JP2011528902A - 抗ａ型インフルエンザウイルス中和抗体およびその使用 - Google Patents
抗ａ型インフルエンザウイルス中和抗体およびその使用 Download PDFInfo
- Publication number
- JP2011528902A JP2011528902A JP2011519253A JP2011519253A JP2011528902A JP 2011528902 A JP2011528902 A JP 2011528902A JP 2011519253 A JP2011519253 A JP 2011519253A JP 2011519253 A JP2011519253 A JP 2011519253A JP 2011528902 A JP2011528902 A JP 2011528902A
- Authority
- JP
- Japan
- Prior art keywords
- seq
- antibody
- antigen
- binding fragment
- influenza
- 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
- 230000003472 neutralizing effect Effects 0.000 title claims description 37
- 241000700605 Viruses Species 0.000 title claims description 28
- 208000037797 influenza A Diseases 0.000 title claims description 12
- 230000027455 binding Effects 0.000 claims abstract description 114
- 239000000427 antigen Substances 0.000 claims abstract description 107
- 108091007433 antigens Proteins 0.000 claims abstract description 106
- 102000036639 antigens Human genes 0.000 claims abstract description 106
- 239000012634 fragment Substances 0.000 claims abstract description 105
- 241000712431 Influenza A virus Species 0.000 claims abstract description 80
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 64
- 238000000034 method Methods 0.000 claims abstract description 62
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 52
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 52
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims abstract description 40
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims abstract description 40
- 206010022000 influenza Diseases 0.000 claims abstract description 38
- 210000003719 b-lymphocyte Anatomy 0.000 claims abstract description 35
- 238000011282 treatment Methods 0.000 claims abstract description 28
- 208000015181 infectious disease Diseases 0.000 claims abstract description 23
- 238000003745 diagnosis Methods 0.000 claims abstract description 6
- 238000012216 screening Methods 0.000 claims abstract description 6
- 210000004027 cell Anatomy 0.000 claims description 74
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 43
- 239000008194 pharmaceutical composition Substances 0.000 claims description 33
- 239000003814 drug Substances 0.000 claims description 25
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 24
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 22
- 229920001184 polypeptide Polymers 0.000 claims description 20
- 229960005486 vaccine Drugs 0.000 claims description 20
- 239000013598 vector Substances 0.000 claims description 20
- 238000004519 manufacturing process Methods 0.000 claims description 15
- 238000006386 neutralization reaction Methods 0.000 claims description 12
- 230000002163 immunogen Effects 0.000 claims description 11
- 108010047041 Complementarity Determining Regions Proteins 0.000 claims description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 9
- 239000003446 ligand Substances 0.000 claims description 8
- 238000002560 therapeutic procedure Methods 0.000 claims description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- 238000012544 monitoring process Methods 0.000 claims description 5
- 241000712461 unidentified influenza virus Species 0.000 claims description 5
- 108091033319 polynucleotide Proteins 0.000 claims description 4
- 102000040430 polynucleotide Human genes 0.000 claims description 4
- 239000002157 polynucleotide Substances 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 3
- 239000003085 diluting agent Substances 0.000 claims description 2
- 230000009385 viral infection Effects 0.000 claims 1
- 101710154606 Hemagglutinin Proteins 0.000 abstract description 39
- 101710093908 Outer capsid protein VP4 Proteins 0.000 abstract description 39
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 abstract description 39
- 101710176177 Protein A56 Proteins 0.000 abstract description 39
- 239000000185 hemagglutinin Substances 0.000 abstract description 39
- 210000004180 plasmocyte Anatomy 0.000 abstract description 22
- 230000002265 prevention Effects 0.000 abstract description 5
- 239000000203 mixture Substances 0.000 description 51
- 239000003937 drug carrier Substances 0.000 description 19
- 108090000623 proteins and genes Proteins 0.000 description 18
- 210000003128 head Anatomy 0.000 description 17
- 230000001225 therapeutic effect Effects 0.000 description 17
- 241000699670 Mus sp. Species 0.000 description 14
- 150000001413 amino acids Chemical class 0.000 description 12
- 102000004169 proteins and genes Human genes 0.000 description 12
- 239000002202 Polyethylene glycol Substances 0.000 description 10
- 229920001223 polyethylene glycol Polymers 0.000 description 10
- 230000000694 effects Effects 0.000 description 9
- 241000282412 Homo Species 0.000 description 8
- 102000005348 Neuraminidase Human genes 0.000 description 8
- 108010006232 Neuraminidase Proteins 0.000 description 8
- 238000012258 culturing Methods 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 238000000338 in vitro Methods 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 239000011159 matrix material Substances 0.000 description 7
- 239000000725 suspension Substances 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 229960003971 influenza vaccine Drugs 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 230000001932 seasonal effect Effects 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 201000010099 disease Diseases 0.000 description 5
- 238000012377 drug delivery Methods 0.000 description 5
- 238000001802 infusion Methods 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 238000002255 vaccination Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 4
- 230000000890 antigenic effect Effects 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 210000001035 gastrointestinal tract Anatomy 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N glycerol group Chemical group OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 4
- 229940022353 herceptin Drugs 0.000 description 4
- 210000004408 hybridoma Anatomy 0.000 description 4
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 238000003018 immunoassay Methods 0.000 description 4
- 230000002458 infectious effect Effects 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 238000003046 intermediate neglect of differential overlap Methods 0.000 description 4
- 231100000518 lethal Toxicity 0.000 description 4
- 230000001665 lethal effect Effects 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 210000004072 lung Anatomy 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 238000005457 optimization Methods 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 230000002195 synergetic effect Effects 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108010032595 Antibody Binding Sites Proteins 0.000 description 3
- 241000271566 Aves Species 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 239000013543 active substance Substances 0.000 description 3
- 230000005875 antibody response Effects 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000000120 cytopathologic effect Effects 0.000 description 3
- 229940033324 influenza A vaccine Drugs 0.000 description 3
- 238000007912 intraperitoneal administration Methods 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 210000001806 memory b lymphocyte Anatomy 0.000 description 3
- 201000000050 myeloid neoplasm Diseases 0.000 description 3
- 238000011275 oncology therapy Methods 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 238000011321 prophylaxis Methods 0.000 description 3
- 125000006239 protecting group Chemical group 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 238000003127 radioimmunoassay Methods 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 238000006722 reduction reaction Methods 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 229940124597 therapeutic agent Drugs 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 230000003442 weekly effect Effects 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 241000283707 Capra Species 0.000 description 2
- 108700010070 Codon Usage Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 208000032163 Emerging Communicable disease Diseases 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 241000702620 H-1 parvovirus Species 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 241001500351 Influenzavirus A Species 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- 108060001084 Luciferase Proteins 0.000 description 2
- 239000005089 Luciferase Substances 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 241000282341 Mustela putorius furo Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241000702437 Parvovirus H3 Species 0.000 description 2
- 238000010306 acid treatment Methods 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000002301 combined effect Effects 0.000 description 2
- 229940127089 cytotoxic agent Drugs 0.000 description 2
- 231100000599 cytotoxic agent Toxicity 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000002405 diagnostic procedure Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 150000002314 glycerols Polymers 0.000 description 2
- 230000035931 haemagglutination Effects 0.000 description 2
- 230000000521 hyperimmunizing effect Effects 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000006193 liquid solution Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 231100001160 nonlethal Toxicity 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- PGZUMBJQJWIWGJ-ONAKXNSWSA-N oseltamivir phosphate Chemical compound OP(O)(O)=O.CCOC(=O)C1=C[C@@H](OC(CC)CC)[C@H](NC(C)=O)[C@@H](N)C1 PGZUMBJQJWIWGJ-ONAKXNSWSA-N 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 108010052044 polyclonal B cell activator Proteins 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 230000000069 prophylactic effect Effects 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000008223 sterile water Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 239000006188 syrup Substances 0.000 description 2
- 235000020357 syrup Nutrition 0.000 description 2
- 239000003826 tablet Substances 0.000 description 2
- 229940061367 tamiflu Drugs 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000007502 viral entry Effects 0.000 description 2
- 230000029812 viral genome replication Effects 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- 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 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- 108010066676 Abrin Proteins 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 102100038080 B-cell receptor CD22 Human genes 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000282832 Camelidae Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229940046168 CpG oligodeoxynucleotide Drugs 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-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 Polymers OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108060003393 Granulin Proteins 0.000 description 1
- 101000884305 Homo sapiens B-cell receptor CD22 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- CPELXLSAUQHCOX-UHFFFAOYSA-N Hydrogen bromide Chemical compound Br CPELXLSAUQHCOX-UHFFFAOYSA-N 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 231100000111 LD50 Toxicity 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- OFOBLEOULBTSOW-UHFFFAOYSA-L Malonate Chemical compound [O-]C(=O)CC([O-])=O OFOBLEOULBTSOW-UHFFFAOYSA-L 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- XBDQKXXYIPTUBI-UHFFFAOYSA-M Propionate Chemical compound CCC([O-])=O XBDQKXXYIPTUBI-UHFFFAOYSA-M 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101000762949 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) Exotoxin A Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 231100000645 Reed–Muench method Toxicity 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- FBPFZTCFMRRESA-NQAPHZHOSA-N Sorbitol Polymers OCC(O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-NQAPHZHOSA-N 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 230000024932 T cell mediated immunity Effects 0.000 description 1
- 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 1
- 230000010530 Virus Neutralization Effects 0.000 description 1
- 210000000683 abdominal cavity Anatomy 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 210000004100 adrenal gland Anatomy 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 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 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000012830 cancer therapeutic Substances 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000013553 cell monolayer Substances 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 230000000973 chemotherapeutic effect Effects 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000005515 coenzyme Substances 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 239000000599 controlled substance Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000008298 dragée Substances 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000012407 engineering method Methods 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 210000001508 eye Anatomy 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 150000002303 glucose derivatives Polymers 0.000 description 1
- 150000002304 glucoses Polymers 0.000 description 1
- 125000002791 glucosyl group Polymers C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000028996 humoral immune response Effects 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 230000036046 immunoreaction Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- APFVFJFRJDLVQX-UHFFFAOYSA-N indium atom Chemical compound [In] APFVFJFRJDLVQX-UHFFFAOYSA-N 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 238000007914 intraventricular administration Methods 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000012804 iterative process Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 230000021633 leukocyte mediated immunity Effects 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 210000003928 nasal cavity Anatomy 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920001583 poly(oxyethylated polyols) Polymers 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229950008882 polysorbate Drugs 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 239000012857 radioactive material Substances 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 229960004641 rituximab Drugs 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 238000007860 single-cell PCR Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 239000000021 stimulant Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 229940036185 synagis Drugs 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- HFTAFOQKODTIJY-UHFFFAOYSA-N umbelliferone Natural products Cc1cc2C=CC(=O)Oc2cc1OCC=CC(C)(C)O HFTAFOQKODTIJY-UHFFFAOYSA-N 0.000 description 1
- 239000006216 vaginal suppository Substances 0.000 description 1
- 229940120293 vaginal suppository Drugs 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 229910052727 yttrium Inorganic materials 0.000 description 1
- VWQVUPCCIRVNHF-UHFFFAOYSA-N yttrium atom Chemical compound [Y] VWQVUPCCIRVNHF-UHFFFAOYSA-N 0.000 description 1
Images
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
- C07K16/1018—Orthomyxoviridae, e.g. influenza 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- 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
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- 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
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)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Communicable Diseases (AREA)
- Engineering & Computer Science (AREA)
- Pulmonology (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Oncology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Mycology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US8383808P | 2008-07-25 | 2008-07-25 | |
| US61/083,838 | 2008-07-25 | ||
| US18158209P | 2009-05-27 | 2009-05-27 | |
| US61/181,582 | 2009-05-27 | ||
| PCT/IB2009/006623 WO2010010467A2 (en) | 2008-07-25 | 2009-07-27 | Neutralizing anti-influenza a virus antibodies and uses thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2011528902A true JP2011528902A (ja) | 2011-12-01 |
| JP2011528902A5 JP2011528902A5 (enExample) | 2012-09-13 |
Family
ID=41570664
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011519253A Pending JP2011528902A (ja) | 2008-07-25 | 2009-07-27 | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
| JP2011519252A Active JP5607620B2 (ja) | 2008-07-25 | 2009-07-27 | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
| JP2014174221A Active JP6022515B2 (ja) | 2008-07-25 | 2014-08-28 | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011519252A Active JP5607620B2 (ja) | 2008-07-25 | 2009-07-27 | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
| JP2014174221A Active JP6022515B2 (ja) | 2008-07-25 | 2014-08-28 | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
Country Status (20)
| Country | Link |
|---|---|
| US (2) | US9340603B2 (enExample) |
| EP (2) | EP2313433A2 (enExample) |
| JP (3) | JP2011528902A (enExample) |
| KR (2) | KR20110049802A (enExample) |
| CN (2) | CN102216327A (enExample) |
| AU (2) | AU2009275227A1 (enExample) |
| BR (1) | BRPI0911699B8 (enExample) |
| CA (2) | CA2733218A1 (enExample) |
| CO (1) | CO6341572A2 (enExample) |
| CR (2) | CR20110079A (enExample) |
| EC (1) | ECSP11010823A (enExample) |
| ES (1) | ES2662519T3 (enExample) |
| GT (1) | GT201100023A (enExample) |
| IL (2) | IL210772A0 (enExample) |
| MA (1) | MA32577B1 (enExample) |
| MX (2) | MX2011000768A (enExample) |
| NZ (2) | NZ590891A (enExample) |
| RU (1) | RU2553325C2 (enExample) |
| WO (2) | WO2010010466A2 (enExample) |
| ZA (2) | ZA201101113B (enExample) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2011528901A (ja) * | 2008-07-25 | 2011-12-01 | インスティテュート・フォー・リサーチ・イン・バイオメディシン | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
| WO2015068781A1 (ja) * | 2013-11-06 | 2015-05-14 | 国立大学法人大阪大学 | インフルエンザウイルスａ型のグループ１に対して広域な中和活性を有する抗体 |
| JP2015518369A (ja) * | 2012-03-08 | 2015-07-02 | クルセル ホランド ベー ヴェー | Ｂ型インフルエンザウイルスに結合して中和することができるヒト結合分子およびその使用 |
| JP2016503413A (ja) * | 2012-11-13 | 2016-02-04 | ジェネンテック， インコーポレイテッド | 抗ヘマグルチニン抗体及び使用方法 |
| JP2022119757A (ja) * | 2013-10-02 | 2022-08-17 | メディミューン，エルエルシー | 抗ａ型インフルエンザ抗体の中和及びその使用 |
Families Citing this family (73)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2708221C (en) | 2007-12-06 | 2017-07-25 | Wayne A. Marasco | Antibodies against influenza virus and methods of use thereof |
| US8871207B2 (en) | 2008-07-25 | 2014-10-28 | Humabs, LLC | Neutralizing anti-influenza A virus antibodies and uses thereof |
| EP2545074A4 (en) * | 2010-03-08 | 2014-01-08 | Celltrion Inc | HUMAN MONOCLONAL ANTIBODIES MADE FROM HUMAN B-CELLS WITH NEUTRALIZING EFFECT AGAINST INFLUENZA A-VIRUS |
| CA2839421C (en) * | 2010-06-17 | 2019-12-03 | Trellis Bioscience, Llc | Antibodies useful in passive influenza immunization |
| US9534042B2 (en) * | 2010-09-03 | 2017-01-03 | Fujita Health University | Influenza virus-neutralizing antibody and screening method therefor |
| WO2012045001A2 (en) * | 2010-09-30 | 2012-04-05 | Vanderbilt University | Influenza virus antibodies and immunogens and uses therefor |
| EP2699688A1 (en) | 2011-04-20 | 2014-02-26 | The Trustees Of The University Of Pennsylvania | Regimens and compositions for aav-mediated passive immunization of airborne pathogens |
| US8961978B2 (en) * | 2011-07-14 | 2015-02-24 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza A viruses of phylogenetic group 1 and phylogenetic group 2 and influenza B viruses |
| LT3418300T (lt) * | 2011-07-18 | 2021-01-11 | Institute For Research In Biomedicine | Neutralizuojantys antikūnai prieš gripo virusą a ir jų panaudojimas |
| CN107417789A (zh) * | 2011-07-18 | 2017-12-01 | 生物医学学会 | 中和抗甲型流感病毒抗体及其用途 |
| AU2012289926A1 (en) * | 2011-08-03 | 2014-03-13 | Children's Medical Center Corporation | A broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza hemagglutinin |
| US9512202B2 (en) | 2011-08-27 | 2016-12-06 | University Of Zurich | Multi-strain-reactive antibodies for therapy and diagnosis of influenza |
| JP5998222B2 (ja) * | 2011-09-30 | 2016-09-28 | セルトリオン・インコーポレイテッド | ヒトｂ細胞で生産されたインフルエンザａウイルス中和活性を持つ結合分子 |
| CA2852474A1 (en) * | 2011-10-18 | 2013-04-25 | Emory University | Antibodies directed against influenza |
| KR20130059721A (ko) * | 2011-11-29 | 2013-06-07 | (주)셀트리온 | 인간 ｂ 세포에서 생산된 인플루엔자 ａ 바이러스 중화 활성을 가지는 결합 분자 |
| SG11201402780UA (en) | 2011-12-02 | 2014-10-30 | Aimm Therapeutics Bv | Influenza a virus specific antibodies |
| BR112014013640A8 (pt) * | 2011-12-05 | 2021-03-16 | Trellis Bioscience Llc | anticorpos úteis em imunização passiva para influenza |
| US20140335507A1 (en) * | 2011-12-12 | 2014-11-13 | Novartis Ag | Assays for influenza virus hemagglutinins |
| KR101749316B1 (ko) | 2011-12-15 | 2017-06-21 | (주) 에이프로젠 | Ｈ１ｎ１―감염된 환자들로부터 유도된 매우 잠재력 있는 넓은-스펙트럼 중화 단일클론 항체 및 이를 포함하는 바이러스의 치료용 조성물 |
| RU2502745C2 (ru) * | 2011-12-30 | 2013-12-27 | Общество с ограниченной ответственностью "Технофарма" | Наноантитело "anti-flu", рекомбинантные вирусные векторы и фармацевтические композиции для профилактики и терапии гриппа типа а |
| US9969794B2 (en) | 2012-05-10 | 2018-05-15 | Visterra, Inc. | HA binding agents |
| HK1207970A1 (en) | 2012-05-10 | 2016-02-19 | Massachusetts Institute Of Technology | Agents for influenza neutralization |
| CN103665155B (zh) * | 2012-09-14 | 2016-07-06 | 中国科学院上海生命科学研究院 | 一种抗流感病毒广谱中和性的中和分子1f2 |
| CN103665157B (zh) * | 2012-09-14 | 2016-06-29 | 中国科学院上海生命科学研究院 | 一种抗流感病毒广谱中和性的中和分子1c4 |
| CN103665156B (zh) * | 2012-09-14 | 2016-08-03 | 中国科学院上海生命科学研究院 | 一种抗流感病毒广谱中和性的结合分子3e1 |
| CN103665154B (zh) * | 2012-09-14 | 2016-08-03 | 中国科学院上海生命科学研究院 | 一种抗流感病毒广谱中和性的中和分子3c4 |
| IL241552B2 (en) * | 2013-03-14 | 2023-09-01 | Contrafect Corp | Preparation and methods based on neutralizing antibodies administered intranasally for increased therapeutic efficacy |
| KR20140118682A (ko) * | 2013-03-29 | 2014-10-08 | (주)셀트리온 | 2 이상의 인플루엔자 ａ 바이러스 중화 결합 분자를 포함하는 조성물 |
| EP2982691B1 (en) * | 2013-04-02 | 2020-05-06 | Xiamen University | Broad spectrum monoclonal antibody identifying ha1 structural domain of influenza virus hemagglutinin proteins |
| AU2015214146B2 (en) | 2014-02-04 | 2020-09-17 | Contrafect Corporation | Antibodies useful in passive influenza immunization, and compositions, combinations and methods for use thereof |
| US10639370B2 (en) | 2014-02-04 | 2020-05-05 | Contrafect Corporation | Antibodies useful in passive influenza immunization, and compositions, combinations and methods for use thereof |
| CN110642944B (zh) * | 2014-03-07 | 2021-06-11 | 神州细胞工程有限公司 | 一种中和人感染h7n9甲型流感病毒的抗体及其用途 |
| HRP20201530T1 (hr) | 2014-05-13 | 2020-12-11 | The Trustees Of The University Of Pennsylvania | Kompozicije koje sadrže aav koji eksprimira konstrukte dvojnih antitijela i njihove primjene |
| JP6495434B2 (ja) * | 2014-07-14 | 2019-04-03 | ザ ペン ステイト リサーチ ファンデーション | サーファクタントタンパク質ａ受容体を標的とする組成物及び方法 |
| CN113563462B (zh) | 2014-07-15 | 2024-08-13 | 免疫医疗有限责任公司 | 中和抗乙型流感抗体及其用途 |
| JPWO2016010160A1 (ja) * | 2014-07-18 | 2017-06-01 | 国立感染症研究所長 | 抗インフルエンザウイルス抗体及びその利用 |
| US20180008702A1 (en) * | 2014-12-05 | 2018-01-11 | Celltrion Inc. | Adjuvant composition containing at least one influenza virus neutralizing and binding molecule and vaccine composition containing same |
| WO2016089181A1 (ko) * | 2014-12-05 | 2016-06-09 | (주)셀트리온 | 1 이상의 인플루엔자 바이러스 중화 결합 분자를 포함하는 애주번트 조성물 및 이를 포함하는 백신 조성물 |
| TWI702229B (zh) * | 2014-12-19 | 2020-08-21 | 美商再生元醫藥公司 | 流行性感冒病毒血球凝集素之人類抗體 |
| US11535665B2 (en) | 2015-05-13 | 2022-12-27 | The Trustees Of The University Of Pennsylvania | AAV-mediated expression of anti-influenza antibodies and methods of use thereof |
| LT3303384T (lt) | 2015-06-01 | 2021-10-11 | Medimmune, Llc | Neutralizuojančios surišančios molekulės prieš gripą ir jų naudojimas |
| WO2017083627A1 (en) | 2015-11-13 | 2017-05-18 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| IL304940A (en) | 2016-01-13 | 2023-10-01 | Medimmune Llc | A method for treating type A influenza |
| US20170240617A1 (en) | 2016-02-24 | 2017-08-24 | Visterra, Inc. | Formulations of antibody molecules to influenza virus |
| US12065482B2 (en) * | 2016-08-10 | 2024-08-20 | Celltrion Inc. | Stable liquid pharmaceutical formulation of anti-influenza virus antibody |
| JP2017086068A (ja) * | 2016-10-31 | 2017-05-25 | インスティテュート・フォー・リサーチ・イン・バイオメディシンＩｎｓｔｉｔｕｔｅ Ｆｏｒ Ｒｅｓｅａｒｃｈ Ｉｎ Ｂｉｏｍｅｄｉｃｉｎｅ | Ａ型インフルエンザウイルス中和抗体及びその使用法 |
| RU2671477C2 (ru) * | 2016-12-30 | 2018-10-31 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Московский государственный университет имени М.В. Ломоносова" (МГУ) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pBiPr-ABIgA2m1F16-ht ДЛЯ ПОЛУЧЕНИЯ РЕКОМБИНАНТНОГО ИММУНОГЛОБУЛИНА А ИЗОТИПА IGA2m1 |
| RU2664184C2 (ru) * | 2016-12-30 | 2018-08-15 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Московский государственный университет имени М.В. Ломоносова" (МГУ) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pBiPr-ABIgA1FI6-Intht ДЛЯ ПОЛУЧЕНИЯ РЕКОМБИНАНТНОГО ИММУНОГЛОБУЛИНА А ИЗОТИПА IgA1 |
| RU2656142C1 (ru) * | 2016-12-30 | 2018-05-31 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Московский государственный университет имени М.В. Ломоносова" (МГУ) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pBiPr-ABIgA1FI6-ht ДЛЯ ПОЛУЧЕНИЯ РЕКОМБИНАНТНОГО ИММУНОГЛОБУЛИНА А ИЗОТИПА IGA1 |
| JOP20190200A1 (ar) | 2017-02-28 | 2019-08-27 | Univ Pennsylvania | تركيبات نافعة في معالجة ضمور العضل النخاعي |
| PT3589730T (pt) | 2017-02-28 | 2024-02-28 | Univ Pennsylvania | Vetor de vírus adenoassociado (aav) de clado f e suas utilizações |
| CN110573523A (zh) | 2017-02-28 | 2019-12-13 | 宾夕法尼亚州大学信托人 | 基于aav载体的流感疫苗 |
| JP7403733B2 (ja) | 2017-09-04 | 2023-12-25 | 国立感染症研究所長 | インフルエンザｈａスプリットワクチンの製造方法 |
| US11685934B2 (en) | 2017-09-18 | 2023-06-27 | Amyris, Inc. | Methods for genomic integration for Kluyveromyces host cells |
| BR112020005154A2 (pt) * | 2017-09-18 | 2020-09-15 | Amyris, Inc. | métodos de integração genômica em pichia e outras células hospedeiras |
| CN109988236B (zh) * | 2017-12-30 | 2022-04-01 | 中国科学院天津工业生物技术研究所 | 一种流感病毒抗体的应用 |
| HRP20220980T1 (hr) * | 2018-01-23 | 2022-11-11 | Janssen Vaccines & Prevention B.V. | Cjepiva protiv virusa influence i njihova uporaba |
| JP6622825B2 (ja) * | 2018-01-25 | 2019-12-18 | インスティテュート・フォー・リサーチ・イン・バイオメディシンＩｎｓｔｉｔｕｔｅ Ｆｏｒ Ｒｅｓｅａｒｃｈ Ｉｎ Ｂｉｏｍｅｄｉｃｉｎｅ | Ａ型インフルエンザウイルス中和抗体及びその使用法 |
| IL275884B2 (en) | 2018-01-26 | 2024-11-01 | Regeneron Pharma | Human antibodies to influenza hemagglutinin |
| TW202011986A (zh) | 2018-07-23 | 2020-04-01 | 公益財團法人日本健康科學振興財團 | 包含流感疫苗之組合物 |
| WO2020160560A2 (en) * | 2019-02-01 | 2020-08-06 | Novarock Biotherapeutics, Ltd. | Anti-claudin 18 antibodies and methods of use thereof |
| MY208974A (en) | 2019-03-04 | 2025-06-14 | Sumitomo Pharma Co Ltd | Method for preparing influenza ha split vaccine |
| US11230593B2 (en) | 2019-03-25 | 2022-01-25 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| JP2020048568A (ja) * | 2019-11-22 | 2020-04-02 | インスティテュート・フォー・リサーチ・イン・バイオメディシンＩｎｓｔｉｔｕｔｅ Ｆｏｒ Ｒｅｓｅａｒｃｈ Ｉｎ Ｂｉｏｍｅｄｉｃｉｎｅ | Ａ型インフルエンザウイルス中和抗体及びその使用法 |
| AU2020403133A1 (en) | 2019-12-11 | 2022-06-23 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| WO2021201677A1 (en) | 2020-04-01 | 2021-10-07 | Kiadis Pharma Intellectual Property B.V. | Compositions and methods targeting influenza |
| CN111825763B (zh) * | 2020-07-15 | 2022-04-19 | 扬州大学 | 流感病毒ha蛋白茎部特异性单克隆抗体及其制备方法和应用 |
| CN114181303B (zh) * | 2020-09-14 | 2022-12-23 | 东莞市朋志生物科技有限公司 | 抗甲型流感病毒的抗体和试剂盒 |
| TW202237850A (zh) | 2020-12-01 | 2022-10-01 | 賓州大學委員會 | 具有組織特異性靶向基序的新穎構成物及含有其之組成物 |
| WO2022232289A1 (en) | 2021-04-27 | 2022-11-03 | Generation Bio Co. | Non-viral dna vectors expressing therapeutic antibodies and uses thereof |
| WO2023177655A1 (en) | 2022-03-14 | 2023-09-21 | Generation Bio Co. | Heterologous prime boost vaccine compositions and methods of use |
| KR20240088574A (ko) | 2022-11-21 | 2024-06-20 | (주)샤페론 | 인플루엔자 바이러스에 대한 단일 도메인 항체 및 이의 용도 |
| CN119930806B (zh) * | 2025-01-21 | 2025-12-02 | 中国医学科学院病原生物学研究所 | 一种甲型流感病毒中和抗体及其应用 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007134327A2 (en) * | 2006-05-15 | 2007-11-22 | Sea Lane Biotechnologies, Llc. | Neutralizing antibodies to influenza viruses |
| WO2008028946A2 (en) * | 2006-09-07 | 2008-03-13 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| JP2011528901A (ja) * | 2008-07-25 | 2011-12-01 | インスティテュート・フォー・リサーチ・イン・バイオメディシン | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
Family Cites Families (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US630064A (en) * | 1899-02-10 | 1899-08-01 | William Martindale | Safety-hook. |
| NL154600B (nl) | 1971-02-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van specifiek bindende eiwitten en hun corresponderende bindbare stoffen. |
| US3817837A (en) | 1971-05-14 | 1974-06-18 | Syva Corp | Enzyme amplification assay |
| US3766162A (en) | 1971-08-24 | 1973-10-16 | Hoffmann La Roche | Barbituric acid antigens and antibodies specific therefor |
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| US4233402A (en) | 1978-04-05 | 1980-11-11 | Syva Company | Reagents and method employing channeling |
| JPS5896026A (ja) | 1981-10-30 | 1983-06-07 | Nippon Chemiphar Co Ltd | 新規ウロキナ−ゼ誘導体およびその製造法ならびにそれを含有する血栓溶解剤 |
| DE3380726D1 (en) | 1982-06-24 | 1989-11-23 | Japan Chem Res | Long-acting composition |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US4766106A (en) | 1985-06-26 | 1988-08-23 | Cetus Corporation | Solubilization of proteins for pharmaceutical compositions using polymer conjugation |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US4831175A (en) | 1986-09-05 | 1989-05-16 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Backbone polysubstituted chelates for forming a metal chelate-protein conjugate |
| RU2031941C1 (ru) * | 1991-03-14 | 1995-03-27 | Научно-исследовательский институт гриппа РАМН | Штамм вируса гриппа а(нini) для получения живой гриппозной интраназальной вакцины для взрослых и детей |
| US5595721A (en) | 1993-09-16 | 1997-01-21 | Coulter Pharmaceutical, Inc. | Radioimmunotherapy of lymphoma using anti-CD20 |
| DK1143006T3 (da) * | 1995-08-18 | 2008-07-14 | Morphosys Ip Gmbh | Vektorer/DNA-sekvenser fra humane kombinatoriske antistofbiblioteker |
| WO1998057993A1 (en) | 1997-06-19 | 1998-12-23 | The Regents Of The University Of California | Secretory immunoglobulin produced by single cells and methods for making and using same |
| MY133346A (en) | 1999-03-01 | 2007-11-30 | Biogen Inc | Kit for radiolabeling ligands with yttrium-90 |
| US20020102208A1 (en) | 1999-03-01 | 2002-08-01 | Paul Chinn | Radiolabeling kit and binding assay |
| US8101553B1 (en) * | 2000-02-22 | 2012-01-24 | Medical & Biological Laboratories Co., Ltd. | Antibody library |
| AU2003251809A1 (en) | 2002-07-11 | 2004-02-02 | The General Hospital Corporation | Polynucleotide and polypeptide fat metabolism regulators and uses thereof |
| CN1756562A (zh) * | 2003-03-07 | 2006-04-05 | 麦克公司 | 流感病毒疫苗 |
| RU2390351C2 (ru) * | 2003-08-11 | 2010-05-27 | Дзе Ресерч Фаундейшн Фо Макробайал Дизизес Оф Осака Юниверсити | Вакцина против вируса гриппа для введения через слизистую и способ предотвращения гриппа |
| WO2006124269A2 (en) * | 2005-05-16 | 2006-11-23 | Amgen Fremont Inc. | Human monoclonal antibodies that bind to very late antigen-1 for the treatment of inflammation and other disorders |
| EP2532677A1 (en) | 2005-10-21 | 2012-12-12 | Novartis AG | Human antibodies against il13 and therapeutic uses |
| TWI477602B (zh) | 2006-02-09 | 2015-03-21 | Educational Foundation Jichi Medical Univ | Novel viral vector |
| EP2769992B1 (en) * | 2006-10-02 | 2020-12-30 | Regeneron Pharmaceuticals, Inc. | High affinity human antibodies to human IL-4 receptor |
| WO2008066691A2 (en) * | 2006-11-08 | 2008-06-05 | Macrogenics West, Inc. | Tes7 and antibodies that bind thereto |
| EP1925318A1 (en) * | 2006-11-20 | 2008-05-28 | Paul-Ehrlich-Institut | Recombinant modified vaccinia virus Ankara (MVA)-based vaccine for the avian flu |
| RU2448979C2 (ru) | 2006-12-14 | 2012-04-27 | Ридженерон Фармасьютикалз, Инк. | Антитела человека к дельта-подобному лиганду-4 человека |
| GB0700133D0 (en) * | 2007-01-04 | 2007-02-14 | Humabs Llc | Human cytomegalovirus neutralising antibodies and use thereof |
| JP5346820B2 (ja) | 2007-03-13 | 2013-11-20 | エイチユーエムエイビーエス・リミテッド・ライアビリティ・カンパニー | Ｈ５ｎ１亜型ａ型インフルエンザウィルスに対する抗体 |
| ITTO20080204A1 (it) | 2008-03-17 | 2009-09-18 | Pomona Biotechnologies Llc | Anticorpi monoclonali atti a reagire con una pluralita di sottotipi del virus influenzale a |
| US8871207B2 (en) * | 2008-07-25 | 2014-10-28 | Humabs, LLC | Neutralizing anti-influenza A virus antibodies and uses thereof |
-
2009
- 2009-07-27 AU AU2009275227A patent/AU2009275227A1/en not_active Abandoned
- 2009-07-27 WO PCT/IB2009/006616 patent/WO2010010466A2/en not_active Ceased
- 2009-07-27 CA CA2733218A patent/CA2733218A1/en not_active Abandoned
- 2009-07-27 CA CA2731686A patent/CA2731686C/en active Active
- 2009-07-27 JP JP2011519253A patent/JP2011528902A/ja active Pending
- 2009-07-27 EP EP09759983A patent/EP2313433A2/en not_active Withdrawn
- 2009-07-27 NZ NZ590891A patent/NZ590891A/xx not_active IP Right Cessation
- 2009-07-27 RU RU2011105062/10A patent/RU2553325C2/ru active
- 2009-07-27 US US12/509,731 patent/US9340603B2/en active Active
- 2009-07-27 ES ES09745097.7T patent/ES2662519T3/es active Active
- 2009-07-27 EP EP09745097.7A patent/EP2313112B1/en active Active
- 2009-07-27 KR KR1020117003495A patent/KR20110049802A/ko not_active Withdrawn
- 2009-07-27 MX MX2011000768A patent/MX2011000768A/es not_active Application Discontinuation
- 2009-07-27 CN CN2009801329884A patent/CN102216327A/zh active Pending
- 2009-07-27 JP JP2011519252A patent/JP5607620B2/ja active Active
- 2009-07-27 CN CN200980132989.9A patent/CN102164613B/zh active Active
- 2009-07-27 US US12/509,835 patent/US8685402B2/en active Active
- 2009-07-27 WO PCT/IB2009/006623 patent/WO2010010467A2/en not_active Ceased
- 2009-07-27 BR BRPI0911699A patent/BRPI0911699B8/pt active IP Right Grant
- 2009-07-27 NZ NZ590890A patent/NZ590890A/xx not_active IP Right Cessation
- 2009-07-27 KR KR1020117003526A patent/KR101732056B1/ko active Active
- 2009-07-27 MX MX2011000767A patent/MX2011000767A/es active IP Right Grant
- 2009-07-27 AU AU2009275226A patent/AU2009275226B2/en active Active
-
2011
- 2011-01-20 IL IL210772A patent/IL210772A0/en unknown
- 2011-01-20 IL IL210771A patent/IL210771A0/en unknown
- 2011-01-21 GT GT201100023A patent/GT201100023A/es unknown
- 2011-02-09 CO CO11015221A patent/CO6341572A2/es active IP Right Grant
- 2011-02-11 ZA ZA2011/01113A patent/ZA201101113B/en unknown
- 2011-02-11 CR CR20110079A patent/CR20110079A/es unknown
- 2011-02-11 EC EC2011010823A patent/ECSP11010823A/es unknown
- 2011-02-14 ZA ZA2011/01150A patent/ZA201101150B/en unknown
- 2011-02-14 CR CR20110084A patent/CR20110084A/es unknown
- 2011-02-22 MA MA33633A patent/MA32577B1/fr unknown
-
2014
- 2014-08-28 JP JP2014174221A patent/JP6022515B2/ja active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007134327A2 (en) * | 2006-05-15 | 2007-11-22 | Sea Lane Biotechnologies, Llc. | Neutralizing antibodies to influenza viruses |
| WO2008028946A2 (en) * | 2006-09-07 | 2008-03-13 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| JP2011528901A (ja) * | 2008-07-25 | 2011-12-01 | インスティテュート・フォー・リサーチ・イン・バイオメディシン | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2011528901A (ja) * | 2008-07-25 | 2011-12-01 | インスティテュート・フォー・リサーチ・イン・バイオメディシン | 抗ａ型インフルエンザウイルス中和抗体およびその使用 |
| JP2015518369A (ja) * | 2012-03-08 | 2015-07-02 | クルセル ホランド ベー ヴェー | Ｂ型インフルエンザウイルスに結合して中和することができるヒト結合分子およびその使用 |
| JP2016503413A (ja) * | 2012-11-13 | 2016-02-04 | ジェネンテック， インコーポレイテッド | 抗ヘマグルチニン抗体及び使用方法 |
| JP2018108086A (ja) * | 2012-11-13 | 2018-07-12 | ジェネンテック， インコーポレイテッド | 抗ヘマグルチニン抗体及び使用方法 |
| JP2022119757A (ja) * | 2013-10-02 | 2022-08-17 | メディミューン，エルエルシー | 抗ａ型インフルエンザ抗体の中和及びその使用 |
| JP2024119930A (ja) * | 2013-10-02 | 2024-09-03 | メディミューン，エルエルシー | 抗ａ型インフルエンザ抗体の中和及びその使用 |
| JP7602508B2 (ja) | 2013-10-02 | 2024-12-18 | メディミューン，エルエルシー | 抗ａ型インフルエンザ抗体の中和及びその使用 |
| WO2015068781A1 (ja) * | 2013-11-06 | 2015-05-14 | 国立大学法人大阪大学 | インフルエンザウイルスａ型のグループ１に対して広域な中和活性を有する抗体 |
| JPWO2015068781A1 (ja) * | 2013-11-06 | 2017-03-09 | 国立大学法人大阪大学 | インフルエンザウイルスａ型のグループ１に対して広域な中和活性を有する抗体 |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP6022515B2 (ja) | 抗ａ型インフルエンザウイルス中和抗体およびその使用 | |
| US10815294B2 (en) | Neutralizing anti-influenza A virus antibodies and uses thereof | |
| US8871207B2 (en) | Neutralizing anti-influenza A virus antibodies and uses thereof | |
| JP2012504955A (ja) | デングウイルス中和抗体およびその使用 | |
| JP2020048568A (ja) | Ａ型インフルエンザウイルス中和抗体及びその使用法 | |
| JP6622825B2 (ja) | Ａ型インフルエンザウイルス中和抗体及びその使用法 | |
| JP2017086068A (ja) | Ａ型インフルエンザウイルス中和抗体及びその使用法 | |
| HK1260890B (zh) | 登革热病毒中和抗体及其用途 | |
| HK1259389A1 (en) | Neutralizing anti-influenza a virus antibodies and uses thereof | |
| HK1259389B (en) | Neutralizing anti-influenza a virus antibodies and uses thereof | |
| HK1247620A1 (zh) | 中和抗甲型流感病毒抗体及其用途 | |
| HK1161110B (en) | Neutralizing anti-influenza a virus antibodies and uses thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20120727 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20120727 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20140120 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20140225 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20140902 |