WO2024109611A1 - Protéine f de pré-fusion du virus respiratoire syncytial mutant et son utilisation - Google Patents
Protéine f de pré-fusion du virus respiratoire syncytial mutant et son utilisation Download PDFInfo
- Publication number
- WO2024109611A1 WO2024109611A1 PCT/CN2023/131875 CN2023131875W WO2024109611A1 WO 2024109611 A1 WO2024109611 A1 WO 2024109611A1 CN 2023131875 W CN2023131875 W CN 2023131875W WO 2024109611 A1 WO2024109611 A1 WO 2024109611A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- respiratory syncytial
- syncytial virus
- protein
- mutant
- prefusion
- Prior art date
Links
- 241000725643 Respiratory syncytial virus Species 0.000 title claims abstract description 153
- 230000004927 fusion Effects 0.000 title claims abstract description 82
- 108090000623 proteins and genes Proteins 0.000 title description 31
- 102000004169 proteins and genes Human genes 0.000 title description 20
- 108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 claims abstract description 136
- 230000035772 mutation Effects 0.000 claims abstract description 38
- 125000000539 amino acid group Chemical group 0.000 claims abstract description 26
- 235000018417 cysteine Nutrition 0.000 claims abstract description 24
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims abstract description 23
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims abstract description 20
- 108010075254 C-Peptide Proteins 0.000 claims description 35
- 210000004027 cell Anatomy 0.000 claims description 31
- 238000000034 method Methods 0.000 claims description 29
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 28
- 206010061603 Respiratory syncytial virus infection Diseases 0.000 claims description 27
- 239000012620 biological material Substances 0.000 claims description 25
- 238000006467 substitution reaction Methods 0.000 claims description 22
- 208000030925 respiratory syncytial virus infectious disease Diseases 0.000 claims description 21
- 239000013612 plasmid Substances 0.000 claims description 17
- 239000013598 vector Substances 0.000 claims description 17
- 241000700605 Viruses Species 0.000 claims description 13
- 108020004707 nucleic acids Proteins 0.000 claims description 13
- 102000039446 nucleic acids Human genes 0.000 claims description 13
- 150000007523 nucleic acids Chemical class 0.000 claims description 13
- 102220259718 rs34120878 Human genes 0.000 claims description 13
- 239000003814 drug Substances 0.000 claims description 12
- 108700001237 Nucleic Acid-Based Vaccines Proteins 0.000 claims description 11
- 229940023146 nucleic acid vaccine Drugs 0.000 claims description 11
- 229940126583 recombinant protein vaccine Drugs 0.000 claims description 11
- 229940126580 vector vaccine Drugs 0.000 claims description 11
- 239000003153 chemical reaction reagent Substances 0.000 claims description 9
- 210000004962 mammalian cell Anatomy 0.000 claims description 7
- 210000004978 chinese hamster ovary cell Anatomy 0.000 claims description 6
- 238000002360 preparation method Methods 0.000 claims description 6
- 229940079593 drug Drugs 0.000 claims description 5
- 241000894006 Bacteria Species 0.000 claims description 4
- 241000702421 Dependoparvovirus Species 0.000 claims description 4
- 241000233866 Fungi Species 0.000 claims description 4
- 241000238631 Hexapoda Species 0.000 claims description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 4
- 241000700618 Vaccinia virus Species 0.000 claims description 4
- 230000001177 retroviral effect Effects 0.000 claims description 4
- 210000004881 tumor cell Anatomy 0.000 claims description 4
- 241000701161 unidentified adenovirus Species 0.000 claims description 4
- 241001529453 unidentified herpesvirus Species 0.000 claims description 4
- 230000027455 binding Effects 0.000 abstract description 39
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 14
- 230000003472 neutralizing effect Effects 0.000 abstract description 11
- 229960005486 vaccine Drugs 0.000 abstract description 11
- 102000036639 antigens Human genes 0.000 description 62
- 108091007433 antigens Proteins 0.000 description 62
- 239000000427 antigen Substances 0.000 description 60
- 230000000694 effects Effects 0.000 description 17
- 235000018102 proteins Nutrition 0.000 description 16
- 239000013638 trimer Substances 0.000 description 13
- 238000010438 heat treatment Methods 0.000 description 12
- 239000000523 sample Substances 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- 235000001014 amino acid Nutrition 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 10
- 238000011161 development Methods 0.000 description 9
- 239000013641 positive control Substances 0.000 description 9
- 239000012634 fragment Substances 0.000 description 8
- 230000001965 increasing effect Effects 0.000 description 8
- 229960001521 motavizumab Drugs 0.000 description 8
- 229940121468 nirsevimab Drugs 0.000 description 8
- 238000012216 screening Methods 0.000 description 8
- 229960000402 palivizumab Drugs 0.000 description 7
- 238000013461 design Methods 0.000 description 6
- 239000000178 monomer Substances 0.000 description 6
- 230000002265 prevention Effects 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 241000270730 Alligator mississippiensis Species 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 4
- 102000008300 Mutant Proteins Human genes 0.000 description 4
- 108010021466 Mutant Proteins Proteins 0.000 description 4
- 229940124679 RSV vaccine Drugs 0.000 description 4
- 238000010521 absorption reaction Methods 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 210000000170 cell membrane Anatomy 0.000 description 4
- 239000011248 coating agent Substances 0.000 description 4
- 238000000576 coating method Methods 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 239000013639 protein trimer Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- 102000004961 Furin Human genes 0.000 description 3
- 108090001126 Furin Proteins 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 239000006143 cell culture medium Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 238000002844 melting Methods 0.000 description 3
- 230000008018 melting Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 101150012619 FCS1 gene Proteins 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000008876 conformational transition Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 230000002708 enhancing effect Effects 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000034217 membrane fusion Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 238000005829 trimerization reaction Methods 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 206010006448 Bronchiolitis Diseases 0.000 description 1
- 108091028075 Circular RNA Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 101001121408 Homo sapiens L-amino-acid oxidase Proteins 0.000 description 1
- HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 102100026388 L-amino-acid oxidase Human genes 0.000 description 1
- 206010024971 Lower respiratory tract infections Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 206010038687 Respiratory distress Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101100012902 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) FIG2 gene Proteins 0.000 description 1
- 101100233916 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) KAR5 gene Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 108010003533 Viral Envelope Proteins Proteins 0.000 description 1
- 108010065667 Viral Matrix Proteins Proteins 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- VZTDIZULWFCMLS-UHFFFAOYSA-N ammonium formate Chemical compound [NH4+].[O-]C=O VZTDIZULWFCMLS-UHFFFAOYSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000000149 argon plasma sintering Methods 0.000 description 1
- 238000003766 bioinformatics method Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 230000034303 cell budding Effects 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 231100000517 death Toxicity 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000002866 fluorescence resonance energy transfer Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000007499 fusion processing Methods 0.000 description 1
- 230000008642 heat stress Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 230000005965 immune activity Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 108091055883 miR-6003 stem-loop Proteins 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000012514 monoclonal antibody product Substances 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 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
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000000455 protein structure prediction Methods 0.000 description 1
- 229940023143 protein vaccine Drugs 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000003753 real-time PCR Methods 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000001338 self-assembly Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000005728 strengthening Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000003313 weakening effect Effects 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
- 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
- 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
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56983—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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/18011—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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/005—Assays involving biological materials from specific organisms or of a specific nature from viruses
- G01N2333/08—RNA viruses
- G01N2333/115—Paramyxoviridae, e.g. parainfluenza virus
- G01N2333/135—Respiratory syncytial virus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2469/00—Immunoassays for the detection of microorganisms
- G01N2469/10—Detection of antigens from microorganism in sample from host
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2469/00—Immunoassays for the detection of microorganisms
- G01N2469/20—Detection of antibodies in sample from host which are directed against antigens from microorganisms
-
- 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)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Public Health (AREA)
- Urology & Nephrology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Hematology (AREA)
- Pharmacology & Pharmacy (AREA)
- Biomedical Technology (AREA)
- Animal Behavior & Ethology (AREA)
- Biophysics (AREA)
- Veterinary Medicine (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Communicable Diseases (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Tropical Medicine & Parasitology (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Cell Biology (AREA)
- Pulmonology (AREA)
- Mycology (AREA)
- Food Science & Technology (AREA)
- Oncology (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Peptides Or Proteins (AREA)
Abstract
L'invention concerne une protéine F de pré-fusion du virus respiratoire syncytial mutant, ayant les mutations suivantes par comparaison avec une protéine F de pré-fusion du virus respiratoire syncytial de type sauvage : (a) au moins un résidu d'acide aminé dans une sous-unité F1 et/ou une sous-unité F2 est substitué par la cystéine, et (b) les résidus d'acides aminés aux positions 104-144 de la protéine F de pré-fusion du virus respiratoire syncytial de type sauvage sont partiellement ou complètement substitués par un peptide lieur, au moins deux longueurs des résidus d'acides aminés du peptide lieur étant comprises. Par comparaison avec des produits similaires, la protéine F de pré-fusion du virus respiratoire syncytial mutant présente une excellente activité de liaison à l'anticorps neutralisant et une excellente stabilité thermique, et est appropriée pour être développée dans l'un des composants de vaccins contre le virus respiratoire syncytial.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN202211472876.7A CN116284266B (zh) | 2022-11-21 | 2022-11-21 | 突变型呼吸道合胞病毒融合前f蛋白及其应用 |
CN202211472876.7 | 2022-11-21 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO2024109611A1 true WO2024109611A1 (fr) | 2024-05-30 |
Family
ID=86791194
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/CN2023/131875 WO2024109611A1 (fr) | 2022-11-21 | 2023-11-15 | Protéine f de pré-fusion du virus respiratoire syncytial mutant et son utilisation |
Country Status (2)
Country | Link |
---|---|
CN (1) | CN116284266B (fr) |
WO (1) | WO2024109611A1 (fr) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN117487823A (zh) * | 2023-09-28 | 2024-02-02 | 怡道生物科技(苏州)有限公司 | 呼吸道合胞体病毒mRNA疫苗及其制备方法和应用 |
CN117304281B (zh) * | 2023-11-28 | 2024-04-16 | 江苏瑞科生物技术股份有限公司 | 一种重组rsv f蛋白及其应用 |
CN117886902A (zh) * | 2023-12-21 | 2024-04-16 | 易康生物(苏州)有限公司 | 改良的呼吸道合胞病毒融合f蛋白突变体及其应用 |
CN117586358A (zh) * | 2024-01-19 | 2024-02-23 | 北京安百胜生物科技有限公司 | 一种具有免疫原性的呼吸道合胞病毒(rsv)多肽 |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
PL2988780T3 (pl) * | 2013-04-25 | 2019-06-28 | Janssen Vaccines & Prevention B.V. | Stabilizowane rozpuszczalne prefuzyjne polipeptydy F RSV |
BR112018010805A2 (pt) * | 2015-12-23 | 2018-11-27 | Pfizer Inc. | mutantes de proteína f de rsv |
-
2022
- 2022-11-21 CN CN202211472876.7A patent/CN116284266B/zh active Active
-
2023
- 2023-11-15 WO PCT/CN2023/131875 patent/WO2024109611A1/fr unknown
Also Published As
Publication number | Publication date |
---|---|
CN116284266A (zh) | 2023-06-23 |
CN116284266B (zh) | 2024-01-19 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
WO2024109611A1 (fr) | Protéine f de pré-fusion du virus respiratoire syncytial mutant et son utilisation | |
CN114057894B (zh) | 一种产生广谱交叉中和活性的重组新型冠状病毒rbd三聚体蛋白疫苗、其制备方法和应用 | |
CN108129566B (zh) | 靶向间皮素的c-型单域抗体及其制备方法与应用 | |
JP6450688B2 (ja) | 呼吸器合胞体ウイルスfタンパク質エピトープ | |
WO2022089471A1 (fr) | ANTIGÈNE MULTIMÈRE DE β-CORONAVIRUS, SON PROCÉDÉ DE PRÉPARATION ET SON UTILISATION | |
WO2023019724A1 (fr) | Anticorps monoclonal 35b5, son procédé de préparation et son utilisation | |
CN112521494B (zh) | 一种抗SARS-CoV-2的单克隆抗体2B11 | |
CN116528897A (zh) | 靶向SARS-CoV-2的抗原结合分子 | |
WO2022068846A1 (fr) | Nouveau vaccin à arnm contre un coronavirus, sa méthode de préparation et son utilisation | |
EP4206224A1 (fr) | Anticorps humain ou fragment de liaison à l'antigène de celui-ci dirigé contre une protéine de spicule de coronavirus | |
WO2022011717A1 (fr) | Nanocorps dirigé contre le nouveau coronavirus et son utilisation | |
US20170198014A1 (en) | Polypeptides and their use for treating influenza | |
EP4299745A1 (fr) | Anticorps anti-sars-cov-2 | |
WO2022102744A1 (fr) | Anticorps visant la protéine de spicule du sars-cov-2 | |
TWI775422B (zh) | 重組抗體、包含重組抗體之套組及其用途 | |
WO2018175518A1 (fr) | Mini-protéines immunogènes présentant des épitopes de neutralisation du virus respiratoire syncytial (vrs) | |
JP7038367B2 (ja) | 抗SARS-CoV-2抗体 | |
WO2021221137A1 (fr) | Médicament et kit de test utilisant chacun un anticorps anti-sars-cov-2 | |
WO2021227687A1 (fr) | Plate-forme pour la construction d'anticorps de coronavirus | |
WO2022148374A1 (fr) | Anticorps 76e1 neutralisant entièrement humain à large spectre contre le coronavirus, et utilisation associée | |
TW202309069A (zh) | 糖鏈修飾rbd及其用途 | |
CN116472278A (zh) | 与埃博拉病毒疫苗相关的组合物和方法 | |
WO2023240246A1 (fr) | Anticorps monocolonaux modifiés par calcul informatique et fragments de liaison à l'antigène spécifiques de protéines de spicule du sars-cov-2 et leurs utilisations | |
KR20230066722A (ko) | 시나지스 내성 호흡기세포융합바이러스 검출 방법 | |
AU2022346446A1 (en) | Multivalent polypeptide constructs capable of binding viral spike proteins and methods of using the same |