NZ585589A - Anti-rsv g protein antibodies - Google Patents
Anti-rsv g protein antibodiesInfo
- Publication number
- NZ585589A NZ585589A NZ585589A NZ58558908A NZ585589A NZ 585589 A NZ585589 A NZ 585589A NZ 585589 A NZ585589 A NZ 585589A NZ 58558908 A NZ58558908 A NZ 58558908A NZ 585589 A NZ585589 A NZ 585589A
- Authority
- NZ
- New Zealand
- Prior art keywords
- seq
- positions
- region
- rsv
- mab
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title description 37
- 102000004169 proteins and genes Human genes 0.000 title description 23
- 108091006027 G proteins Proteins 0.000 claims abstract description 74
- 102000030782 GTP binding Human genes 0.000 claims abstract description 74
- 108091000058 GTP-Binding Proteins 0.000 claims abstract description 74
- 239000012634 fragment Substances 0.000 claims abstract description 46
- 241000725643 Respiratory syncytial virus Species 0.000 claims description 81
- 210000004027 cell Anatomy 0.000 claims description 64
- 208000015181 infectious disease Diseases 0.000 claims description 31
- 238000000034 method Methods 0.000 claims description 23
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 claims description 14
- 238000000338 in vitro Methods 0.000 claims description 11
- 239000008194 pharmaceutical composition Substances 0.000 claims description 11
- 230000000295 complement effect Effects 0.000 claims description 8
- 239000003814 drug Substances 0.000 claims description 8
- 239000002773 nucleotide Substances 0.000 claims description 8
- 125000003729 nucleotide group Chemical group 0.000 claims description 8
- 208000037883 airway inflammation Diseases 0.000 claims description 7
- 108020004707 nucleic acids Proteins 0.000 claims description 5
- 102000039446 nucleic acids Human genes 0.000 claims description 5
- 150000007523 nucleic acids Chemical class 0.000 claims description 5
- 241000238631 Hexapoda Species 0.000 claims description 4
- 210000004962 mammalian cell Anatomy 0.000 claims description 4
- 230000000813 microbial effect Effects 0.000 claims description 4
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 4
- 230000009257 reactivity Effects 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 2
- 230000002708 enhancing effect Effects 0.000 claims description 2
- 239000008177 pharmaceutical agent Substances 0.000 claims 1
- 206010061603 Respiratory syncytial virus infection Diseases 0.000 abstract description 13
- 230000002163 immunogen Effects 0.000 abstract description 7
- 235000018102 proteins Nutrition 0.000 description 22
- 229940036185 synagis Drugs 0.000 description 21
- 241000700605 Viruses Species 0.000 description 20
- 238000003556 assay Methods 0.000 description 20
- 210000004072 lung Anatomy 0.000 description 19
- 230000003612 virological effect Effects 0.000 description 18
- 241000699670 Mus sp. Species 0.000 description 17
- 239000000203 mixture Substances 0.000 description 16
- 210000003719 b-lymphocyte Anatomy 0.000 description 14
- 238000003752 polymerase chain reaction Methods 0.000 description 13
- 108090000765 processed proteins & peptides Proteins 0.000 description 12
- 238000011282 treatment Methods 0.000 description 12
- 230000000694 effects Effects 0.000 description 11
- 150000001413 amino acids Chemical class 0.000 description 10
- 239000000427 antigen Substances 0.000 description 10
- 102000036639 antigens Human genes 0.000 description 10
- 108091007433 antigens Proteins 0.000 description 10
- 201000010099 disease Diseases 0.000 description 10
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 10
- 238000002474 experimental method Methods 0.000 description 9
- 102000004196 processed proteins & peptides Human genes 0.000 description 9
- 241001529936 Murinae Species 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 210000004602 germ cell Anatomy 0.000 description 8
- 238000006386 neutralization reaction Methods 0.000 description 8
- 241000282412 Homo Species 0.000 description 7
- 238000010240 RT-PCR analysis Methods 0.000 description 7
- 101150117115 V gene Proteins 0.000 description 7
- 230000002349 favourable effect Effects 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- 206010061218 Inflammation Diseases 0.000 description 6
- 230000003321 amplification Effects 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 230000004054 inflammatory process Effects 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 230000000069 prophylactic effect Effects 0.000 description 6
- 208000024891 symptom Diseases 0.000 description 6
- 230000001225 therapeutic effect Effects 0.000 description 6
- 238000011529 RT qPCR Methods 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 238000013507 mapping Methods 0.000 description 5
- 230000003472 neutralizing effect Effects 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 241000283707 Capra Species 0.000 description 4
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 4
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 4
- 108020005067 RNA Splice Sites Proteins 0.000 description 4
- 230000000875 corresponding effect Effects 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 230000000670 limiting effect Effects 0.000 description 4
- 230000003389 potentiating effect Effects 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 230000002035 prolonged effect Effects 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 229960005486 vaccine Drugs 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- UZOVYGYOLBIAJR-UHFFFAOYSA-N 4-isocyanato-4'-methyldiphenylmethane Chemical compound C1=CC(C)=CC=C1CC1=CC=C(N=C=O)C=C1 UZOVYGYOLBIAJR-UHFFFAOYSA-N 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 206010035664 Pneumonia Diseases 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- 125000003275 alpha amino acid group Chemical group 0.000 description 3
- 230000003110 anti-inflammatory effect Effects 0.000 description 3
- 230000000840 anti-viral effect Effects 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 108010060686 dual specificity phosphatase 12 Proteins 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 238000011081 inoculation Methods 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 3
- 238000011321 prophylaxis Methods 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 238000013207 serial dilution Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 229940124597 therapeutic agent Drugs 0.000 description 3
- 238000002255 vaccination Methods 0.000 description 3
- QDZOEBFLNHCSSF-PFFBOGFISA-N (2S)-2-[[(2R)-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-1-[(2R)-2-amino-5-carbamimidamidopentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-N-[(2R)-1-[[(2S)-1-[[(2R)-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]pentanediamide Chemical compound C([C@@H](C(=O)N[C@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(N)=O)NC(=O)[C@@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](N)CCCNC(N)=N)C1=CC=CC=C1 QDZOEBFLNHCSSF-PFFBOGFISA-N 0.000 description 2
- 102000004298 CX3C Chemokine Receptor 1 Human genes 0.000 description 2
- 108090000835 CX3C Chemokine Receptor 1 Proteins 0.000 description 2
- 108010078239 Chemokine CX3CL1 Proteins 0.000 description 2
- 102000019034 Chemokines Human genes 0.000 description 2
- 108010012236 Chemokines Proteins 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 208000007569 Giant Cell Tumors Diseases 0.000 description 2
- 101150008942 J gene Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 102000014171 Milk Proteins Human genes 0.000 description 2
- 108010011756 Milk Proteins Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241000831652 Salinivibrio sharmensis Species 0.000 description 2
- 102000007562 Serum Albumin Human genes 0.000 description 2
- 108010071390 Serum Albumin Proteins 0.000 description 2
- 102400000096 Substance P Human genes 0.000 description 2
- 101800003906 Substance P Proteins 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000010171 animal model Methods 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 230000002596 correlated effect Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 210000000265 leukocyte Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 229920000609 methyl cellulose Polymers 0.000 description 2
- 239000001923 methylcellulose Substances 0.000 description 2
- 235000010981 methylcellulose Nutrition 0.000 description 2
- 235000021239 milk protein Nutrition 0.000 description 2
- 238000010172 mouse model Methods 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 102000013415 peroxidase activity proteins Human genes 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 102000054765 polymorphisms of proteins Human genes 0.000 description 2
- 230000002028 premature Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000008707 rearrangement Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 230000003637 steroidlike Effects 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- WONRDHPFOHAWOG-UHFFFAOYSA-N 2-chloronaphthalen-1-ol Chemical compound C1=CC=C2C(O)=C(Cl)C=CC2=C1 WONRDHPFOHAWOG-UHFFFAOYSA-N 0.000 description 1
- 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 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 206010006448 Bronchiolitis Diseases 0.000 description 1
- 108090000565 Capsid Proteins Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 206010013975 Dyspnoeas Diseases 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 206010014950 Eosinophilia Diseases 0.000 description 1
- 102000013818 Fractalkine Human genes 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 101710180643 Leishmanolysin Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 239000012124 Opti-MEM Substances 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 208000037656 Respiratory Sounds Diseases 0.000 description 1
- 108010015329 Respiratory syncytial virus G glycoprotein Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 102000008233 Toll-Like Receptor 4 Human genes 0.000 description 1
- 108010060804 Toll-Like Receptor 4 Proteins 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 206010047924 Wheezing Diseases 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 108010088716 attachment protein G Proteins 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- -1 cationic lipid Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000002038 chemiluminescence detection Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 208000027744 congestion Diseases 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000000779 depleting effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000000499 gel Substances 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
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 230000005965 immune activity Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000006054 immunological memory Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 210000004969 inflammatory cell Anatomy 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 230000022023 interleukin-5 production Effects 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000000644 isotonic solution Substances 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 230000011268 leukocyte chemotaxis Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 238000007885 magnetic separation Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- CWWARWOPSKGELM-SARDKLJWSA-N methyl (2s)-2-[[(2s)-2-[[2-[[(2s)-2-[[(2s)-2-[[(2s)-5-amino-2-[[(2s)-5-amino-2-[[(2s)-1-[(2s)-6-amino-2-[[(2s)-1-[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-5 Chemical compound C([C@@H](C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)OC)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CCCN=C(N)N)C1=CC=CC=C1 CWWARWOPSKGELM-SARDKLJWSA-N 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 229960001521 motavizumab Drugs 0.000 description 1
- 230000008450 motivation Effects 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- KDWFDOFTPHDNJL-TUBOTVQJSA-N odn-2006 Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@H]2[C@H]([C@@H](O[C@@H]2COP(O)(=S)O[C@H]2[C@H]([C@@H](O[C@@H]2COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@H]2[C@H]([C@@H](O[C@@H]2COP(O)(=O)O[C@@H]2[C@H](O[C@H](C2)N2C(NC(=O)C(C)=C2)=O)COP(O)(=O)O[C@H]2[C@H]([C@@H](O[C@@H]2COP(O)(=S)O[C@H]2[C@H]([C@@H](O[C@@H]2COP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=C(C(NC(N)=N3)=O)N=C2)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=C(C(NC(N)=N3)=O)N=C2)OP(S)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C(N=C(N)C=C2)=O)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP(O)(=O)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)O)N2C3=C(C(NC(N)=N3)=O)N=C2)O)N2C(N=C(N)C=C2)=O)O)N2C3=C(C(NC(N)=N3)=O)N=C2)O)N2C3=C(C(NC(N)=N3)=O)N=C2)O)N2C(N=C(N)C=C2)=O)O)[C@@H](O)C1 KDWFDOFTPHDNJL-TUBOTVQJSA-N 0.000 description 1
- 229960000402 palivizumab Drugs 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 229940021222 peritoneal dialysis isotonic solution Drugs 0.000 description 1
- 230000000505 pernicious effect Effects 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
- 238000002360 preparation method Methods 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 201000009732 pulmonary eosinophilia Diseases 0.000 description 1
- 238000012207 quantitative assay Methods 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000012340 reverse transcriptase PCR Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000011808 rodent model Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 238000000954 titration curve Methods 0.000 description 1
- 239000012096 transfection reagent Substances 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1027—Paramyxoviridae, e.g. respiratory syncytial virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- 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
- 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
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- 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
- C07K2317/54—F(ab')2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/11011—Alpharetrovirus, e.g. avian leucosis virus
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Molecular Biology (AREA)
- Pulmonology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Engineering & Computer Science (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US46907P | 2007-10-25 | 2007-10-25 | |
| US8940108P | 2008-08-15 | 2008-08-15 | |
| PCT/US2008/081175 WO2009055711A2 (en) | 2007-10-25 | 2008-10-24 | Anti-rsv g protein antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ585589A true NZ585589A (en) | 2012-07-27 |
Family
ID=40580419
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ585589A NZ585589A (en) | 2007-10-25 | 2008-10-24 | Anti-rsv g protein antibodies |
Country Status (14)
| Country | Link |
|---|---|
| US (3) | US7736648B2 (enExample) |
| EP (1) | EP2214711B1 (enExample) |
| JP (2) | JP5808536B2 (enExample) |
| KR (1) | KR101671452B1 (enExample) |
| CN (1) | CN101808663B (enExample) |
| AU (1) | AU2008316703B2 (enExample) |
| BR (1) | BRPI0819210A2 (enExample) |
| CA (1) | CA2703667C (enExample) |
| IL (1) | IL205257A (enExample) |
| MX (1) | MX2010004482A (enExample) |
| NZ (1) | NZ585589A (enExample) |
| RU (1) | RU2526517C2 (enExample) |
| WO (1) | WO2009055711A2 (enExample) |
| ZA (1) | ZA201003131B (enExample) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040156888A1 (en) * | 2002-11-26 | 2004-08-12 | Jensen Gerard M. | Liposomal formulations |
| NZ585589A (en) * | 2007-10-25 | 2012-07-27 | Trellis Bioscience Inc | Anti-rsv g protein antibodies |
| WO2013095091A2 (en) | 2011-11-17 | 2013-06-27 | Aimm Therapeutics B.V. | Rsv g protein specific antibodies |
| US10131709B2 (en) | 2011-12-28 | 2018-11-20 | Immunoqure Ag | Nucleic acid molecules encoding monoclonal antibodies specific for IL-22 |
| AU2013206788B2 (en) * | 2011-12-28 | 2017-11-30 | Immunoqure Ag | Method of providing monoclonal auto-antibodies with desired specificity |
| US9546219B2 (en) | 2012-02-08 | 2017-01-17 | North Carolina State University | Treatment of allergic diseases with recombinant antibodies |
| TWI659968B (zh) | 2013-03-14 | 2019-05-21 | 再生元醫藥公司 | 針對呼吸道融合病毒ｆ蛋白質的人類抗體及其使用方法 |
| US10035842B2 (en) | 2013-04-15 | 2018-07-31 | Janssen Vaccines & Prevention B.V. | Human antibodies binding to RSV G proteins |
| CN111303278B (zh) * | 2013-04-15 | 2022-09-06 | 扬森疫苗与预防公司 | 结合到rsv g蛋白的人类抗体 |
| WO2014170257A1 (en) * | 2013-04-15 | 2014-10-23 | Crucell Holland B.V. | Human antibodies binding to rsv g protein |
| WO2015120474A1 (en) * | 2014-02-10 | 2015-08-13 | Igm Biosciences, Inc. | Iga multi-specific binding molecules |
| CN103911389A (zh) * | 2014-04-09 | 2014-07-09 | 南昌大学 | 一种检测人呼吸道合胞病毒抗体的g和f蛋白的制备方法 |
| RS62870B1 (sr) | 2014-12-05 | 2022-02-28 | Memorial Sloan Kettering Cancer Center | Himerni antigenski receptori sa ciljanim delovanjem na receptore spregnute sa g-proteinom i njihove upotrebe |
| SG10201913937QA (en) | 2014-12-05 | 2020-03-30 | Memorial Sloan Kettering Cancer Center | Antibodies targeting g-protein coupled receptor and methods of use |
| CN106496324B (zh) * | 2015-11-30 | 2020-01-14 | 天津昊免生物技术有限公司 | 一种抗呼吸道合胞病毒的全人源抗体 |
| CN105542003B (zh) * | 2016-03-01 | 2019-12-06 | 苏州博泰神州生物技术有限公司 | 一种针对rsv粘附g蛋白表面抗原的全人源单克隆抗体 |
| EP3538558A4 (en) | 2016-11-09 | 2020-07-15 | North Carolina State University | TREATMENT OF ALLERGIC DISEASES USING CHIMERIC PROTEIN |
| SG11201906682YA (en) | 2017-01-27 | 2019-08-27 | Ngm Biopharmaceuticals Inc | Glucagon receptor binding proteins and methods of use thereof |
| WO2019075400A1 (en) * | 2017-10-13 | 2019-04-18 | Trellis Bioscience, Llc | CONFORMATIONAL EPITOPES IN A CENTRAL PROTECTED REGION OF SYNCYTIAL RESPIRATORY VIRUS PROTEIN G |
| WO2019183437A1 (en) | 2018-03-23 | 2019-09-26 | North Carolina State University | Methods and compositions for antibody to high affinity receptor for ige |
| EP3829636A1 (en) | 2018-07-27 | 2021-06-09 | NGM Biopharmaceuticals, Inc. | Use of glucagon receptor antagonists with immunotherapeutic agent |
| JP2021534239A (ja) * | 2018-08-08 | 2021-12-09 | トレリス・バイオサイエンス，エルエルシー | Ｒｓｖの改善された受動的および能動的ワクチン |
| KR102679227B1 (ko) | 2019-02-28 | 2024-06-28 | 케이엠 바이올로직스 가부시키가이샤 | Rsv f/g 키메라 백신 |
| WO2021046390A1 (en) | 2019-09-06 | 2021-03-11 | Silgan White Cap LLC | Tethered, hinged closure |
| EP4031171A1 (en) * | 2019-09-20 | 2022-07-27 | Universiteit Antwerpen | A novel human respiratory syncytial virus strain and its use |
| EP4429966A1 (en) | 2021-11-08 | 2024-09-18 | Silgan White Cap LLC | Protrusion on container neck |
| TW202415409A (zh) * | 2022-08-02 | 2024-04-16 | 中國商諾納生物（蘇州）有限公司 | Msln抗體藥物複合體 |
| WO2025106427A1 (en) * | 2023-11-14 | 2025-05-22 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Neutralizing and protective monoclonal antibodies against respiratory syncytial virus (rsv) |
| WO2025194126A1 (en) * | 2024-03-15 | 2025-09-18 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Respiratory syncytial virus (rsv) g and f antibodies with high rsv-neutralizing potency |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3734263B2 (ja) * | 1993-05-25 | 2006-01-11 | ワイス・ホールディングズ・コーポレイション | 呼吸器シンシチウムウイルスに対するワクチンのためのアジュバント |
| US6020182A (en) * | 1996-07-12 | 2000-02-01 | Connaught Laboratories Limited | Subunit respiratory syncytial virus vaccine preparation |
| FR2766192B1 (fr) * | 1997-07-17 | 2001-07-13 | Pf Medicament | Epitopes du vrs et anticorps les comportant, utiles dans le diagnostic et la therapie |
| US6642062B2 (en) | 1998-09-03 | 2003-11-04 | Trellis Bioinformatics, Inc. | Multihued labels |
| US7083950B2 (en) | 1998-09-25 | 2006-08-01 | Regeneron Pharmaceuticals, Inc. | High affinity fusion proteins and therapeutic and diagnostic methods for use |
| CA2359776C (en) | 1999-01-22 | 2010-08-03 | Ralph A. Tripp | Methods for the prevention and treatment of diseases caused by an inflammatory response mediated by endogenous substance p by using anti-substance p antibodies |
| ATE412666T1 (de) * | 2000-10-18 | 2008-11-15 | Us Gov Health & Human Serv | Zusammensetzungen und verfahren zur modulierung von rsv-infektionen und -immunität |
| US7413868B2 (en) | 2003-11-05 | 2008-08-19 | Trellis Bioscience, Inc. | Use of particulate labels in bioanalyte detection methods |
| JP4736037B2 (ja) * | 2005-10-26 | 2011-07-27 | 株式会社イーベック | ヒトｇｍ−ｃｓｆに結合するヒトのモノクローナル抗体並びにその抗原結合部分 |
| CN1986569A (zh) * | 2005-12-23 | 2007-06-27 | 首都儿科研究所 | 人源抗呼吸道合胞病毒中和性基因工程Fab抗体 |
| WO2007094423A1 (ja) * | 2006-02-15 | 2007-08-23 | Evec Incorporated | ヒトサイトメガロウイルスに結合するヒトのモノクローナル抗体並びにその抗原結合部分 |
| KR20080113223A (ko) * | 2006-03-06 | 2008-12-29 | 심포젠 에이/에스 | 호흡기세포 융합 바이러스 감염 치료용 재조합 폴리클로날 항체 |
| CA2657123A1 (en) | 2006-07-12 | 2008-01-17 | Trellis Bioscience, Inc. | Cellspottm applications |
| NZ585589A (en) * | 2007-10-25 | 2012-07-27 | Trellis Bioscience Inc | Anti-rsv g protein antibodies |
-
2008
- 2008-10-24 NZ NZ585589A patent/NZ585589A/en not_active IP Right Cessation
- 2008-10-24 EP EP08841063.4A patent/EP2214711B1/en active Active
- 2008-10-24 US US12/258,260 patent/US7736648B2/en active Active
- 2008-10-24 AU AU2008316703A patent/AU2008316703B2/en active Active
- 2008-10-24 CN CN200880117420.0A patent/CN101808663B/zh not_active Expired - Fee Related
- 2008-10-24 RU RU2010120879/10A patent/RU2526517C2/ru not_active IP Right Cessation
- 2008-10-24 JP JP2010531283A patent/JP5808536B2/ja active Active
- 2008-10-24 CA CA2703667A patent/CA2703667C/en active Active
- 2008-10-24 BR BRPI0819210-3A patent/BRPI0819210A2/pt not_active IP Right Cessation
- 2008-10-24 MX MX2010004482A patent/MX2010004482A/es active IP Right Grant
- 2008-10-24 WO PCT/US2008/081175 patent/WO2009055711A2/en not_active Ceased
- 2008-10-24 KR KR1020107011433A patent/KR101671452B1/ko active Active
-
2010
- 2010-04-22 IL IL205257A patent/IL205257A/en not_active IP Right Cessation
- 2010-05-04 ZA ZA2010/03131A patent/ZA201003131B/en unknown
- 2010-05-12 US US12/778,933 patent/US8273354B2/en active Active
-
2012
- 2012-09-25 US US13/626,852 patent/US9321830B2/en active Active
-
2015
- 2015-01-16 JP JP2015006644A patent/JP2015078231A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| AU2008316703A2 (en) | 2010-07-22 |
| AU2008316703B2 (en) | 2012-09-27 |
| RU2010120879A (ru) | 2011-11-27 |
| JP5808536B2 (ja) | 2015-11-10 |
| CA2703667A1 (en) | 2009-04-30 |
| US8273354B2 (en) | 2012-09-25 |
| WO2009055711A2 (en) | 2009-04-30 |
| IL205257A (en) | 2014-12-31 |
| JP2015078231A (ja) | 2015-04-23 |
| US20090130120A1 (en) | 2009-05-21 |
| US20130034564A1 (en) | 2013-02-07 |
| ZA201003131B (en) | 2011-03-30 |
| WO2009055711A3 (en) | 2009-09-24 |
| US20100285022A1 (en) | 2010-11-11 |
| RU2526517C2 (ru) | 2014-08-20 |
| BRPI0819210A2 (pt) | 2015-06-23 |
| CN101808663A (zh) | 2010-08-18 |
| CN101808663B (zh) | 2015-09-30 |
| IL205257A0 (en) | 2010-12-30 |
| US7736648B2 (en) | 2010-06-15 |
| EP2214711A2 (en) | 2010-08-11 |
| KR20100091195A (ko) | 2010-08-18 |
| EP2214711A4 (en) | 2011-12-21 |
| US9321830B2 (en) | 2016-04-26 |
| MX2010004482A (es) | 2010-07-06 |
| EP2214711B1 (en) | 2018-08-15 |
| JP2011500091A (ja) | 2011-01-06 |
| KR101671452B1 (ko) | 2016-11-17 |
| AU2008316703A1 (en) | 2009-04-30 |
| CA2703667C (en) | 2015-12-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2008316703B2 (en) | Anti-RSV G protein antibodies | |
| US7879329B2 (en) | Recombinant antibodies for treatment of respiratory syncytial virus infections | |
| US20240101646A1 (en) | Sars-cov-2 coronavirus antibodies and uses thereof | |
| US9688744B2 (en) | High affinity human antibodies to human cytomegalovirus (CMV) GB protein | |
| CN115515976A (zh) | 冠状病毒抗体 | |
| CN114174331A (zh) | 结合人类偏肺病毒融合蛋白的抗体及其用途 | |
| TW202306980A (zh) | 一種呼吸道融合病毒的抗體及其應用 | |
| EP4442276A1 (en) | Combined antibodies against sarbecoviruses and uses thereof | |
| CN116162154B (zh) | 抗人巨细胞病毒抗体及其用途 | |
| US20250026814A1 (en) | Polypeptides for detection and treatment of coronavirus infection | |
| CN116987183A (zh) | 抗呼吸道合胞病毒中和性抗体及其用途 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PSEA | Patent sealed | ||
| RENW | Renewal (renewal fees accepted) |
Free format text: PATENT RENEWED FOR 3 YEARS UNTIL 24 OCT 2015 BY CPA GLOBAL Effective date: 20130129 |
|
| RENW | Renewal (renewal fees accepted) |
Free format text: PATENT RENEWED FOR 1 YEAR UNTIL 24 OCT 2016 BY CPA GLOBAL Effective date: 20150918 |
|
| LAPS | Patent lapsed |