CA2684578A1 - Chimeric antigens - Google Patents
Chimeric antigens Download PDFInfo
- Publication number
- CA2684578A1 CA2684578A1 CA002684578A CA2684578A CA2684578A1 CA 2684578 A1 CA2684578 A1 CA 2684578A1 CA 002684578 A CA002684578 A CA 002684578A CA 2684578 A CA2684578 A CA 2684578A CA 2684578 A1 CA2684578 A1 CA 2684578A1
- Authority
- CA
- Canada
- Prior art keywords
- polypeptide
- rsv
- protein
- chimeric
- amino acid
- 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.)
- Abandoned
Links
- 108091007433 antigens Proteins 0.000 title claims abstract description 117
- 102000036639 antigens Human genes 0.000 title claims abstract description 117
- 239000000427 antigen Substances 0.000 title claims abstract description 116
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 307
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 296
- 229920001184 polypeptide Polymers 0.000 claims abstract description 294
- 241000725643 Respiratory syncytial virus Species 0.000 claims abstract description 247
- 102000030782 GTP binding Human genes 0.000 claims abstract description 117
- 108091000058 GTP-Binding Proteins 0.000 claims abstract description 117
- 108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 claims abstract description 97
- 108091006027 G proteins Proteins 0.000 claims abstract description 85
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 68
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 67
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 67
- 238000000034 method Methods 0.000 claims abstract description 53
- 210000004899 c-terminal region Anatomy 0.000 claims abstract description 16
- 235000001014 amino acid Nutrition 0.000 claims description 282
- 229940024606 amino acid Drugs 0.000 claims description 265
- 150000001413 amino acids Chemical class 0.000 claims description 265
- 239000000203 mixture Substances 0.000 claims description 152
- 108090000623 proteins and genes Proteins 0.000 claims description 115
- 102000004169 proteins and genes Human genes 0.000 claims description 115
- 235000018102 proteins Nutrition 0.000 claims description 112
- 230000002163 immunogen Effects 0.000 claims description 90
- 210000004027 cell Anatomy 0.000 claims description 81
- 239000013598 vector Substances 0.000 claims description 65
- 239000002671 adjuvant Substances 0.000 claims description 63
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 54
- 230000004044 response Effects 0.000 claims description 46
- 230000014509 gene expression Effects 0.000 claims description 43
- 230000028993 immune response Effects 0.000 claims description 43
- 238000006467 substitution reaction Methods 0.000 claims description 31
- 108091033319 polynucleotide Proteins 0.000 claims description 30
- 102000040430 polynucleotide Human genes 0.000 claims description 30
- 239000002157 polynucleotide Substances 0.000 claims description 30
- 102000004961 Furin Human genes 0.000 claims description 29
- 108090001126 Furin Proteins 0.000 claims description 29
- 208000015181 infectious disease Diseases 0.000 claims description 24
- 244000052769 pathogen Species 0.000 claims description 24
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 23
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 22
- 239000000872 buffer Substances 0.000 claims description 21
- 229960005486 vaccine Drugs 0.000 claims description 21
- 238000003776 cleavage reaction Methods 0.000 claims description 20
- 238000002360 preparation method Methods 0.000 claims description 20
- 201000010099 disease Diseases 0.000 claims description 19
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 19
- 230000004048 modification Effects 0.000 claims description 19
- 238000012986 modification Methods 0.000 claims description 19
- 230000007017 scission Effects 0.000 claims description 19
- 239000013604 expression vector Substances 0.000 claims description 18
- 108020004705 Codon Proteins 0.000 claims description 16
- 125000000539 amino acid group Chemical group 0.000 claims description 16
- 230000001580 bacterial effect Effects 0.000 claims description 15
- 235000018417 cysteine Nutrition 0.000 claims description 15
- 241000700605 Viruses Species 0.000 claims description 13
- 235000009582 asparagine Nutrition 0.000 claims description 13
- 125000000613 asparagine group Chemical class N[C@@H](CC(N)=O)C(=O)* 0.000 claims description 13
- 230000003612 virological effect Effects 0.000 claims description 12
- 241000238631 Hexapoda Species 0.000 claims description 11
- 101000669447 Homo sapiens Toll-like receptor 4 Proteins 0.000 claims description 11
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 11
- 102100039360 Toll-like receptor 4 Human genes 0.000 claims description 11
- 230000002209 hydrophobic effect Effects 0.000 claims description 11
- 230000001681 protective effect Effects 0.000 claims description 11
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 9
- 238000012217 deletion Methods 0.000 claims description 9
- 230000037430 deletion Effects 0.000 claims description 9
- 239000007764 o/w emulsion Substances 0.000 claims description 9
- BACYUWVYYTXETD-UHFFFAOYSA-N N-Lauroylsarcosine Chemical compound CCCCCCCCCCCC(=O)N(C)CC(O)=O BACYUWVYYTXETD-UHFFFAOYSA-N 0.000 claims description 8
- 206010061603 Respiratory syncytial virus infection Diseases 0.000 claims description 8
- 235000004279 alanine Nutrition 0.000 claims description 8
- 239000003599 detergent Substances 0.000 claims description 8
- 108700004121 sarkosyl Proteins 0.000 claims description 8
- 210000004962 mammalian cell Anatomy 0.000 claims description 7
- 239000004475 Arginine Substances 0.000 claims description 6
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 6
- 235000009697 arginine Nutrition 0.000 claims description 6
- 239000003446 ligand Substances 0.000 claims description 6
- 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 claims description 6
- 230000001575 pathological effect Effects 0.000 claims description 6
- 229930006000 Sucrose Natural products 0.000 claims description 5
- 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 claims description 5
- 229940037003 alum Drugs 0.000 claims description 5
- 229960000310 isoleucine Drugs 0.000 claims description 5
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 5
- 239000005720 sucrose Substances 0.000 claims description 5
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 4
- 239000000969 carrier Substances 0.000 claims description 4
- 239000003814 drug Substances 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 4
- 230000002708 enhancing effect Effects 0.000 claims description 4
- 206010022000 influenza Diseases 0.000 claims description 4
- 229930182817 methionine Natural products 0.000 claims description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 3
- 238000007496 glass forming Methods 0.000 claims description 3
- 238000007918 intramuscular administration Methods 0.000 claims description 3
- 229920002704 polyhistidine Polymers 0.000 claims description 3
- 229920005862 polyol Polymers 0.000 claims description 3
- 150000003077 polyols Chemical class 0.000 claims description 3
- 230000009467 reduction Effects 0.000 claims description 3
- 239000013638 trimer Substances 0.000 claims description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 2
- 241000991587 Enterovirus C Species 0.000 claims description 2
- 208000002606 Paramyxoviridae Infections Diseases 0.000 claims description 2
- 201000005702 Pertussis Diseases 0.000 claims description 2
- 206010043376 Tetanus Diseases 0.000 claims description 2
- 229960001230 asparagine Drugs 0.000 claims description 2
- 206010013023 diphtheria Diseases 0.000 claims description 2
- 208000002672 hepatitis B Diseases 0.000 claims description 2
- 229920000136 polysorbate Polymers 0.000 claims description 2
- 230000002829 reductive effect Effects 0.000 claims description 2
- 230000002265 prevention Effects 0.000 claims 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims 1
- 102100023206 Neuromodulin Human genes 0.000 claims 1
- 210000005253 yeast cell Anatomy 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 abstract description 21
- 239000008194 pharmaceutical composition Substances 0.000 abstract 1
- 239000002773 nucleotide Substances 0.000 description 151
- 125000003729 nucleotide group Chemical group 0.000 description 136
- 235000014304 histidine Nutrition 0.000 description 36
- 239000000556 agonist Substances 0.000 description 34
- 125000000487 histidyl group Chemical class [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 33
- 239000012634 fragment Substances 0.000 description 27
- 102000002689 Toll-like receptor Human genes 0.000 description 25
- 108020000411 Toll-like receptor Proteins 0.000 description 25
- 238000009472 formulation Methods 0.000 description 23
- 230000001717 pathogenic effect Effects 0.000 description 21
- 230000011664 signaling Effects 0.000 description 19
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 18
- 239000002158 endotoxin Substances 0.000 description 15
- 150000007949 saponins Chemical class 0.000 description 15
- 229920006008 lipopolysaccharide Polymers 0.000 description 14
- 229930182490 saponin Natural products 0.000 description 14
- 235000017709 saponins Nutrition 0.000 description 14
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 13
- 239000004471 Glycine Substances 0.000 description 13
- 241000196324 Embryophyta Species 0.000 description 12
- 239000003795 chemical substances by application Substances 0.000 description 12
- 238000000746 purification Methods 0.000 description 12
- -1 two amino acids Chemical class 0.000 description 12
- 241000588724 Escherichia coli Species 0.000 description 10
- 108091034117 Oligonucleotide Proteins 0.000 description 10
- 239000007983 Tris buffer Substances 0.000 description 10
- 230000000890 antigenic effect Effects 0.000 description 10
- 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 10
- CTMZLDSMFCVUNX-VMIOUTBZSA-N cytidylyl-(3'->5')-guanosine Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@H](O)[C@H](OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=C(C(N=C(N)N3)=O)N=C2)O)[C@@H](CO)O1 CTMZLDSMFCVUNX-VMIOUTBZSA-N 0.000 description 10
- 108020001507 fusion proteins Proteins 0.000 description 10
- 102000037865 fusion proteins Human genes 0.000 description 10
- 230000003308 immunostimulating effect Effects 0.000 description 10
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 10
- GVJHHUAWPYXKBD-IEOSBIPESA-N α-tocopherol Chemical compound OC1=C(C)C(C)=C2O[C@@](CCC[C@H](C)CCC[C@H](C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-IEOSBIPESA-N 0.000 description 10
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 9
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 9
- 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 9
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 9
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 9
- 238000009396 hybridization Methods 0.000 description 9
- 230000003472 neutralizing effect Effects 0.000 description 9
- 230000008569 process Effects 0.000 description 9
- 238000012545 processing Methods 0.000 description 9
- 235000004252 protein component Nutrition 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 8
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 8
- 239000000839 emulsion Substances 0.000 description 8
- 230000004927 fusion Effects 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 238000006386 neutralization reaction Methods 0.000 description 8
- 241000701447 unidentified baculovirus Species 0.000 description 8
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 7
- 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 7
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 7
- 241001465754 Metazoa Species 0.000 description 7
- 108091005461 Nucleic proteins Proteins 0.000 description 7
- 101710116435 Outer membrane protein Proteins 0.000 description 7
- PZBFGYYEXUXCOF-UHFFFAOYSA-N TCEP Chemical compound OC(=O)CCP(CCC(O)=O)CCC(O)=O PZBFGYYEXUXCOF-UHFFFAOYSA-N 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 208000024891 symptom Diseases 0.000 description 7
- 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 6
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 6
- 108010053070 Glutathione Disulfide Proteins 0.000 description 6
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 6
- 206010024971 Lower respiratory tract infections Diseases 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 108010075142 Protollin Proteins 0.000 description 6
- 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 6
- 150000001294 alanine derivatives Chemical class 0.000 description 6
- 238000013320 baculovirus expression vector system Methods 0.000 description 6
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 6
- 150000001875 compounds Chemical class 0.000 description 6
- 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 6
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 231100000252 nontoxic Toxicity 0.000 description 6
- 230000003000 nontoxic effect Effects 0.000 description 6
- 239000002245 particle Substances 0.000 description 6
- 238000004153 renaturation Methods 0.000 description 6
- 229940031439 squalene Drugs 0.000 description 6
- 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 6
- 108091026890 Coding region Proteins 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 108090000288 Glycoproteins Proteins 0.000 description 5
- 102000003886 Glycoproteins Human genes 0.000 description 5
- 241000699670 Mus sp. Species 0.000 description 5
- 108091081024 Start codon Proteins 0.000 description 5
- 238000007792 addition Methods 0.000 description 5
- 229940087168 alpha tocopherol Drugs 0.000 description 5
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 235000012000 cholesterol Nutrition 0.000 description 5
- 229940107161 cholesterol Drugs 0.000 description 5
- 239000003085 diluting agent Substances 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 230000002349 favourable effect Effects 0.000 description 5
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 5
- 210000003000 inclusion body Anatomy 0.000 description 5
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 5
- 229920000053 polysorbate 80 Polymers 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- 230000004224 protection Effects 0.000 description 5
- 229960000984 tocofersolan Drugs 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 239000002076 α-tocopherol Substances 0.000 description 5
- 235000004835 α-tocopherol Nutrition 0.000 description 5
- 241000701022 Cytomegalovirus Species 0.000 description 4
- 241000588653 Neisseria Species 0.000 description 4
- 102000017033 Porins Human genes 0.000 description 4
- 108010013381 Porins Proteins 0.000 description 4
- 230000005867 T cell response Effects 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 229910021502 aluminium hydroxide Inorganic materials 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 210000003719 b-lymphocyte Anatomy 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000004422 calculation algorithm Methods 0.000 description 4
- 238000009295 crossflow filtration Methods 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 4
- 230000002480 immunoprotective effect Effects 0.000 description 4
- 239000002502 liposome Substances 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 230000001323 posttranslational effect Effects 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 238000012552 review Methods 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 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 3
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 3
- 108091035707 Consensus sequence Proteins 0.000 description 3
- 108010024636 Glutathione Proteins 0.000 description 3
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 3
- 229930064664 L-arginine Natural products 0.000 description 3
- 235000014852 L-arginine Nutrition 0.000 description 3
- 108010028921 Lipopeptides Proteins 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- 101100481584 Mus musculus Tlr1 gene Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 108091006629 SLC13A2 Proteins 0.000 description 3
- 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 3
- 108010003533 Viral Envelope Proteins Proteins 0.000 description 3
- UZQJVUCHXGYFLQ-AYDHOLPZSA-N [(2s,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-4-[(2r,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2s,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-6-(hy Chemical compound O([C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1CC[C@]2(C)[C@H]3CC=C4[C@@]([C@@]3(CC[C@H]2[C@@]1(C=O)C)C)(C)CC(O)[C@]1(CCC(CC14)(C)C)C(=O)O[C@H]1[C@@H]([C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O[C@H]4[C@@H]([C@@H](O[C@H]5[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O5)O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO)O2)O)[C@H](O)[C@@H](CO)O1)O)[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O UZQJVUCHXGYFLQ-AYDHOLPZSA-N 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 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 3
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 3
- 159000000013 aluminium salts Chemical class 0.000 description 3
- 229910000329 aluminium sulfate Inorganic materials 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 238000002869 basic local alignment search tool Methods 0.000 description 3
- 239000001506 calcium phosphate Substances 0.000 description 3
- 229910000389 calcium phosphate Inorganic materials 0.000 description 3
- 235000011010 calcium phosphates Nutrition 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 231100000517 death Toxicity 0.000 description 3
- 230000003292 diminished effect Effects 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 230000002538 fungal effect Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 102000005396 glutamine synthetase Human genes 0.000 description 3
- 108020002326 glutamine synthetase Proteins 0.000 description 3
- 229960003180 glutathione Drugs 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 230000002949 hemolytic effect Effects 0.000 description 3
- 125000001165 hydrophobic group Chemical group 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 229960001438 immunostimulant agent Drugs 0.000 description 3
- 239000003022 immunostimulating agent Substances 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 229910052500 inorganic mineral Inorganic materials 0.000 description 3
- 239000007927 intramuscular injection Substances 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 239000011707 mineral Substances 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 229920001542 oligosaccharide Polymers 0.000 description 3
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 210000001236 prokaryotic cell Anatomy 0.000 description 3
- 238000001742 protein purification Methods 0.000 description 3
- 230000000601 reactogenic effect Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 239000012465 retentate Substances 0.000 description 3
- 238000002864 sequence alignment Methods 0.000 description 3
- 238000001542 size-exclusion chromatography Methods 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 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 3
- 210000002845 virion Anatomy 0.000 description 3
- DFUSDJMZWQVQSF-XLGIIRLISA-N (2r)-2-methyl-2-[(4r,8r)-4,8,12-trimethyltridecyl]-3,4-dihydrochromen-6-ol Chemical compound OC1=CC=C2O[C@@](CCC[C@H](C)CCC[C@H](C)CCCC(C)C)(C)CCC2=C1 DFUSDJMZWQVQSF-XLGIIRLISA-N 0.000 description 2
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 2
- 241000201370 Autographa californica nucleopolyhedrovirus Species 0.000 description 2
- 206010006448 Bronchiolitis Diseases 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 241000701867 Enterobacteria phage T7 Species 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- 229920002683 Glycosaminoglycan Polymers 0.000 description 2
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 2
- 108010004889 Heat-Shock Proteins Proteins 0.000 description 2
- 101000831567 Homo sapiens Toll-like receptor 2 Proteins 0.000 description 2
- 101000669402 Homo sapiens Toll-like receptor 7 Proteins 0.000 description 2
- 241000711920 Human orthopneumovirus Species 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- 108090000978 Interleukin-4 Proteins 0.000 description 2
- 108010002616 Interleukin-5 Proteins 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 241001092142 Molina Species 0.000 description 2
- 108090001074 Nucleocapsid Proteins Proteins 0.000 description 2
- 206010035664 Pneumonia Diseases 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 101710182846 Polyhedrin Proteins 0.000 description 2
- 241001454523 Quillaja saponaria Species 0.000 description 2
- 235000009001 Quillaja saponaria Nutrition 0.000 description 2
- 229940124679 RSV vaccine Drugs 0.000 description 2
- 102100029557 Ras-related protein Rab-40B Human genes 0.000 description 2
- 206010057190 Respiratory tract infections Diseases 0.000 description 2
- 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 2
- 229940124614 TLR 8 agonist Drugs 0.000 description 2
- 102100024333 Toll-like receptor 2 Human genes 0.000 description 2
- 102100039390 Toll-like receptor 7 Human genes 0.000 description 2
- 241000255993 Trichoplusia ni Species 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 108020005202 Viral DNA Proteins 0.000 description 2
- 108010059722 Viral Fusion Proteins Proteins 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- 229940001007 aluminium phosphate Drugs 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 239000008365 aqueous carrier Substances 0.000 description 2
- 102000005936 beta-Galactosidase Human genes 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- NAGJZTKCGNOGPW-UHFFFAOYSA-K dioxido-sulfanylidene-sulfido-$l^{5}-phosphane Chemical group [O-]P([O-])([S-])=S NAGJZTKCGNOGPW-UHFFFAOYSA-K 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000003995 emulsifying agent Substances 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 210000002443 helper t lymphocyte Anatomy 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 230000005745 host immune response Effects 0.000 description 2
- 229940124669 imidazoquinoline Drugs 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 230000029226 lipidation Effects 0.000 description 2
- 239000012160 loading buffer Substances 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 210000004779 membrane envelope Anatomy 0.000 description 2
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 2
- BSOQXXWZTUDTEL-ZUYCGGNHSA-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)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 2
- 210000003463 organelle Anatomy 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000000069 prophylactic effect Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- BXNMTOQRYBFHNZ-UHFFFAOYSA-N resiquimod Chemical compound C1=CC=CC2=C(N(C(COCC)=N3)CC(C)(C)O)C3=C(N)N=C21 BXNMTOQRYBFHNZ-UHFFFAOYSA-N 0.000 description 2
- 230000000241 respiratory effect Effects 0.000 description 2
- 210000002345 respiratory system Anatomy 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000011537 solubilization buffer Substances 0.000 description 2
- 230000003381 solubilizing effect Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000014621 translational initiation Effects 0.000 description 2
- 108010087967 type I signal peptidase Proteins 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 230000007501 viral attachment Effects 0.000 description 2
- 230000029812 viral genome replication Effects 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- PSBDWGZCVUAZQS-UHFFFAOYSA-N (dimethylsulfonio)acetate Chemical compound C[S+](C)CC([O-])=O PSBDWGZCVUAZQS-UHFFFAOYSA-N 0.000 description 1
- HTSGKJQDMSTCGS-UHFFFAOYSA-N 1,4-bis(4-chlorophenyl)-2-(4-methylphenyl)sulfonylbutane-1,4-dione Chemical compound C1=CC(C)=CC=C1S(=O)(=O)C(C(=O)C=1C=CC(Cl)=CC=1)CC(=O)C1=CC=C(Cl)C=C1 HTSGKJQDMSTCGS-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- LBCZOTMMGHGTPH-UHFFFAOYSA-N 2-[2-[4-(2,4,4-trimethylpentan-2-yl)phenoxy]ethoxy]ethanol Chemical compound CC(C)(C)CC(C)(C)C1=CC=C(OCCOCCO)C=C1 LBCZOTMMGHGTPH-UHFFFAOYSA-N 0.000 description 1
- VDCRFBBZFHHYGT-IOSLPCCCSA-N 2-amino-9-[(2r,3r,4s,5r)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-7-prop-2-enyl-3h-purine-6,8-dione Chemical compound O=C1N(CC=C)C=2C(=O)NC(N)=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O VDCRFBBZFHHYGT-IOSLPCCCSA-N 0.000 description 1
- ASJSAQIRZKANQN-CRCLSJGQSA-N 2-deoxy-D-ribose Chemical group OC[C@@H](O)[C@@H](O)CC=O ASJSAQIRZKANQN-CRCLSJGQSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- WKALLSVICJPZTM-UHFFFAOYSA-N 3-[decyl(dimethyl)azaniumyl]propane-1-sulfonate Chemical compound CCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O WKALLSVICJPZTM-UHFFFAOYSA-N 0.000 description 1
- QZRAABPTWGFNIU-UHFFFAOYSA-N 3-[dimethyl(octyl)azaniumyl]propane-1-sulfonate Chemical compound CCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O QZRAABPTWGFNIU-UHFFFAOYSA-N 0.000 description 1
- TUBRCQBRKJXJEA-UHFFFAOYSA-N 3-[hexadecyl(dimethyl)azaniumyl]propane-1-sulfonate Chemical compound CCCCCCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O TUBRCQBRKJXJEA-UHFFFAOYSA-N 0.000 description 1
- 108010025188 Alcohol oxidase Proteins 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
- 108091008875 B cell receptors Proteins 0.000 description 1
- 108020000946 Bacterial DNA Proteins 0.000 description 1
- 241000589968 Borrelia Species 0.000 description 1
- 102000004298 CX3C Chemokine Receptor 1 Human genes 0.000 description 1
- 108090000835 CX3C Chemokine Receptor 1 Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical group [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical compound [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 241000251204 Chimaeridae Species 0.000 description 1
- 201000006306 Cor pulmonale Diseases 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 241000195493 Cryptophyta Species 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 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
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 206010014950 Eosinophilia Diseases 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 101000738180 Euglena gracilis Chaperonin CPN60, mitochondrial Proteins 0.000 description 1
- 108091092566 Extrachromosomal DNA Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108010040721 Flagellin Proteins 0.000 description 1
- 241000700662 Fowlpox virus Species 0.000 description 1
- 241000233866 Fungi Species 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
- 229930186217 Glycolipid Natural products 0.000 description 1
- NYHBQMYGNKIUIF-UUOKFMHZSA-N Guanosine Chemical group 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 1
- 241001316290 Gypsophila Species 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 101710113864 Heat shock protein 90 Proteins 0.000 description 1
- 102100034051 Heat shock protein HSP 90-alpha Human genes 0.000 description 1
- 229920002971 Heparan sulfate Polymers 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000831496 Homo sapiens Toll-like receptor 3 Proteins 0.000 description 1
- 101000669406 Homo sapiens Toll-like receptor 6 Proteins 0.000 description 1
- 101000800483 Homo sapiens Toll-like receptor 8 Proteins 0.000 description 1
- 206010022004 Influenza like illness Diseases 0.000 description 1
- 108020005350 Initiator Codon Proteins 0.000 description 1
- 108090000176 Interleukin-13 Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-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
- 244000147568 Laurus nobilis Species 0.000 description 1
- 235000017858 Laurus nobilis Nutrition 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 208000016604 Lyme disease Diseases 0.000 description 1
- 102000043131 MHC class II family Human genes 0.000 description 1
- 108091054438 MHC class II family Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 201000005505 Measles Diseases 0.000 description 1
- 108010036176 Melitten Proteins 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 108010084333 N-palmitoyl-S-(2,3-bis(palmitoyloxy)propyl)cysteinyl-seryl-lysyl-lysyl-lysyl-lysine Proteins 0.000 description 1
- 241000588650 Neisseria meningitidis Species 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 241000221961 Neurospora crassa Species 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 235000010676 Ocimum basilicum Nutrition 0.000 description 1
- 240000007926 Ocimum gratissimum Species 0.000 description 1
- 108700006640 OspA Proteins 0.000 description 1
- 208000005141 Otitis Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000711504 Paramyxoviridae Species 0.000 description 1
- 108010013639 Peptidoglycan Proteins 0.000 description 1
- 241000711904 Pneumoviridae Species 0.000 description 1
- 241000711902 Pneumovirus Species 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 206010036590 Premature baby Diseases 0.000 description 1
- 101710118538 Protease Proteins 0.000 description 1
- 102000007615 Pulmonary Surfactant-Associated Protein A Human genes 0.000 description 1
- 108010007100 Pulmonary Surfactant-Associated Protein A Proteins 0.000 description 1
- 231100000645 Reed–Muench method Toxicity 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 241000219287 Saponaria Species 0.000 description 1
- 108010077895 Sarcosine Proteins 0.000 description 1
- 108091058545 Secretory proteins Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 241000144290 Sigmodon hispidus Species 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 241000256248 Spodoptera Species 0.000 description 1
- 241000256251 Spodoptera frugiperda Species 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 229940124615 TLR 7 agonist Drugs 0.000 description 1
- 235000005212 Terminalia tomentosa Nutrition 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 108010060818 Toll-Like Receptor 9 Proteins 0.000 description 1
- 102100024324 Toll-like receptor 3 Human genes 0.000 description 1
- 102100039387 Toll-like receptor 6 Human genes 0.000 description 1
- 102100033110 Toll-like receptor 8 Human genes 0.000 description 1
- 102100033117 Toll-like receptor 9 Human genes 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
- BHATUINFZWUDIX-UHFFFAOYSA-N Zwittergent 3-14 Chemical compound CCCCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O BHATUINFZWUDIX-UHFFFAOYSA-N 0.000 description 1
- 229920000392 Zymosan Polymers 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000000787 affinity precipitation Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 239000004411 aluminium Substances 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 230000001668 ameliorated effect Effects 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 108010088716 attachment protein G Proteins 0.000 description 1
- 210000001224 bacterial fimbriae Anatomy 0.000 description 1
- 239000003855 balanced salt solution Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000021523 carboxylation Effects 0.000 description 1
- 238000006473 carboxylation reaction Methods 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- SQQXRXKYTKFFSM-UHFFFAOYSA-N chembl1992147 Chemical compound OC1=C(OC)C(OC)=CC=C1C1=C(C)C(C(O)=O)=NC(C=2N=C3C4=NC(C)(C)N=C4C(OC)=C(O)C3=CC=2)=C1N SQQXRXKYTKFFSM-UHFFFAOYSA-N 0.000 description 1
- 208000029771 childhood onset asthma Diseases 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000007398 colorimetric assay Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical class NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000011026 diafiltration Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 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
- 238000009826 distribution Methods 0.000 description 1
- 208000019258 ear infection Diseases 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 239000006274 endogenous ligand Substances 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- NLFBCYMMUAKCPC-KQQUZDAGSA-N ethyl (e)-3-[3-amino-2-cyano-1-[(e)-3-ethoxy-3-oxoprop-1-enyl]sulfanyl-3-oxoprop-1-enyl]sulfanylprop-2-enoate Chemical compound CCOC(=O)\C=C\SC(=C(C#N)C(N)=O)S\C=C\C(=O)OCC NLFBCYMMUAKCPC-KQQUZDAGSA-N 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000006277 exogenous ligand Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960002442 glucosamine Drugs 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical class O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229940099552 hyaluronan Drugs 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 229960002751 imiquimod Drugs 0.000 description 1
- DOUYETYNHWVLEO-UHFFFAOYSA-N imiquimod Chemical group C1=CC=CC2=C3N(CC(C)C)C=NC3=C(N)N=C21 DOUYETYNHWVLEO-UHFFFAOYSA-N 0.000 description 1
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 230000002134 immunopathologic effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
- 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 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 125000000400 lauroyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- IZWSFJTYBVKZNK-UHFFFAOYSA-N lauryl sulfobetaine Chemical compound CCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O IZWSFJTYBVKZNK-UHFFFAOYSA-N 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229950005634 loxoribine Drugs 0.000 description 1
- 239000007937 lozenge Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- VDXZNPDIRNWWCW-JFTDCZMZSA-N melittin Chemical group NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(N)=O)CC1=CNC2=CC=CC=C12 VDXZNPDIRNWWCW-JFTDCZMZSA-N 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- DVEKCXOJTLDBFE-UHFFFAOYSA-N n-dodecyl-n,n-dimethylglycinate Chemical compound CCCCCCCCCCCC[N+](C)(C)CC([O-])=O DVEKCXOJTLDBFE-UHFFFAOYSA-N 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- HEGSGKPQLMEBJL-RKQHYHRCSA-N octyl beta-D-glucopyranoside Chemical compound CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RKQHYHRCSA-N 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 229960000402 palivizumab Drugs 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 150000004713 phosphodiesters Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 230000007505 plaque formation Effects 0.000 description 1
- 238000002962 plaque-reduction assay Methods 0.000 description 1
- 229940115272 polyinosinic:polycytidylic acid Drugs 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
- 229940068968 polysorbate 80 Drugs 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 229940021993 prophylactic vaccine Drugs 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 238000001814 protein method Methods 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 208000009305 pseudorabies Diseases 0.000 description 1
- 201000009732 pulmonary eosinophilia Diseases 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 229940044601 receptor agonist Drugs 0.000 description 1
- 239000000018 receptor agonist Substances 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 229950010550 resiquimod Drugs 0.000 description 1
- 210000003660 reticulum Anatomy 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 206010039083 rhinitis Diseases 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 102200123930 rs121908143 Human genes 0.000 description 1
- 102220005324 rs34703513 Human genes 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 238000013515 script Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 101150091813 shfl gene Proteins 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- FHHPUSMSKHSNKW-SMOYURAASA-M sodium deoxycholate Chemical compound [Na+].C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 FHHPUSMSKHSNKW-SMOYURAASA-M 0.000 description 1
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000008247 solid mixture Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000010473 stable expression Effects 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L sulfate group Chemical group S(=O)(=O)([O-])[O-] QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 229940117986 sulfobetaine Drugs 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229940021747 therapeutic vaccine Drugs 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
- 238000012090 tissue culture technique Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 229940044616 toll-like receptor 7 agonist Drugs 0.000 description 1
- 229940044655 toll-like receptor 9 agonist Drugs 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 229940093609 tricaprylin Drugs 0.000 description 1
- UYPYRKYUKCHHIB-UHFFFAOYSA-N trimethylamine N-oxide Chemical compound C[N+](C)(C)[O-] UYPYRKYUKCHHIB-UHFFFAOYSA-N 0.000 description 1
- VLPFTAMPNXLGLX-UHFFFAOYSA-N trioctanoin Chemical compound CCCCCCCC(=O)OCC(OC(=O)CCCCCCC)COC(=O)CCCCCCC VLPFTAMPNXLGLX-UHFFFAOYSA-N 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 229940045136 urea Drugs 0.000 description 1
- 239000012646 vaccine adjuvant Substances 0.000 description 1
- 229940124931 vaccine adjuvant Drugs 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 230000007923 virulence factor Effects 0.000 description 1
- 239000000304 virulence factor Substances 0.000 description 1
- 230000036266 weeks of gestation Effects 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
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1027—Paramyxoviridae, e.g. respiratory syncytial virus
-
- 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
- A61K39/12—Viral antigens
-
- 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
- A61K39/12—Viral antigens
- A61K39/155—Paramyxoviridae, e.g. parainfluenza virus
-
- 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
-
- 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
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- 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
- A61K2039/54—Medicinal preparations containing antigens or antibodies characterised by the route of administration
-
- 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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55566—Emulsions, e.g. Freund's adjuvant, MF59
-
- 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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/55572—Lipopolysaccharides; Lipid A; Monophosphoryl lipid A
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- 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
- C12N2760/18011—Paramyxoviridae
- C12N2760/18511—Pneumovirus, e.g. human respiratory syncytial virus
- C12N2760/18522—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
- C12N2760/18011—Paramyxoviridae
- C12N2760/18511—Pneumovirus, e.g. human respiratory syncytial virus
- C12N2760/18534—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Pulmonology (AREA)
- Mycology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Gastroenterology & Hepatology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicinal Preparation (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US89620107P | 2007-03-21 | 2007-03-21 | |
| US60/896,201 | 2007-03-21 | ||
| PCT/IB2008/001286 WO2008114149A2 (en) | 2007-03-21 | 2008-03-20 | Chimeric antigens |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2684578A1 true CA2684578A1 (en) | 2008-09-25 |
Family
ID=39766560
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002684578A Abandoned CA2684578A1 (en) | 2007-03-21 | 2008-03-20 | Chimeric antigens |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US20100203071A1 (enExample) |
| EP (1) | EP2181121A4 (enExample) |
| JP (1) | JP2010522540A (enExample) |
| CA (1) | CA2684578A1 (enExample) |
| WO (1) | WO2008114149A2 (enExample) |
Families Citing this family (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20160000902A1 (en) * | 2003-07-11 | 2016-01-07 | Novavax, Inc. | Combination vaccine for respiratory syncytial virus and influenza |
| DK2347775T3 (da) | 2005-12-13 | 2020-07-13 | Harvard College | Skabeloner til celletransplantation |
| WO2009002401A2 (en) | 2007-06-21 | 2008-12-31 | President And Fellows Of Harvard College | Scaffolds for cell collection or elimination |
| WO2009079796A1 (en) | 2007-12-24 | 2009-07-02 | Id Biomedical Corporation Of Quebec | Recombinant rsv antigens |
| US10328133B2 (en) | 2008-02-13 | 2019-06-25 | President And Fellows Of Harvard College | Continuous cell programming devices |
| US9370558B2 (en) | 2008-02-13 | 2016-06-21 | President And Fellows Of Harvard College | Controlled delivery of TLR agonists in structural polymeric devices |
| US11446374B2 (en) | 2008-12-09 | 2022-09-20 | Novavax, Inc. | Modified RSV F proteins and methods of their use |
| PL3067064T3 (pl) * | 2008-12-09 | 2020-11-02 | Novavax, Inc. | Zmodyfikowane białka f rsv i sposoby ich wykorzystania |
| WO2010149743A2 (en) | 2009-06-24 | 2010-12-29 | Id Biomedical Corporation Of Quebec | Vaccine |
| AU2010264688A1 (en) | 2009-06-24 | 2012-01-19 | Glaxosmithkline Biologicals S.A. | Recombinant RSV antigens |
| SI3178490T1 (sl) | 2009-07-15 | 2022-08-31 | Glaxosmithkline Biologicals S.A. | Sestavki proteina F RSV-ja in postopki za pripravo le-teh |
| CN103977394B (zh) * | 2009-07-17 | 2016-03-09 | 翰林大学校产学协力团 | 包含脂质体包胶的寡核苷酸和表位的免疫刺激性组合物 |
| WO2011014871A1 (en) | 2009-07-31 | 2011-02-03 | President And Fellows Of Harvard College | Programming of cells for tolerogenic therapies |
| US8846056B2 (en) * | 2009-08-04 | 2014-09-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, Centers For Disease Control | Anti-RSV immunogens and methods of immunization |
| EP2590675B1 (en) | 2010-07-07 | 2018-08-29 | Artificial Cell Technologies, Inc. | Respiratory syncytial virus antigenic compositions and methods |
| CN107648668B (zh) | 2010-10-06 | 2021-06-18 | 哈佛学院董事会 | 用于基于材料的细胞疗法的可注射的成孔水凝胶 |
| US20140024076A1 (en) * | 2011-01-28 | 2014-01-23 | Medimmune, Llc. | Expression Of Soluble Viral Fusion Glycoproteins In Mammalian Cells |
| EA034702B1 (ru) * | 2011-04-26 | 2020-03-10 | Молекулар Экспресс, Инк. | Липосомные композиции |
| WO2012149358A1 (en) | 2011-04-28 | 2012-11-01 | President And Fellows Of Harvard College | Injectable preformed macroscopic 3-dimensional scaffolds for minimally invasive administration |
| US9675561B2 (en) | 2011-04-28 | 2017-06-13 | President And Fellows Of Harvard College | Injectable cryogel vaccine devices and methods of use thereof |
| SI3275892T1 (sl) | 2011-05-13 | 2020-06-30 | Glaxosmithkline Biologicals S.A. | Prefuzijski RSV F antigeni |
| AU2012261848B2 (en) | 2011-06-03 | 2017-06-15 | President And Fellows Of Harvard College | In situ antigen-generating cancer vaccine |
| ES2395677B1 (es) * | 2011-07-29 | 2013-12-26 | Instituto De Salud Carlos Iii | Proteína F del VRSH en conformación pre-fusión estabilizada y anticuerpos neutralizantes específicos frente a la misma. |
| EP2752199A4 (en) | 2011-08-29 | 2015-04-29 | Univ Tokushima | RSV MUCOSA VACCINE |
| CA2849471A1 (en) * | 2011-09-30 | 2013-04-04 | Novavax, Inc. | Recombinant nanoparticle rsv f vaccine for respiratory syncytial virus |
| EP3511337A1 (en) * | 2012-04-10 | 2019-07-17 | The Trustees of The University of Pennsylvania | Human respiratory syncytial virus concensus antigens, nucleic acid constructs and vaccines made thereform, and methods of using same |
| CN104244929B (zh) | 2012-04-16 | 2017-04-05 | 哈佛学院董事会 | 用于调节免疫反应的介孔二氧化硅组合物 |
| DK2879702T3 (da) * | 2012-08-01 | 2020-02-24 | Bavarian Nordic As | Rekombinant modificeret vacciniavirus ankara (mva)-vaccine mod respiratorisk syncytialvirus (rsv) |
| WO2014019718A1 (en) | 2012-08-01 | 2014-02-06 | Bavarian Nordic A/S | Recombinant modified vaccinia virus ankara (mva) respiratory syncytial virus (rsv) vaccine |
| JP2015525794A (ja) * | 2012-08-06 | 2015-09-07 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | 乳児においてｒｓｖ及び百日咳菌に対する免疫応答を惹起するための方法 |
| US20140037680A1 (en) * | 2012-08-06 | 2014-02-06 | Glaxosmithkline Biologicals, S.A. | Novel method |
| BR112015019126A2 (pt) * | 2013-02-11 | 2017-08-22 | Novavax Inc | Vacina de combinação para vírus sincicial respiratório e influenza |
| CA2919773A1 (en) | 2013-08-05 | 2015-02-12 | Glaxosmithkline Biologicals S.A. | Combination immunogenic compositions |
| US10682400B2 (en) | 2014-04-30 | 2020-06-16 | President And Fellows Of Harvard College | Combination vaccine devices and methods of killing cancer cells |
| CN106659777A (zh) | 2014-06-13 | 2017-05-10 | 葛兰素史密丝克莱恩生物有限公司 | 免疫原性组合产品 |
| EP3250250A4 (en) | 2015-01-30 | 2019-05-22 | President and Fellows of Harvard College | PERITUMORAL AND INTRATUMORAL MATERIALS FOR CANCER THERAPY |
| JP7094533B2 (ja) | 2015-04-10 | 2022-07-04 | プレジデント アンド フェローズ オブ ハーバード カレッジ | 免疫細胞捕捉デバイスおよびその製造および使用方法 |
| US10426829B2 (en) | 2015-09-03 | 2019-10-01 | Novavax, Inc. | Vaccine compositions having improved stability and immunogenicity |
| PE20181354A1 (es) | 2015-12-23 | 2018-08-22 | Pfizer | Mutantes de proteina f de rsv |
| EP3411475B1 (en) | 2016-02-06 | 2025-08-27 | President and Fellows of Harvard College | Recapitulating the hematopoietic niche to reconstitute immunity |
| CN115537372A (zh) | 2016-07-13 | 2022-12-30 | 哈佛学院院长等 | 抗原呈递细胞模拟支架及其制备和使用方法 |
| EP3493842A4 (en) | 2016-08-02 | 2020-07-29 | President and Fellows of Harvard College | BIOMATERIALS TO MODULATE IMMUNE RESPONSES |
| IL264464B2 (en) | 2016-08-03 | 2024-02-01 | Lonza Walkersville Inc | A method for detecting endotoxin using Limulus extract of amoeba, which is mainly free of coagulogen |
| GB201620968D0 (en) | 2016-12-09 | 2017-01-25 | Glaxosmithkline Biologicals Sa | Adenovirus polynucleotides and polypeptides |
| US11352656B2 (en) * | 2017-01-11 | 2022-06-07 | Lonza Walkersville, Inc. | Coagulogen-free clarified limulus amebocyte lysate and chromogenic assay of endotoxin |
| ES3028362T3 (en) | 2017-07-24 | 2025-06-19 | Novavax Inc | Methods and compositions for treating respiratory disease |
| WO2019076892A1 (en) | 2017-10-16 | 2019-04-25 | Glaxosmithkline Biologicals Sa | ENHANCED PROMOTER |
| US11859199B2 (en) | 2017-10-16 | 2024-01-02 | Glaxosmithkline Biologicals Sa | Adenoviral vectors with two expression cassettes encoding RSV antigenic proteins or fragments thereof |
| CN111479926A (zh) | 2017-10-16 | 2020-07-31 | 葛兰素史密丝克莱恩生物有限公司 | 具有两个表达盒的猿猴腺病毒载体 |
| US11905313B2 (en) | 2017-11-28 | 2024-02-20 | The United States of America, as represented by the Secretary, Department of Health and Human Services. | Recombinant RSV G proteins and their use |
| CA3092984A1 (en) | 2018-03-19 | 2019-09-26 | Novavax, Inc. | Multivalent influenza nanoparticle vaccines |
| CN112638936A (zh) | 2018-06-12 | 2021-04-09 | 葛兰素史密丝克莱恩生物有限公司 | 腺病毒多核苷酸和多肽 |
| WO2020061129A1 (en) | 2018-09-19 | 2020-03-26 | President And Fellows Of Harvard College | Compositions and methods for labeling and modulation of cells in vitro and in vivo |
| KR102725189B1 (ko) | 2018-11-01 | 2024-10-31 | 에스케이바이오사이언스(주) | 재조합 호흡기 세포융합 바이러스 f 단백질 및 이를 포함하는 백신 조성물 |
| KR102679227B1 (ko) | 2019-02-28 | 2024-06-28 | 케이엠 바이올로직스 가부시키가이샤 | Rsv f/g 키메라 백신 |
| CN114993784B (zh) * | 2022-05-27 | 2025-07-29 | 重庆医科大学 | 一种乙肝病毒颗粒裂解液及其制备与应用 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2236946T3 (es) * | 1997-09-19 | 2005-07-16 | Wyeth Holdings Corporation | Peptidos derivados de la proteina de union (g) del virus respiratorio sincitial. |
-
2008
- 2008-03-20 US US12/531,758 patent/US20100203071A1/en not_active Abandoned
- 2008-03-20 CA CA002684578A patent/CA2684578A1/en not_active Abandoned
- 2008-03-20 EP EP08751012A patent/EP2181121A4/en not_active Withdrawn
- 2008-03-20 JP JP2009554098A patent/JP2010522540A/ja active Pending
- 2008-03-20 WO PCT/IB2008/001286 patent/WO2008114149A2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| EP2181121A4 (en) | 2012-07-11 |
| WO2008114149A2 (en) | 2008-09-25 |
| US20100203071A1 (en) | 2010-08-12 |
| EP2181121A2 (en) | 2010-05-05 |
| WO2008114149A3 (en) | 2011-04-21 |
| JP2010522540A (ja) | 2010-07-08 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20100203071A1 (en) | Chimeric antigens | |
| CA2710600C (en) | Recombinant rsv antigens | |
| AU2014203636C1 (en) | Recombinant RSV antigens | |
| US20110177117A1 (en) | Chimeric respiratory syncytial virus polypeptide antigens | |
| US20120135028A1 (en) | Vaccine | |
| US20160122398A1 (en) | Recombinant rsv antigens | |
| HK40091519A (en) | Recombinant rsv antigens | |
| HK40085221A (en) | Recombinant rsv antigens | |
| HK40092189A (en) | Recombinant rsv antigens | |
| HK40083885A (en) | Recombinant rsv antigens | |
| AU2013201836B2 (en) | Recombinant RSV antigens |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20140207 |