CA2997181A1 - Stabilized viral class i fusion proteins - Google Patents
Stabilized viral class i fusion proteins Download PDFInfo
- Publication number
- CA2997181A1 CA2997181A1 CA2997181A CA2997181A CA2997181A1 CA 2997181 A1 CA2997181 A1 CA 2997181A1 CA 2997181 A CA2997181 A CA 2997181A CA 2997181 A CA2997181 A CA 2997181A CA 2997181 A1 CA2997181 A1 CA 2997181A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- amino acid
- fusion
- seq
- class
- 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.)
- Pending
Links
- 108020001507 fusion proteins Proteins 0.000 title claims abstract description 94
- 102000037865 fusion proteins Human genes 0.000 title claims abstract description 94
- 230000003612 virological effect Effects 0.000 title description 9
- 230000004927 fusion Effects 0.000 claims abstract description 112
- 230000035772 mutation Effects 0.000 claims abstract description 63
- 108090000623 proteins and genes Proteins 0.000 claims description 98
- 102000004169 proteins and genes Human genes 0.000 claims description 97
- 101710154606 Hemagglutinin Proteins 0.000 claims description 59
- 101710093908 Outer capsid protein VP4 Proteins 0.000 claims description 59
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 claims description 59
- 101710176177 Protein A56 Proteins 0.000 claims description 59
- 125000000539 amino acid group Chemical group 0.000 claims description 45
- 239000000185 hemagglutinin Substances 0.000 claims description 42
- 150000007523 nucleic acids Chemical group 0.000 claims description 39
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 38
- 108020004707 nucleic acids Proteins 0.000 claims description 36
- 102000039446 nucleic acids Human genes 0.000 claims description 36
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 34
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 33
- 229920001184 polypeptide Polymers 0.000 claims description 32
- 101710091045 Envelope protein Proteins 0.000 claims description 27
- 101710188315 Protein X Proteins 0.000 claims description 27
- 206010022000 influenza Diseases 0.000 claims description 24
- 241000713772 Human immunodeficiency virus 1 Species 0.000 claims description 19
- 239000000203 mixture Substances 0.000 claims description 14
- 208000031886 HIV Infections Diseases 0.000 claims description 10
- 241000713340 Human immunodeficiency virus 2 Species 0.000 claims description 10
- 241000711950 Filoviridae Species 0.000 claims description 8
- 230000001177 retroviral effect Effects 0.000 claims description 6
- 241001115402 Ebolavirus Species 0.000 claims description 4
- 241000713196 Influenza B virus Species 0.000 claims description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 4
- 108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 claims 7
- 102100021696 Syncytin-1 Human genes 0.000 claims 4
- 241001115401 Marburgvirus Species 0.000 claims 2
- 235000018102 proteins Nutrition 0.000 description 66
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 39
- 239000013638 trimer Substances 0.000 description 38
- 210000004027 cell Anatomy 0.000 description 37
- 238000006467 substitution reaction Methods 0.000 description 30
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 27
- 239000013598 vector Substances 0.000 description 26
- 102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 24
- 230000007935 neutral effect Effects 0.000 description 17
- 238000012815 AlphaLISA Methods 0.000 description 15
- 108020004705 Codon Proteins 0.000 description 15
- 235000001014 amino acid Nutrition 0.000 description 15
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 15
- 239000006228 supernatant Substances 0.000 description 15
- 229940024606 amino acid Drugs 0.000 description 14
- 238000000034 method Methods 0.000 description 14
- 241000725303 Human immunodeficiency virus Species 0.000 description 13
- 241000700605 Viruses Species 0.000 description 13
- 201000011001 Ebola Hemorrhagic Fever Diseases 0.000 description 12
- 150000001413 amino acids Chemical class 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 11
- 230000028993 immune response Effects 0.000 description 11
- 230000000087 stabilizing effect Effects 0.000 description 11
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 10
- 238000005516 engineering process Methods 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 9
- 239000011324 bead Substances 0.000 description 9
- 230000027455 binding Effects 0.000 description 9
- 210000004899 c-terminal region Anatomy 0.000 description 9
- 238000000569 multi-angle light scattering Methods 0.000 description 9
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 208000034628 Celiac artery compression syndrome Diseases 0.000 description 7
- 108010088468 Ebola virus envelope glycoprotein Proteins 0.000 description 7
- 108010059722 Viral Fusion Proteins Proteins 0.000 description 7
- 239000002671 adjuvant Substances 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 230000001939 inductive effect Effects 0.000 description 7
- 101900000220 Lake Victoria marburgvirus Envelope glycoprotein Proteins 0.000 description 6
- 230000002209 hydrophobic effect Effects 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 241000712431 Influenza A virus Species 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 230000002427 irreversible effect Effects 0.000 description 5
- 230000007246 mechanism Effects 0.000 description 5
- 230000003472 neutralizing effect Effects 0.000 description 5
- 238000011002 quantification Methods 0.000 description 5
- 230000006641 stabilisation Effects 0.000 description 5
- 238000011105 stabilization Methods 0.000 description 5
- 229960005486 vaccine Drugs 0.000 description 5
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 4
- 102100034353 Integrase Human genes 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 4
- 108700019146 Transgenes Proteins 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 108010078428 env Gene Products Proteins 0.000 description 4
- 108010028403 hemagglutinin esterase Proteins 0.000 description 4
- 230000002163 immunogen Effects 0.000 description 4
- 239000002523 lectin Substances 0.000 description 4
- 239000000546 pharmaceutical excipient Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 230000009385 viral infection Effects 0.000 description 4
- 241000234271 Galanthus Species 0.000 description 3
- 108090001090 Lectins Proteins 0.000 description 3
- 102000004856 Lectins Human genes 0.000 description 3
- 239000004472 Lysine Substances 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
- 238000004113 cell culture Methods 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 210000005260 human cell Anatomy 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 3
- 230000030788 protein refolding Effects 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 108700010070 Codon Usage Proteins 0.000 description 2
- 230000006820 DNA synthesis Effects 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- 125000000174 L-prolyl group Chemical group [H]N1C([H])([H])C([H])([H])C([H])([H])[C@@]1([H])C(*)=O 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Chemical group CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 241000711504 Paramyxoviridae Species 0.000 description 2
- 108010001267 Protein Subunits Proteins 0.000 description 2
- 102000002067 Protein Subunits Human genes 0.000 description 2
- 238000011529 RT qPCR Methods 0.000 description 2
- 241000712907 Retroviridae Species 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 239000004411 aluminium Substances 0.000 description 2
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 2
- 229910052782 aluminium Inorganic materials 0.000 description 2
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 2
- 229910021502 aluminium hydroxide Inorganic materials 0.000 description 2
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 2
- 229940001007 aluminium phosphate Drugs 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- -1 enhancer(s) Chemical class 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 238000005558 fluorometry Methods 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 208000037797 influenza A Diseases 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 239000000155 melt Substances 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 229910052759 nickel Inorganic materials 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 239000012146 running buffer Substances 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 238000002864 sequence alignment Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 239000008174 sterile solution Substances 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000011282 treatment Methods 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000710929 Alphavirus Species 0.000 description 1
- 241000712892 Arenaviridae Species 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
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000711573 Coronaviridae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 101000916289 Ctenocephalides felis Salivary antigen 1 Proteins 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 101710086762 Diamine acetyltransferase 1 Proteins 0.000 description 1
- 102100034274 Diamine acetyltransferase 1 Human genes 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 101710146739 Enterotoxin Proteins 0.000 description 1
- 101710204837 Envelope small membrane protein Proteins 0.000 description 1
- 241000710781 Flaviviridae Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 102000004961 Furin Human genes 0.000 description 1
- 108090001126 Furin Proteins 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 102100039289 Glial fibrillary acidic protein Human genes 0.000 description 1
- 101710193519 Glial fibrillary acidic protein Proteins 0.000 description 1
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 241000700586 Herpesviridae Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 description 1
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- XQFRJNBWHJMXHO-RRKCRQDMSA-N IDUR Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(I)=C1 XQFRJNBWHJMXHO-RRKCRQDMSA-N 0.000 description 1
- 108700002232 Immediate-Early Genes Proteins 0.000 description 1
- 241001016884 Influenza B virus (B/Yamanashi/166/1998) Species 0.000 description 1
- 101710125507 Integrase/recombinase Proteins 0.000 description 1
- 108091092195 Intron Proteins 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
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-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
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- 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 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 101710145006 Lysis protein Proteins 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 239000012515 MabSelect SuRe Substances 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102100026009 NF-kappa-B inhibitor zeta Human genes 0.000 description 1
- 101710115530 NF-kappa-B inhibitor zeta Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000150350 Peribunyaviridae Species 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 101710185720 Putative ethidium bromide resistance protein Proteins 0.000 description 1
- 235000001630 Pyrus pyrifolia var culta Nutrition 0.000 description 1
- 240000002609 Pyrus pyrifolia var. culta Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000725643 Respiratory syncytial virus Species 0.000 description 1
- 241000711931 Rhabdoviridae Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 101710181456 Spermidine N(1)-acetyltransferase Proteins 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 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
- 241000710771 Tick-borne encephalitis virus Species 0.000 description 1
- 241000710924 Togaviridae Species 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 206010058874 Viraemia Diseases 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 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 1
- 239000002253 acid Substances 0.000 description 1
- 238000004115 adherent culture Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 159000000013 aluminium salts Chemical class 0.000 description 1
- NTGGOTYRTOXKMQ-UHFFFAOYSA-K aluminum;potassium;phosphate Chemical compound [Al+3].[K+].[O-]P([O-])([O-])=O NTGGOTYRTOXKMQ-UHFFFAOYSA-K 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 230000002155 anti-virotic effect Effects 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 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
- 101150036080 at gene Proteins 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 238000012439 bead-based proximity assay Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 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
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000000147 enterotoxin Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000012537 formulation buffer Substances 0.000 description 1
- 238000012395 formulation development Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000000799 fusogenic effect Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 210000005046 glial fibrillary acidic protein Anatomy 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 150000004676 glycans Chemical group 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 229960001438 immunostimulant agent Drugs 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 208000037798 influenza B Diseases 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 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
- 229910052743 krypton Inorganic materials 0.000 description 1
- DNNSSWSSYDEUBZ-UHFFFAOYSA-N krypton atom Chemical compound [Kr] DNNSSWSSYDEUBZ-UHFFFAOYSA-N 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000034217 membrane fusion Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000001426 native polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 239000007764 o/w emulsion Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 229940124531 pharmaceutical excipient Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000005498 polishing Methods 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 239000013639 protein trimer Substances 0.000 description 1
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 229940124856 vaccine component Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- 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
- 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
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- 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
- A61P31/20—Antivirals for DNA viruses
- A61P31/22—Antivirals for DNA viruses for herpes 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
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16022—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
- C12N2760/14011—Filoviridae
- C12N2760/14111—Ebolavirus, e.g. Zaire ebolavirus
- C12N2760/14122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16111—Influenzavirus A, i.e. influenza A virus
- C12N2760/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N7/00—Viruses; Bacteriophages; Compositions thereof; Preparation or purification thereof
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Virology (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Immunology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Pulmonology (AREA)
- AIDS & HIV (AREA)
- Bioinformatics & Cheminformatics (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)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201562213466P | 2015-09-02 | 2015-09-02 | |
| US62/213,466 | 2015-09-02 | ||
| PCT/EP2016/070654 WO2017037196A1 (en) | 2015-09-02 | 2016-09-01 | Stabilized viral class i fusion proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2997181A1 true CA2997181A1 (en) | 2017-03-09 |
Family
ID=56855456
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2997181A Pending CA2997181A1 (en) | 2015-09-02 | 2016-09-01 | Stabilized viral class i fusion proteins |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US10538557B2 (enExample) |
| EP (2) | EP4019044A3 (enExample) |
| JP (2) | JP6975709B2 (enExample) |
| CN (1) | CN108025057B (enExample) |
| AU (2) | AU2016316723B2 (enExample) |
| CA (1) | CA2997181A1 (enExample) |
| WO (1) | WO2017037196A1 (enExample) |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10426829B2 (en) | 2015-09-03 | 2019-10-01 | Novavax, Inc. | Vaccine compositions having improved stability and immunogenicity |
| WO2018081318A1 (en) | 2016-10-25 | 2018-05-03 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Prefusion coronavirus spike proteins and their use |
| ES3028362T3 (en) | 2017-07-24 | 2025-06-19 | Novavax Inc | Methods and compositions for treating respiratory disease |
| CA3092984A1 (en) | 2018-03-19 | 2019-09-26 | Novavax, Inc. | Multivalent influenza nanoparticle vaccines |
| EP3836961A1 (en) | 2018-08-13 | 2021-06-23 | Janssen Vaccines & Prevention B.V. | Stabilized filovirus glycoprotein trimers |
| CN109142723B (zh) * | 2018-08-21 | 2021-07-13 | 苏州华益美生物科技有限公司 | 人类免疫缺陷病毒快速检测测试卡及其应用 |
| US10953089B1 (en) | 2020-01-27 | 2021-03-23 | Novavax, Inc. | Coronavirus vaccine formulations |
| CA3183500A1 (en) | 2020-05-11 | 2021-11-18 | Janssen Pharmaceuticals, Inc. | Sars-cov-2 vaccines |
| KR20230009445A (ko) | 2020-05-11 | 2023-01-17 | 얀센 파마슈티칼즈, 인코포레이티드 | 안정화된 코로나바이러스 스파이크 단백질 융합 단백질 |
| WO2021229448A1 (en) | 2020-05-11 | 2021-11-18 | Janssen Pharmaceuticals, Inc. | Rna replicon encoding a stabilized corona virus spike protein |
| US20230242594A1 (en) * | 2020-05-29 | 2023-08-03 | Board Of Regents, The University Of Texas System | Engineered coronavirus spike (s) protein and methods of use thereof |
| CN111704657B (zh) * | 2020-06-16 | 2021-11-09 | 四川安可瑞新材料技术有限公司 | Hiv-2重组抗原及其制备方法、用途 |
| PH12022553417A1 (en) | 2020-07-06 | 2024-04-22 | Janssen Pharmaceuticals Inc | Stabilized corona virus spike protein fusion proteins |
| US20230270838A1 (en) * | 2020-08-02 | 2023-08-31 | Richard Ascione | Vaccine compositions for influenza viruses and methods of use |
| CA3214759A1 (en) * | 2021-03-30 | 2022-10-06 | Baylor College Of Medicine | Methods and compositions for high-potency polypeptide-based protein inhibition |
| WO2023047349A1 (en) | 2021-09-24 | 2023-03-30 | Janssen Pharmaceuticals, Inc. | Stabilized coronavirus spike protein fusion proteins |
| WO2023047348A1 (en) | 2021-09-24 | 2023-03-30 | Janssen Pharmaceuticals, Inc. | Stabilized corona virus spike protein fusion proteins |
| WO2024061759A1 (en) | 2022-09-23 | 2024-03-28 | Janssen Vaccines & Prevention B.V. | Stabilized coronavirus s proteins |
| CN116947982B (zh) * | 2023-07-12 | 2024-05-14 | 吉林大学 | 三条优势表位肽序列及其在流感病毒疫苗的应用 |
| TW202527960A (zh) * | 2023-09-06 | 2025-07-16 | 美商賽諾菲巴斯德公司 | 經修飾b型流感血球凝集素多肽及核酸及其用途 |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3584341D1 (de) | 1984-08-24 | 1991-11-14 | Upjohn Co | Rekombinante dna-verbindungen und expression von polypeptiden wie tpa. |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US5057540A (en) | 1987-05-29 | 1991-10-15 | Cambridge Biotech Corporation | Saponin adjuvant |
| NZ230747A (en) | 1988-09-30 | 1992-05-26 | Bror Morein | Immunomodulating matrix comprising a complex of at least one lipid and at least one saponin; certain glycosylated triterpenoid saponins derived from quillaja saponaria molina |
| HU212924B (en) | 1989-05-25 | 1996-12-30 | Chiron Corp | Adjuvant formulation comprising a submicron oil droplet emulsion |
| US5786464C1 (en) | 1994-09-19 | 2012-04-24 | Gen Hospital Corp | Overexpression of mammalian and viral proteins |
| AUPM873294A0 (en) | 1994-10-12 | 1994-11-03 | Csl Limited | Saponin preparations and use thereof in iscoms |
| SE0202110D0 (sv) | 2002-07-05 | 2002-07-05 | Isconova Ab | Iscom preparation and use thereof |
| SE0301998D0 (sv) | 2003-07-07 | 2003-07-07 | Isconova Ab | Quil A fraction with low toxicity and use thereof |
| DK2285408T3 (en) * | 2008-06-05 | 2019-02-04 | Ablynx Nv | AMINO ACID SEQUENCES AGAINST COATING PROTEINS IN A VIRUS AND POLYPEPTIDES INCLUDING THESE FOR TREATMENT OF VIRUSAL DISEASES |
| SI3275892T1 (sl) * | 2011-05-13 | 2020-06-30 | Glaxosmithkline Biologicals S.A. | Prefuzijski RSV F antigeni |
| CA2849471A1 (en) * | 2011-09-30 | 2013-04-04 | Novavax, Inc. | Recombinant nanoparticle rsv f vaccine for respiratory syncytial virus |
| MY170927A (en) | 2011-11-28 | 2019-09-19 | Janssen Vaccines & Prevention Bv | Influenza virus vaccines and uses thereof |
| SG11201508567XA (en) | 2013-04-25 | 2015-11-27 | Crucell Holland Bv | Stabilized soluble prefusion rsv f polypeptides |
| EP2873423B1 (en) | 2013-10-07 | 2017-05-31 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| US9931394B2 (en) * | 2015-03-23 | 2018-04-03 | International Aids Vaccine Initiative | Soluble HIV-1 envelope glycoprotein trimers |
-
2016
- 2016-09-01 EP EP21200796.7A patent/EP4019044A3/en not_active Withdrawn
- 2016-09-01 WO PCT/EP2016/070654 patent/WO2017037196A1/en not_active Ceased
- 2016-09-01 AU AU2016316723A patent/AU2016316723B2/en active Active
- 2016-09-01 EP EP16760463.6A patent/EP3344288A1/en not_active Withdrawn
- 2016-09-01 US US15/756,800 patent/US10538557B2/en active Active
- 2016-09-01 CN CN201680051120.1A patent/CN108025057B/zh active Active
- 2016-09-01 JP JP2018511416A patent/JP6975709B2/ja active Active
- 2016-09-01 CA CA2997181A patent/CA2997181A1/en active Pending
-
2019
- 2019-12-03 US US16/701,429 patent/US10711042B2/en active Active
-
2020
- 2020-11-12 JP JP2020188363A patent/JP2021045138A/ja active Pending
-
2021
- 2021-03-02 AU AU2021201330A patent/AU2021201330A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| US20180346521A1 (en) | 2018-12-06 |
| AU2021201330A1 (en) | 2021-03-18 |
| CN108025057B (zh) | 2023-04-18 |
| US20200115421A1 (en) | 2020-04-16 |
| US10711042B2 (en) | 2020-07-14 |
| AU2016316723A1 (en) | 2018-02-22 |
| JP2018529331A (ja) | 2018-10-11 |
| JP6975709B2 (ja) | 2021-12-01 |
| JP2021045138A (ja) | 2021-03-25 |
| EP3344288A1 (en) | 2018-07-11 |
| EP4019044A2 (en) | 2022-06-29 |
| US10538557B2 (en) | 2020-01-21 |
| WO2017037196A1 (en) | 2017-03-09 |
| CN108025057A (zh) | 2018-05-11 |
| EP4019044A3 (en) | 2022-08-24 |
| AU2016316723B2 (en) | 2021-03-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US10711042B2 (en) | Stabilized viral class I fusion proteins | |
| CA2991002C (en) | Vaccine against rsv | |
| AU2014259474B2 (en) | Stabilized soluble prefusion RSV F polypeptides | |
| US10457708B2 (en) | Stabilized soluble pre-fusion RSV F polypeptides | |
| US11759514B2 (en) | Stabilized pre-fusion RSV F proteins | |
| CA3117275A1 (en) | Stabilized pre-fusion rsv f proteins | |
| WO2014202570A1 (en) | Stabilized soluble pre-fusion rsv f polypeptides | |
| AU2017248021A1 (en) | Stabilized soluble pre-fusion RSV F proteins | |
| WO2017207477A1 (en) | Stabilized pre-fusion rsv f proteins | |
| OA19273A (en) | Stabilized pre-fusion RSV F proteins. | |
| HK40000138B (en) | Stabilized pre-fusion rsv f proteins | |
| HK40000138A (en) | Stabilized pre-fusion rsv f proteins |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |
|
| EEER | Examination request |
Effective date: 20210901 |