Drugs for disorders of the respiratory system for throat disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/16—Otologicals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- 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
-
- 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
-
- 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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- 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
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/53—DNA (RNA) vaccination
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Communicable Diseases (AREA)
- Immunology (AREA)
- Pulmonology (AREA)
- Oncology (AREA)
- Virology (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Rheumatology (AREA)
- Otolaryngology (AREA)
- Epidemiology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Physical Education & Sports Medicine (AREA)
- Urology & Nephrology (AREA)
- Ophthalmology & Optometry (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Pain & Pain Management (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB0410866.8A GB0410866D0 (en) | 2004-05-14 | 2004-05-14 | Haemophilius influenzae |
| PCT/IB2005/001775 WO2005111066A2 (en) | 2004-05-14 | 2005-05-16 | Polypeptides from non-typeable haemophilus influenzae |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011166505A Division JP2012000112A (ja) | 2004-05-14 | 2011-07-29 | 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JP2008506364A true JP2008506364A (ja) | 2008-03-06 |
Family
ID=32527109
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007512595A Withdrawn JP2008506364A (ja) | 2004-05-14 | 2005-05-16 | 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド |
| JP2011166505A Pending JP2012000112A (ja) | 2004-05-14 | 2011-07-29 | 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011166505A Pending JP2012000112A (ja) | 2004-05-14 | 2011-07-29 | 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド |
Country Status (10)
| Country | Link |
|---|---|
| US (4) | US7749518B2 (https=) |
| EP (5) | EP2341069A1 (https=) |
| JP (2) | JP2008506364A (https=) |
| CN (1) | CN1997663A (https=) |
| BR (1) | BRPI0511118A (https=) |
| CA (1) | CA2566632A1 (https=) |
| GB (1) | GB0410866D0 (https=) |
| IN (1) | IN2015KN00290A (https=) |
| RU (1) | RU2432357C2 (https=) |
| WO (1) | WO2005111066A2 (https=) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2015515486A (ja) * | 2012-04-26 | 2015-05-28 | ノバルティス アーゲー | 抗原および抗原の組み合わせ |
Families Citing this family (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2281409T3 (es) * | 2000-02-28 | 2007-10-01 | Novartis Vaccines And Diagnostics S.R.L. | Expresion heterologa de proteinas de neisseria. |
| HUE031886T2 (en) * | 2002-10-11 | 2017-08-28 | Glaxosmithkline Biologicals Sa | Polypeptide vaccines for extensive protection against hypervirulent meningococcal lines |
| WO2006138527A2 (en) | 2005-06-16 | 2006-12-28 | Children's Hospital, Inc. | Genes of an otitis media isolate of nontypeable haemophilus influenzae |
| GB0410866D0 (en) | 2004-05-14 | 2004-06-16 | Chiron Srl | Haemophilius influenzae |
| CN101687025A (zh) * | 2005-03-30 | 2010-03-31 | 诺华疫苗和诊断公司 | B型流感嗜血杆菌 |
| WO2007018463A2 (en) | 2005-08-10 | 2007-02-15 | Arne Forsgren Ab | Interaction of moraxella catarrhalis with epithelial cells, extracellular matrix proteins and the complement system |
| AU2007206114B2 (en) * | 2006-01-17 | 2013-01-24 | Arne Forsgren | A novel surface exposed Haemophilus influenzae protein (protein E; pE) |
| US9132183B2 (en) * | 2007-03-09 | 2015-09-15 | Newport Laboratories | Modified live (JMSO strain) Haemophilus parasuis vaccine |
| US8647642B2 (en) | 2008-09-18 | 2014-02-11 | Aviex Technologies, Llc | Live bacterial vaccines resistant to carbon dioxide (CO2), acidic PH and/or osmolarity for viral infection prophylaxis or treatment |
| JP2012512240A (ja) * | 2008-12-17 | 2012-05-31 | ノバルティス アーゲー | ヘモグロビン受容体を含む髄膜炎菌ワクチン |
| WO2010092176A2 (en) * | 2009-02-13 | 2010-08-19 | Intercell Ag | Nontypable haemophilus influenzae antigens |
| ITMI20090946A1 (it) | 2009-05-28 | 2010-11-29 | Novartis Ag | Espressione di proteine ricombinanti |
| HUE026646T2 (en) | 2010-07-06 | 2016-07-28 | Glaxosmithkline Biologicals Sa | Preferred liposomes containing lipids of PKA value for delivery of RNA |
| PL2591114T3 (pl) | 2010-07-06 | 2017-08-31 | Glaxosmithkline Biologicals Sa | Immunizacja dużych ssaków małymi dawkami rna |
| US9770463B2 (en) | 2010-07-06 | 2017-09-26 | Glaxosmithkline Biologicals Sa | Delivery of RNA to different cell types |
| RS63817B1 (sr) | 2010-07-06 | 2023-01-31 | Glaxosmithkline Biologicals Sa | Čestice za isporuku slične virionu za molekule samoreplicirajuće rnk |
| HUE047796T2 (hu) | 2010-07-06 | 2020-05-28 | Glaxosmithkline Biologicals Sa | RNS bevitele több immunútvonal bekapcsolására |
| PT3970742T (pt) | 2010-08-31 | 2022-06-27 | Glaxosmithkline Biologicals Sa | Lipossomas peguilados para entrega de arn codificador de imunogénio |
| ES2727583T3 (es) | 2010-08-31 | 2019-10-17 | Glaxosmithkline Biologicals Sa | Lípidos adecuados para la administración liposómica de ARN que codifica proteínas |
| JP2013544504A (ja) | 2010-10-11 | 2013-12-19 | ノバルティス アーゲー | 抗原送達プラットフォーム |
| TW201302779A (zh) | 2011-04-13 | 2013-01-16 | Glaxosmithkline Biolog Sa | 融合蛋白質及組合疫苗 |
| JP2014516028A (ja) * | 2011-05-11 | 2014-07-07 | リースベック ヘルスケア スウェーデン アクティエボラーグ | ラミニン及びビトロネクチン結合特性を有するタンパク質ｆ−新規インフルエンザ菌付着因子 |
| WO2013006838A1 (en) | 2011-07-06 | 2013-01-10 | Novartis Ag | Immunogenic combination compositions and uses thereof |
| US20140141070A1 (en) | 2011-07-06 | 2014-05-22 | Andrew Geall | Liposomes having useful n:p ratio for delivery of rna molecules |
| EP3508220A1 (en) | 2011-08-31 | 2019-07-10 | GlaxoSmithKline Biologicals S.A. | Pegylated liposomes for delivery of immunogen-encoding rna |
| US10279026B2 (en) | 2012-04-26 | 2019-05-07 | Glaxosmithkline Biologicals Sa | Antigens and antigen combinations |
| US9764027B2 (en) | 2012-09-18 | 2017-09-19 | Glaxosmithkline Biologicals Sa | Outer membrane vesicles |
| EP3608308B1 (en) | 2013-03-08 | 2021-07-21 | Novartis AG | Lipids and lipid compositions for the delivery of active agents |
| US11274144B2 (en) | 2013-06-13 | 2022-03-15 | Research Institute At Nationwide Children's Hospital | Compositions and methods for the removal of biofilms |
| US11248040B2 (en) | 2013-09-26 | 2022-02-15 | Trellis Bioscience, Llc | Binding moieties for biofilm remediation |
| ES2895651T3 (es) | 2013-12-19 | 2022-02-22 | Novartis Ag | Lípidos y composiciones lipídicas para la administración de agentes activos |
| EP4019506A1 (en) | 2013-12-19 | 2022-06-29 | Novartis AG | Lipids and lipid compositions for the delivery of active agents |
| EP3169309B1 (en) | 2014-07-16 | 2023-05-10 | Novartis AG | Method of encapsulating a nucleic acid in a lipid nanoparticle host |
| CA2959322C (en) * | 2014-08-27 | 2022-07-19 | Switchfloat Holdings Limited | An oil field tubular and an internal sleeve for use therewith, and a method of deactivating a float valve within the oil field tubular |
| US10125092B2 (en) | 2014-09-05 | 2018-11-13 | Novartis Ag | Lipids and lipid compositions for the delivery of active agents |
| EP3061826A1 (en) | 2015-02-27 | 2016-08-31 | Novartis AG | Flavivirus replicons |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| WO2016200787A2 (en) | 2015-06-09 | 2016-12-15 | The Board Of Regents Of The University Of Oklahoma | Compositions and treatments for haemophilus influenzae |
| WO2017011588A1 (en) | 2015-07-14 | 2017-01-19 | Research Institute At Nationwide Children's Hospital | Novel formulation for the elimination of cariogenic and opportunistic pathogens within the oral cavity |
| AU2016303688B2 (en) | 2015-07-31 | 2023-06-15 | Research Institute At Nationwide Children's Hospital | Peptides and antibodies for the removal of biofilms |
| WO2017066719A2 (en) | 2015-10-14 | 2017-04-20 | Research Institute At Nationwide Children's Hospital | Hu specific interfering agents |
| EP3450446A1 (en) * | 2016-04-27 | 2019-03-06 | Biocells (Beijing) Biotech Co., Ltd. | Treatment method for excitatory neurotoxicity-related injury |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| JP7514621B2 (ja) | 2017-01-04 | 2024-07-11 | リサーチ インスティチュート アット ネイションワイド チルドレンズ ホスピタル | Ｄｎａｂｉｉワクチンおよび強化された活性を有する抗体 |
| AU2018206560B9 (en) | 2017-01-04 | 2025-04-03 | Research Institute At Nationwide Children's Hospital | Antibody fragments for the treatment of biofilm-related disorders |
| US20180221468A1 (en) * | 2017-01-19 | 2018-08-09 | Iowa State University Research Foundation, Inc. | Haemophilus influenzae immunogen |
| AU2018236271B2 (en) | 2017-03-15 | 2023-12-21 | Research Institute At Nationwide Children's Hospital | Composition and methods for disruption of bacterial biofilms without accompanying inflammation |
| SG11202103001PA (en) | 2018-10-05 | 2021-04-29 | Res Inst Nationwide Childrens Hospital | Hmgb1 protein derivatives for the removal of biofilms cross-reference to related application |
| US12569524B2 (en) | 2018-10-22 | 2026-03-10 | Research Institute At Nationwide Children's Hospital | Compositions and methods for preventing and treating antibiotic induced pathologies using probiotics in the biofilm state |
| WO2020174044A1 (en) * | 2019-02-27 | 2020-09-03 | Evaxion Biotech Aps | Vaccines targeting h. influenzae |
| WO2021007260A2 (en) | 2019-07-08 | 2021-01-14 | Research Institute At Nationwide Children's Hospital | Antibody compositions for disrupting biofilms |
| MX2022010406A (es) * | 2020-02-28 | 2022-11-09 | Trait Biosciences Inc | Sistemas, métodos y composiciones novedosas para la glucosilación de compuestos cannabinoides. |
| US12116614B2 (en) | 2020-06-30 | 2024-10-15 | Research Institute At Nationwide Children's Hospital | Methods for determining antibiotic sensitivity |
| JP2023546175A (ja) | 2020-10-14 | 2023-11-01 | ジョージ・メイソン・リサーチ・ファウンデーション・インコーポレイテッド | 脂質ナノ粒子製造の方法及びそれに由来する組成物 |
| CN115678869B (zh) * | 2021-07-28 | 2025-08-29 | 梅花(上海)生物科技有限公司 | 一株重组菌株及其生产氨基酸的方法 |
| WO2023021421A1 (en) | 2021-08-16 | 2023-02-23 | Glaxosmithkline Biologicals Sa | Low-dose lyophilized rna vaccines and methods for preparing and using the same |
| WO2023021427A1 (en) | 2021-08-16 | 2023-02-23 | Glaxosmithkline Biologicals Sa | Freeze-drying of lipid nanoparticles (lnps) encapsulating rna and formulations thereof |
| CN114574456B (zh) * | 2022-03-18 | 2022-08-12 | 华南理工大学 | 一种亚硝酸盐还原酶突变体及其编码基因和应用 |
| GB202303019D0 (en) | 2023-03-01 | 2023-04-12 | Glaxosmithkline Biologicals Sa | Method of lyophilisation |
| CN116236575B (zh) * | 2023-03-07 | 2025-03-25 | 北京化工大学 | 一种光控偶联型纳米探针及其制备方法、光控偶联的纳米颗粒组合物与应用 |
| GB202311382D0 (en) | 2023-07-25 | 2023-09-06 | Glaxosmithkline Biologicals Sa | Lyophilised compostion |
| CN118388664B (zh) * | 2024-05-21 | 2024-12-03 | 广东省农业科学院动物卫生研究所 | 副猪嗜血杆菌融合抗原及其应用 |
| WO2026033498A1 (en) | 2024-08-09 | 2026-02-12 | Genvax Technologies, Inc. | Methods of self-amplifying rna-lipid nanoparticle manufacture and compositions derived therefrom |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002083723A2 (en) * | 2001-04-12 | 2002-10-24 | Glaxosmithkline Biologicals Sa | Polypeptides from h. influenzae homologous to a surface-exposed protein of neisseria meningitidis |
| JP2006519605A (ja) * | 2003-03-06 | 2006-08-31 | チルドレンズ ホスピタル， インコーポレイテッド | 類型不能ｈａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅの中耳炎単離株の遺伝子 |
Family Cites Families (62)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB234768A (en) * | 1924-05-28 | 1925-08-27 | Ritter Dental Mfg Company Inc | Improvements in adjustable brackets for supporting head-rests or other articles |
| SE8205892D0 (sv) | 1982-10-18 | 1982-10-18 | Bror Morein | Immunogent membranproteinkomplex, sett for framstellning och anvendning derav som immunstimulerande medel och sasom vaccin |
| US6090406A (en) | 1984-04-12 | 2000-07-18 | The Liposome Company, Inc. | Potentiation of immune responses with liposomal adjuvants |
| US5916588A (en) | 1984-04-12 | 1999-06-29 | The Liposome Company, Inc. | Peptide-containing liposomes, immunogenic liposomes and methods of preparation and use |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US5057540A (en) | 1987-05-29 | 1991-10-15 | Cambridge Biotech Corporation | Saponin adjuvant |
| NZ241926A (en) | 1988-08-25 | 1993-08-26 | Liposome Co Inc | Immunisation dosage form comprising a salt of an organic acid derivative of a sterol and an antigen |
| DE3841091A1 (de) | 1988-12-07 | 1990-06-13 | Behringwerke Ag | Synthetische antigene, verfahren zu ihrer herstellung und ihre verwendung |
| EP0378881B1 (en) | 1989-01-17 | 1993-06-09 | ENIRICERCHE S.p.A. | Synthetic peptides and their use as universal carriers for the preparation of immunogenic conjugates suitable for the development of synthetic vaccines |
| HU212924B (en) | 1989-05-25 | 1996-12-30 | Chiron Corp | Adjuvant formulation comprising a submicron oil droplet emulsion |
| WO1991001146A1 (en) | 1989-07-14 | 1991-02-07 | Praxis Biologics, Inc. | Cytokine and hormone carriers for conjugate vaccines |
| IT1237764B (it) | 1989-11-10 | 1993-06-17 | Eniricerche Spa | Peptidi sintetici utili come carriers universali per la preparazione di coniugati immunogenici e loro impiego per lo sviluppo di vaccini sintetici. |
| IL98715A0 (en) | 1990-08-13 | 1992-07-15 | American Cyanamid Co | Filamentous hemaglutinin of bodetella pertussis as a carrier molecule for conjugate vaccines |
| IT1262896B (it) | 1992-03-06 | 1996-07-22 | Composti coniugati formati da proteine heat shock (hsp) e oligo-poli- saccaridi, loro uso per la produzione di vaccini. | |
| DK0671948T3 (da) | 1992-06-25 | 1997-09-01 | Smithkline Beecham Biolog | Vaccinepræparat indeholdende adjuvanser |
| IL102687A (en) | 1992-07-30 | 1997-06-10 | Yeda Res & Dev | Conjugates of poorly immunogenic antigens and synthetic pepide carriers and vaccines comprising them |
| ATE157882T1 (de) | 1993-03-23 | 1997-09-15 | Smithkline Beecham Biolog | 3-0-deazylierte monophosphoryl lipid a enthaltende impfstoff-zusammensetzungen |
| NZ275772A (en) * | 1993-11-08 | 1998-04-27 | Connaught Lab | Haemophilus transferrin receptor genes and proteins including production and use |
| GB9326174D0 (en) | 1993-12-22 | 1994-02-23 | Biocine Sclavo | Mucosal adjuvant |
| GB9326253D0 (en) | 1993-12-23 | 1994-02-23 | Smithkline Beecham Biolog | Vaccines |
| US6207646B1 (en) | 1994-07-15 | 2001-03-27 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules |
| US6429199B1 (en) | 1994-07-15 | 2002-08-06 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules for activating dendritic cells |
| US6239116B1 (en) | 1994-07-15 | 2001-05-29 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules |
| US6245337B1 (en) * | 1994-08-25 | 2001-06-12 | Washington University | Haemophilus adherence and penetration proteins |
| AUPM873294A0 (en) | 1994-10-12 | 1994-11-03 | Csl Limited | Saponin preparations and use thereof in iscoms |
| UA56132C2 (uk) | 1995-04-25 | 2003-05-15 | Смітклайн Бічем Байолоджікалс С.А. | Композиція вакцини (варіанти), спосіб стабілізації qs21 відносно гідролізу (варіанти), спосіб приготування композиції вакцини |
| GB9513261D0 (en) | 1995-06-29 | 1995-09-06 | Smithkline Beecham Biolog | Vaccines |
| US5707829A (en) | 1995-08-11 | 1998-01-13 | Genetics Institute, Inc. | DNA sequences and secreted proteins encoded thereby |
| AU753688B2 (en) | 1997-03-10 | 2002-10-24 | Ottawa Civic Loeb Research Institute | Use of nucleic acids containing unmethylated CpG dinucleotide as an adjuvant |
| US6818222B1 (en) | 1997-03-21 | 2004-11-16 | Chiron Corporation | Detoxified mutants of bacterial ADP-ribosylating toxins as parenteral adjuvants |
| GB9712347D0 (en) | 1997-06-14 | 1997-08-13 | Smithkline Beecham Biolog | Vaccine |
| GB9713156D0 (en) | 1997-06-20 | 1997-08-27 | Microbiological Res Authority | Vaccines |
| ES2298316T3 (es) | 1997-09-05 | 2008-05-16 | Glaxosmithkline Biologicals S.A. | Emulsiones de aceite en agua que contienen saponinas. |
| GB9725084D0 (en) | 1997-11-28 | 1998-01-28 | Medeva Europ Ltd | Vaccine compositions |
| IL137809A0 (en) | 1998-02-12 | 2001-10-31 | American Cyanamid Co | Pneumococcal and meningococcal vaccines formulated with interleukin-12 |
| US6303114B1 (en) | 1998-03-05 | 2001-10-16 | The Medical College Of Ohio | IL-12 enhancement of immune responses to T-independent antigens |
| IL138000A0 (en) | 1998-04-09 | 2001-10-31 | Smithkline Beecham Biolog | Adjuvant compositions |
| US6562798B1 (en) | 1998-06-05 | 2003-05-13 | Dynavax Technologies Corp. | Immunostimulatory oligonucleotides with modified bases and methods of use thereof |
| GB9817052D0 (en) | 1998-08-05 | 1998-09-30 | Smithkline Beecham Biolog | Vaccine |
| DE69935606T9 (de) | 1998-10-16 | 2021-03-11 | Glaxosmithkline Biologicals S.A. | Adjuvanzsysteme und impfstoffe |
| ES2275499T3 (es) | 1999-03-19 | 2007-06-16 | Glaxosmithkline Biologicals S.A. | Vacuna contra streptococcus pneumoniae. |
| WO2000061761A2 (en) | 1999-04-09 | 2000-10-19 | Techlab, Inc. | Recombinant clostridium toxin a protein carrier for polysaccharide conjugate vaccines |
| KR20020048942A (ko) | 1999-09-24 | 2002-06-24 | 장 스테판느 | 폴리옥시에틸렌 알킬 에테르 또는 에스테르 및 하나이상의 비이온성 계면활성제를 포함하는 애쥬번트 |
| CZ20021043A3 (cs) | 1999-09-24 | 2002-08-14 | Smithkline Beecham Biologicals S. A. | Pouľití kombinace polyoxyethylensorbitanového esteru a oktoxynolu pro výrobu pomocného prostředku |
| EP1311288A1 (en) | 2000-01-20 | 2003-05-21 | Ottawa Health Research Institute | Immunostimulatory nucleic acids for inducing a th2 immune response |
| GB0007432D0 (en) | 2000-03-27 | 2000-05-17 | Microbiological Res Authority | Proteins for use as carriers in conjugate vaccines |
| AU9475001A (en) | 2000-09-26 | 2002-04-08 | Hybridon Inc | Modulation of immunostimulatory activity of immunostimulatory oligonucleotide analogs by positional chemical changes |
| EP2088197B8 (en) | 2000-10-02 | 2016-07-20 | ID Biomedical Corporation of Quebec | Haemophilus influenzae antigens and corresponding DNA fragments |
| GB0026002D0 (en) * | 2000-10-24 | 2000-12-13 | Smithkline Beecham Biolog | Novel compounds |
| DK1328543T3 (da) | 2000-10-27 | 2009-11-23 | Novartis Vaccines & Diagnostic | Nukleinsyrer og proteiner fra streptococcus-gruppe A & B |
| GB0115176D0 (en) | 2001-06-20 | 2001-08-15 | Chiron Spa | Capular polysaccharide solubilisation and combination vaccines |
| CA2452720C (en) | 2001-07-26 | 2012-04-17 | Chiron S.R.L. | Vaccines comprising aluminium adjuvants and histidine |
| AU2002339224B2 (en) | 2001-09-14 | 2008-10-09 | Kuros Us Llc | Packaging of immunostimulatory substances into virus-like particles: method of preparation and use |
| JP4360906B2 (ja) | 2001-09-14 | 2009-11-11 | サイトス バイオテクノロジー アーゲー | ウィルス様粒子によって誘導される免疫応答を高めるための、抗原提示細胞のインビボでの活性化 |
| WO2003035836A2 (en) | 2001-10-24 | 2003-05-01 | Hybridon Inc. | Modulation of immunostimulatory properties of oligonucleotide-based compounds by optimal presentation of 5' ends |
| GB0200025D0 (en) * | 2002-01-02 | 2002-02-13 | Glaxosmithkline Biolog Sa | Novel compounds |
| AU2003222249A1 (en) * | 2002-03-04 | 2003-09-22 | Fidelity Systems, Inc., Et Al. | The complete genome and protein sequence of the hyperthermophile methanopyrus kandleri av19 and monophyly of archael methanogens and methods of use thereof |
| WO2006138527A2 (en) | 2005-06-16 | 2006-12-28 | Children's Hospital, Inc. | Genes of an otitis media isolate of nontypeable haemophilus influenzae |
| GB0410866D0 (en) | 2004-05-14 | 2004-06-16 | Chiron Srl | Haemophilius influenzae |
| AU2007206114B2 (en) | 2006-01-17 | 2013-01-24 | Arne Forsgren | A novel surface exposed Haemophilus influenzae protein (protein E; pE) |
| AT507928B1 (de) | 2008-06-30 | 2015-09-15 | Coil Holding Gmbh | Drosselspule für elektrische energieversorgungsnetze mit reduzierten schallemissionen |
| US9018858B2 (en) | 2008-09-24 | 2015-04-28 | B/E Aerospace, Inc. | Calibration method for LED lighting systems |
-
2004
- 2004-05-14 GB GBGB0410866.8A patent/GB0410866D0/en not_active Ceased
-
2005
- 2005-05-16 WO PCT/IB2005/001775 patent/WO2005111066A2/en not_active Ceased
- 2005-05-16 EP EP10190386A patent/EP2341069A1/en not_active Withdrawn
- 2005-05-16 IN IN290KON2015 patent/IN2015KN00290A/en unknown
- 2005-05-16 EP EP05748150A patent/EP1745067A2/en not_active Withdrawn
- 2005-05-16 CN CNA2005800238288A patent/CN1997663A/zh active Pending
- 2005-05-16 BR BRPI0511118-8A patent/BRPI0511118A/pt not_active Application Discontinuation
- 2005-05-16 EP EP10190381A patent/EP2351773A1/en not_active Withdrawn
- 2005-05-16 EP EP10190390A patent/EP2351774A1/en not_active Withdrawn
- 2005-05-16 EP EP10194789A patent/EP2343313A1/en not_active Withdrawn
- 2005-05-16 JP JP2007512595A patent/JP2008506364A/ja not_active Withdrawn
- 2005-05-16 CA CA002566632A patent/CA2566632A1/en not_active Abandoned
- 2005-05-16 US US11/596,557 patent/US7749518B2/en not_active Expired - Fee Related
- 2005-05-16 RU RU2006144093/10A patent/RU2432357C2/ru not_active IP Right Cessation
-
2010
- 2010-05-25 US US12/800,898 patent/US8124098B2/en not_active Expired - Fee Related
-
2011
- 2011-07-29 JP JP2011166505A patent/JP2012000112A/ja active Pending
-
2012
- 2012-01-24 US US13/357,394 patent/US20120148615A1/en not_active Abandoned
-
2014
- 2014-04-29 US US14/264,972 patent/US9102729B2/en not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002083723A2 (en) * | 2001-04-12 | 2002-10-24 | Glaxosmithkline Biologicals Sa | Polypeptides from h. influenzae homologous to a surface-exposed protein of neisseria meningitidis |
| JP2006519605A (ja) * | 2003-03-06 | 2006-08-31 | チルドレンズ ホスピタル， インコーポレイテッド | 類型不能ｈａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅの中耳炎単離株の遺伝子 |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2015515486A (ja) * | 2012-04-26 | 2015-05-28 | ノバルティス アーゲー | 抗原および抗原の組み合わせ |
Also Published As
| Publication number | Publication date |
|---|---|
| US8124098B2 (en) | 2012-02-28 |
| US7749518B2 (en) | 2010-07-06 |
| WO2005111066A3 (en) | 2006-05-26 |
| EP2343313A1 (en) | 2011-07-13 |
| EP2341069A1 (en) | 2011-07-06 |
| CA2566632A1 (en) | 2005-11-24 |
| US20140234363A1 (en) | 2014-08-21 |
| GB0410866D0 (en) | 2004-06-16 |
| EP2351774A1 (en) | 2011-08-03 |
| IN2015KN00290A (https=) | 2015-06-12 |
| BRPI0511118A (pt) | 2007-11-27 |
| EP1745067A2 (en) | 2007-01-24 |
| WO2005111066A2 (en) | 2005-11-24 |
| US20120148615A1 (en) | 2012-06-14 |
| RU2006144093A (ru) | 2008-06-20 |
| WO2005111066A8 (en) | 2007-05-18 |
| EP2351773A1 (en) | 2011-08-03 |
| RU2432357C2 (ru) | 2011-10-27 |
| US9102729B2 (en) | 2015-08-11 |
| JP2012000112A (ja) | 2012-01-05 |
| CN1997663A (zh) | 2007-07-11 |
| US20080267966A1 (en) | 2008-10-30 |
| US20100303822A1 (en) | 2010-12-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2008506364A (ja) | 型分類不能なＨａｅｍｏｐｈｉｌｕｓｉｎｆｌｕｅｎｚａｅ由来のポリペプチド | |
| RU2450019C2 (ru) | Полипептиды из neisseria meningitidis | |
| JP2008538183A (ja) | Ｂ型インフルエンザ菌 | |
| JP5830009B2 (ja) | Ｓｔａｐｈｙｌｏｃｏｃｃｕｓａｕｒｅｕｓに対して免疫化するための組成物 | |
| EP1991565B1 (en) | Shiga toxoid chimeric proteins | |
| US20090104218A1 (en) | Group B Streptococcus | |
| KR102393038B1 (ko) | OspA의 돌연변이체 단편 및 이에 관련된 방법 및 용도 | |
| JP2010500399A (ja) | 尿路病原性大腸菌由来の免疫原 | |
| JP2012501959A (ja) | Ｙｅｒｓｉｎｉａｐｅｓｔｉｓ抗原を含む組成物 | |
| JP2011512152A (ja) | 改善された溶解度を有するＥｓｃｈｅｒｉｃｈｉａｃｏｌｉ免疫原 | |
| JP2012152228A (ja) | 髄膜炎／敗血症に関連する大腸菌由来のタンパク質および核酸 | |
| JP2012502073A (ja) | Ｈ因子結合タンパク質免疫原 | |
| JP2008511306A (ja) | 髄膜炎菌類タンパク質ｎｍｂ１８７０のドメインおよびエピトープ | |
| JP2009515831A (ja) | ペスト菌（Ｙｅｒｓｉｎｉａｐｅｓｔｉｓ）抗原を含む組成物 | |
| JP2009517377A (ja) | 髄膜炎菌のｎｍｂ１８７０のキメラ、ハイブリッドおよびタンデムポリペプチド | |
| JP2013520487A (ja) | 免疫原性タンパク質および組成物 | |
| JP2015227376A (ja) | 肺炎球菌ＲｒｇＢクレイドの組み合わせ | |
| JP2012532626A (ja) | 無毒化されたＥｓｃｈｅｒｉｃｈｉａｃｏｌｉ免疫原 | |
| JP6401148B2 (ja) | 抗原および抗原の組み合わせ | |
| JP2007535899A (ja) | ビルレンス関連付着因子 | |
| CN101213205A (zh) | B族链球菌 | |
| ES2362749T3 (es) | Composiciones inmunógenas para streptococcus agalactiae. | |
| JP2013510188A (ja) | 黄色ブドウ球菌に由来する菌血症関連抗原 | |
| CN112912097A (zh) | 免疫原性蛋白和组合物 | |
| WO2007073706A2 (es) | Péptidos miméticos de carbohidratos y su empleo en formulaciones farmacéuticas |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20080407 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20110201 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20110427 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20110510 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110729 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20111004 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20111228 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20120111 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20120130 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20120216 |