EA027054B1 - Связывающие молекулы человека, способные нейтрализовать вирусы гриппа a филогенетической группы 1 и филогенетической группы 2 и вирусы гриппа b - Google Patents
Связывающие молекулы человека, способные нейтрализовать вирусы гриппа a филогенетической группы 1 и филогенетической группы 2 и вирусы гриппа b Download PDFInfo
- Publication number
- EA027054B1 EA027054B1 EA201490288A EA201490288A EA027054B1 EA 027054 B1 EA027054 B1 EA 027054B1 EA 201490288 A EA201490288 A EA 201490288A EA 201490288 A EA201490288 A EA 201490288A EA 027054 B1 EA027054 B1 EA 027054B1
- Authority
- EA
- Eurasian Patent Office
- Prior art keywords
- region
- influenza
- heavy chain
- binding
- light chain
- Prior art date
Links
- 230000027455 binding Effects 0.000 title claims abstract description 421
- 241000712431 Influenza A virus Species 0.000 title claims abstract description 52
- 230000003472 neutralizing effect Effects 0.000 title claims abstract description 37
- 241000713196 Influenza B virus Species 0.000 title abstract description 32
- 101710154606 Hemagglutinin Proteins 0.000 claims abstract description 115
- 101710093908 Outer capsid protein VP4 Proteins 0.000 claims abstract description 115
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 claims abstract description 115
- 101710176177 Protein A56 Proteins 0.000 claims abstract description 115
- 239000000185 hemagglutinin Substances 0.000 claims abstract description 107
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 53
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 46
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 46
- 238000011282 treatment Methods 0.000 claims abstract description 27
- 108090000623 proteins and genes Proteins 0.000 claims description 52
- 239000012634 fragment Substances 0.000 claims description 51
- 239000000427 antigen Substances 0.000 claims description 46
- 108091007433 antigens Proteins 0.000 claims description 46
- 102000036639 antigens Human genes 0.000 claims description 46
- 102000004169 proteins and genes Human genes 0.000 claims description 44
- 239000008194 pharmaceutical composition Substances 0.000 claims description 28
- 206010022000 influenza Diseases 0.000 claims description 27
- 208000037798 influenza B Diseases 0.000 claims description 18
- 230000000069 prophylactic effect Effects 0.000 claims description 17
- 230000001225 therapeutic effect Effects 0.000 claims description 16
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 14
- 230000002401 inhibitory effect Effects 0.000 claims description 6
- 101100274255 Arabidopsis thaliana CHER1 gene Proteins 0.000 claims 6
- 101100256906 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) SIC1 gene Proteins 0.000 claims 6
- 101000709238 Homo sapiens Serine/threonine-protein kinase SIK1 Proteins 0.000 claims 3
- 101000709250 Homo sapiens Serine/threonine-protein kinase SIK2 Proteins 0.000 claims 3
- 101000654491 Homo sapiens Serine/threonine-protein kinase SIK3 Proteins 0.000 claims 3
- 102100032771 Serine/threonine-protein kinase SIK1 Human genes 0.000 claims 3
- 102100034377 Serine/threonine-protein kinase SIK2 Human genes 0.000 claims 3
- 102100031445 Serine/threonine-protein kinase SIK3 Human genes 0.000 claims 3
- 101100495992 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) CIK1 gene Proteins 0.000 claims 2
- 241000712461 unidentified influenza virus Species 0.000 abstract description 91
- 239000000203 mixture Substances 0.000 abstract description 35
- 238000003745 diagnosis Methods 0.000 abstract description 12
- 238000011321 prophylaxis Methods 0.000 abstract description 8
- 210000004027 cell Anatomy 0.000 description 92
- 125000003275 alpha amino acid group Chemical group 0.000 description 88
- 235000013305 food Nutrition 0.000 description 45
- 238000000034 method Methods 0.000 description 41
- 235000018102 proteins Nutrition 0.000 description 41
- 108020004414 DNA Proteins 0.000 description 33
- 241000700605 Viruses Species 0.000 description 32
- 229940127121 immunoconjugate Drugs 0.000 description 32
- 239000013598 vector Substances 0.000 description 31
- 208000015181 infectious disease Diseases 0.000 description 29
- 125000003729 nucleotide group Chemical group 0.000 description 28
- 239000002773 nucleotide Chemical group 0.000 description 24
- 108090000765 processed proteins & peptides Proteins 0.000 description 22
- 235000001014 amino acid Nutrition 0.000 description 20
- 241000282412 Homo Species 0.000 description 18
- 239000000872 buffer Substances 0.000 description 18
- 239000003795 chemical substances by application Substances 0.000 description 18
- 102000004196 processed proteins & peptides Human genes 0.000 description 18
- 229940024606 amino acid Drugs 0.000 description 17
- 150000001413 amino acids Chemical class 0.000 description 17
- 239000003814 drug Substances 0.000 description 17
- 108060003951 Immunoglobulin Proteins 0.000 description 16
- 102000018358 immunoglobulin Human genes 0.000 description 16
- 238000002360 preparation method Methods 0.000 description 16
- 241000699670 Mus sp. Species 0.000 description 15
- 230000000890 antigenic effect Effects 0.000 description 15
- 208000037797 influenza A Diseases 0.000 description 15
- 239000002609 medium Substances 0.000 description 15
- 239000000523 sample Substances 0.000 description 14
- 239000000126 substance Substances 0.000 description 14
- 230000009385 viral infection Effects 0.000 description 14
- 241000894006 Bacteria Species 0.000 description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 description 13
- 241000196324 Embryophyta Species 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 239000000047 product Substances 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 11
- 230000004927 fusion Effects 0.000 description 11
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 10
- 241001465754 Metazoa Species 0.000 description 10
- 101100439738 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) CIC1 gene Proteins 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 230000008859 change Effects 0.000 description 10
- 230000003321 amplification Effects 0.000 description 9
- 238000005259 measurement Methods 0.000 description 9
- 230000001404 mediated effect Effects 0.000 description 9
- 238000003199 nucleic acid amplification method Methods 0.000 description 9
- 229940124597 therapeutic agent Drugs 0.000 description 9
- 230000009261 transgenic effect Effects 0.000 description 9
- 229940098773 bovine serum albumin Drugs 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 8
- 230000035772 mutation Effects 0.000 description 8
- 229920001184 polypeptide Polymers 0.000 description 8
- 239000000725 suspension Substances 0.000 description 8
- 239000002202 Polyethylene glycol Substances 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 230000037396 body weight Effects 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 239000000463 material Substances 0.000 description 7
- 229920001223 polyethylene glycol Polymers 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 230000009466 transformation Effects 0.000 description 7
- 102100032860 Cell division cycle 5-like protein Human genes 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 101000868318 Homo sapiens Cell division cycle 5-like protein Proteins 0.000 description 6
- 241000124008 Mammalia Species 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 229920001213 Polysorbate 20 Polymers 0.000 description 6
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 6
- 239000003443 antiviral agent Substances 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 210000004602 germ cell Anatomy 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 238000002823 phage display Methods 0.000 description 6
- 108091033319 polynucleotide Proteins 0.000 description 6
- 102000040430 polynucleotide Human genes 0.000 description 6
- 239000002157 polynucleotide Substances 0.000 description 6
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 6
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 6
- 238000012545 processing Methods 0.000 description 6
- 238000003127 radioimmunoassay Methods 0.000 description 6
- 230000001932 seasonal effect Effects 0.000 description 6
- 230000009870 specific binding Effects 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 5
- 101000870565 Pisum sativum Glutathione reductase, cytosolic Proteins 0.000 description 5
- 238000007792 addition Methods 0.000 description 5
- 210000003719 b-lymphocyte Anatomy 0.000 description 5
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 239000012636 effector Substances 0.000 description 5
- 229960001031 glucose Drugs 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 210000003128 head Anatomy 0.000 description 5
- -1 isole 4 027054 zine Chemical compound 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- 230000002265 prevention Effects 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 241000701447 unidentified baculovirus Species 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 4
- 208000000059 Dyspnea Diseases 0.000 description 4
- 206010013975 Dyspnoeas Diseases 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- 101000972485 Homo sapiens Lupus La protein Proteins 0.000 description 4
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 4
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 4
- 102100022742 Lupus La protein Human genes 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 4
- 229960000723 ampicillin Drugs 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000004132 cross linking Methods 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 210000001163 endosome Anatomy 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- 230000003053 immunization Effects 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 230000001965 increasing effect Effects 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 239000000543 intermediate Substances 0.000 description 4
- 231100000518 lethal Toxicity 0.000 description 4
- 230000001665 lethal effect Effects 0.000 description 4
- 230000034217 membrane fusion Effects 0.000 description 4
- 238000006386 neutralization reaction Methods 0.000 description 4
- 229960003752 oseltamivir Drugs 0.000 description 4
- VSZGPKBBMSAYNT-RRFJBIMHSA-N oseltamivir Chemical compound CCOC(=O)C1=C[C@@H](OC(CC)CC)[C@H](NC(C)=O)[C@@H](N)C1 VSZGPKBBMSAYNT-RRFJBIMHSA-N 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 208000013220 shortness of breath Diseases 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 241001500350 Influenzavirus B Species 0.000 description 3
- 101001071620 Pisum sativum Glutathione reductase, chloroplastic/mitochondrial Proteins 0.000 description 3
- 206010037742 Rabies Diseases 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 239000004098 Tetracycline Substances 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 230000000840 anti-viral effect Effects 0.000 description 3
- 239000012472 biological sample Substances 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 239000012707 chemical precursor Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000004590 computer program Methods 0.000 description 3
- 230000000120 cytopathologic effect Effects 0.000 description 3
- 229940039227 diagnostic agent Drugs 0.000 description 3
- 239000000032 diagnostic agent Substances 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 229960003971 influenza vaccine Drugs 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 231100000252 nontoxic Toxicity 0.000 description 3
- 230000003000 nontoxic effect Effects 0.000 description 3
- 238000007911 parenteral administration Methods 0.000 description 3
- 210000004180 plasmocyte Anatomy 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 229920003023 plastic Polymers 0.000 description 3
- 230000003449 preventive effect Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 230000002195 synergetic effect Effects 0.000 description 3
- 229960002180 tetracycline Drugs 0.000 description 3
- 229930101283 tetracycline Natural products 0.000 description 3
- 235000019364 tetracycline Nutrition 0.000 description 3
- 150000003522 tetracyclines Chemical class 0.000 description 3
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 description 2
- UBCHPRBFMUDMNC-UHFFFAOYSA-N 1-(1-adamantyl)ethanamine Chemical compound C1C(C2)CC3CC2CC1(C(N)C)C3 UBCHPRBFMUDMNC-UHFFFAOYSA-N 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- 102100035309 GRIP and coiled-coil domain-containing protein 1 Human genes 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 101001024398 Homo sapiens GRIP and coiled-coil domain-containing protein 1 Proteins 0.000 description 2
- 101000703761 Homo sapiens Leucine-rich repeat protein SHOC-2 Proteins 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 102100031956 Leucine-rich repeat protein SHOC-2 Human genes 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 206010057249 Phagocytosis Diseases 0.000 description 2
- 108010004729 Phycoerythrin Proteins 0.000 description 2
- 239000004698 Polyethylene Substances 0.000 description 2
- 101900083372 Rabies virus Glycoprotein Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 108700019146 Transgenes Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical compound C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- DKNWSYNQZKUICI-UHFFFAOYSA-N amantadine Chemical compound C1C(C2)CC3CC2CC1(N)C3 DKNWSYNQZKUICI-UHFFFAOYSA-N 0.000 description 2
- 229960003805 amantadine Drugs 0.000 description 2
- 238000010171 animal model Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 210000004436 artificial bacterial chromosome Anatomy 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 239000006143 cell culture medium Substances 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 230000001268 conjugating effect Effects 0.000 description 2
- 230000021615 conjugation Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 239000012502 diagnostic product Substances 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 229940042406 direct acting antivirals neuraminidase inhibitors Drugs 0.000 description 2
- 239000002552 dosage form Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000035931 haemagglutination Effects 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000007937 lozenge Substances 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 229910021645 metal ion Inorganic materials 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 230000008782 phagocytosis Effects 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 2
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
- 239000000941 radioactive substance Substances 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 229960000888 rimantadine Drugs 0.000 description 2
- 101150079036 rnc gene Proteins 0.000 description 2
- 229920006395 saturated elastomer Polymers 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 239000002911 sialidase inhibitor Substances 0.000 description 2
- 239000008174 sterile solution Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 230000004580 weight loss Effects 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- 229960001028 zanamivir Drugs 0.000 description 2
- ARAIBEBZBOPLMB-UFGQHTETSA-N zanamivir Chemical compound CC(=O)N[C@@H]1[C@@H](N=C(N)N)C=C(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO ARAIBEBZBOPLMB-UFGQHTETSA-N 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 1
- 101150018711 AASS gene Proteins 0.000 description 1
- 102100037651 AP-2 complex subunit sigma Human genes 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 102220478542 Apoptosis regulator Bcl-2_E53A_mutation Human genes 0.000 description 1
- 241001081972 Arctium medians Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000182988 Assa Species 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 229910004383 CaII Inorganic materials 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 101100246998 Cavia porcellus QSOX1 gene Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101100365490 Drosophila melanogaster Jon99Ci gene Proteins 0.000 description 1
- 241000305071 Enterobacterales Species 0.000 description 1
- 101710104662 Enterotoxin type C-3 Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 102100030844 Exocyst complex component 1 Human genes 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 102100028617 GRIP and coiled-coil domain-containing protein 2 Human genes 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 239000001828 Gelatine Substances 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010015899 Glycopeptides Proteins 0.000 description 1
- 102000002068 Glycopeptides Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 102100036738 Guanine nucleotide-binding protein subunit alpha-11 Human genes 0.000 description 1
- 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 1
- 108700024827 HOC1 Proteins 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 101000806914 Homo sapiens AP-2 complex subunit sigma Proteins 0.000 description 1
- 101001058870 Homo sapiens GRIP and coiled-coil domain-containing protein 2 Proteins 0.000 description 1
- 101001072407 Homo sapiens Guanine nucleotide-binding protein subunit alpha-11 Proteins 0.000 description 1
- 101000601048 Homo sapiens Nidogen-2 Proteins 0.000 description 1
- 101000642195 Homo sapiens Protein turtle homolog A Proteins 0.000 description 1
- 101000843236 Homo sapiens Testis-specific H1 histone Proteins 0.000 description 1
- 229940124873 Influenza virus vaccine Drugs 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 239000004909 Moisturizer Substances 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
- 241000282341 Mustela putorius furo Species 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 102100037371 Nidogen-2 Human genes 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000702437 Parvovirus H3 Species 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 229920002584 Polyethylene Glycol 6000 Polymers 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102100033219 Protein turtle homolog A Human genes 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- PZYAYFPGUMSVJW-UHFFFAOYSA-N SSSSSSS Chemical compound SSSSSSS PZYAYFPGUMSVJW-UHFFFAOYSA-N 0.000 description 1
- USZAOTPETFYQDD-UHFFFAOYSA-N SSSSSSSSSSSSSSSSSSSSSSSSSSS Chemical compound SSSSSSSSSSSSSSSSSSSSSSSSSSS USZAOTPETFYQDD-UHFFFAOYSA-N 0.000 description 1
- 101100068077 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GCN2 gene Proteins 0.000 description 1
- 101100178273 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) HOC1 gene Proteins 0.000 description 1
- 240000005499 Sasa Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 101000882406 Staphylococcus aureus Enterotoxin type C-1 Proteins 0.000 description 1
- JDZPLYBLBIKFHJ-UHFFFAOYSA-N Sulfamoyldapsone Chemical compound C1=CC(N)=CC=C1S(=O)(=O)C1=CC=C(N)C=C1S(N)(=O)=O JDZPLYBLBIKFHJ-UHFFFAOYSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 0.000 description 1
- 102100031010 Testis-specific H1 histone Human genes 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-N Thiophosphoric acid Chemical class OP(O)(S)=O RYYWUUFWQRZTIU-UHFFFAOYSA-N 0.000 description 1
- 108020004440 Thymidine kinase Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 206010058874 Viraemia Diseases 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 230000010530 Virus Neutralization Effects 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 229940100198 alkylating agent Drugs 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- VEZXCJBBBCKRPI-UHFFFAOYSA-N beta-propiolactone Chemical compound O=C1CCO1 VEZXCJBBBCKRPI-UHFFFAOYSA-N 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 150000004657 carbamic acid derivatives Chemical class 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- ZYWFEOZQIUMEGL-UHFFFAOYSA-N chloroform;3-methylbutan-1-ol;phenol Chemical compound ClC(Cl)Cl.CC(C)CCO.OC1=CC=CC=C1 ZYWFEOZQIUMEGL-UHFFFAOYSA-N 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 231100000517 death Toxicity 0.000 description 1
- 239000003405 delayed action preparation Substances 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 239000008298 dragée Substances 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 210000002257 embryonic structure Anatomy 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000005038 ethylene vinyl acetate Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 201000001267 familial hypocalciuric hypercalcemia 2 Diseases 0.000 description 1
- 201000001265 familial hypocalciuric hypercalcemia 3 Diseases 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 210000003608 fece Anatomy 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 235000013355 food flavoring agent Nutrition 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 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
- 239000008187 granular material Substances 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 239000007902 hard capsule Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000003067 hemagglutinative effect Effects 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 238000011532 immunohistochemical staining Methods 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 108700010900 influenza virus proteins Proteins 0.000 description 1
- 239000003978 infusion fluid Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 150000002484 inorganic compounds Chemical group 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 238000005305 interferometry Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000010410 layer Substances 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 239000003589 local anesthetic agent Substances 0.000 description 1
- 229960005015 local anesthetics Drugs 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- YACKEPLHDIMKIO-UHFFFAOYSA-N methylphosphonic acid Chemical class CP(O)(O)=O YACKEPLHDIMKIO-UHFFFAOYSA-N 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 230000001333 moisturizer Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 210000001989 nasopharynx Anatomy 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 239000006186 oral dosage form Substances 0.000 description 1
- 150000002894 organic compounds Chemical group 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 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 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000004091 panning Methods 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 229940124531 pharmaceutical excipient Drugs 0.000 description 1
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 150000008298 phosphoramidates Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000013081 phylogenetic analysis Methods 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 229960000380 propiolactone Drugs 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 208000023504 respiratory system disease Diseases 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 101150008449 ser3 gene Proteins 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 125000005629 sialic acid group Chemical group 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 150000003384 small molecules Chemical group 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- AXXJTNXVUHVOJW-UHFFFAOYSA-M sodium;5-pentan-2-yl-5-prop-2-enylpyrimidin-3-ide-2,4,6-trione Chemical compound [Na+].CCCC(C)C1(CC=C)C(=O)NC(=O)[N-]C1=O AXXJTNXVUHVOJW-UHFFFAOYSA-M 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 229940043517 specific immunoglobulins Drugs 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000004350 spin decoupling difference spectroscopy Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 229940061367 tamiflu Drugs 0.000 description 1
- 230000004797 therapeutic response Effects 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 150000007944 thiolates Chemical class 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 230000002110 toxicologic effect Effects 0.000 description 1
- 231100000759 toxicological effect Toxicity 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
- 230000005026 transcription initiation Effects 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 229910021642 ultra pure water Inorganic materials 0.000 description 1
- 239000012498 ultrapure water Substances 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 230000017260 vegetative to reproductive phase transition of meristem Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000007501 viral attachment Effects 0.000 description 1
- 230000008299 viral mechanism Effects 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 210000005253 yeast cell Anatomy 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
- C07K16/1018—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
- A61K39/42—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum viral
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56983—Viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- 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
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
-
- 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
- C07K2317/50—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
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- 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
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/005—Assays involving biological materials from specific organisms or of a specific nature from viruses
- G01N2333/08—RNA viruses
- G01N2333/11—Orthomyxoviridae, e.g. influenza virus
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Pulmonology (AREA)
- Microbiology (AREA)
- Communicable Diseases (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Biotechnology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Physics & Mathematics (AREA)
- Zoology (AREA)
- General Chemical & Material Sciences (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Cell Biology (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161572417P | 2011-07-14 | 2011-07-14 | |
| EP11173953 | 2011-07-14 | ||
| PCT/EP2012/063637 WO2013007770A1 (en) | 2011-07-14 | 2012-07-12 | Human binding molecules capable of neutralizing influenza a viruses of phylogenetic group 1 and phylogenetic group 2 and influenza b viruses |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA201490288A1 EA201490288A1 (ru) | 2014-05-30 |
| EA027054B1 true EA027054B1 (ru) | 2017-06-30 |
Family
ID=47505543
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA201490288A EA027054B1 (ru) | 2011-07-14 | 2012-07-12 | Связывающие молекулы человека, способные нейтрализовать вирусы гриппа a филогенетической группы 1 и филогенетической группы 2 и вирусы гриппа b |
Country Status (18)
| Country | Link |
|---|---|
| US (2) | US8961978B2 (enExample) |
| EP (1) | EP2731967B1 (enExample) |
| JP (1) | JP5683752B2 (enExample) |
| KR (1) | KR101941724B1 (enExample) |
| CN (1) | CN103906763B (enExample) |
| AU (1) | AU2012282504B2 (enExample) |
| BR (1) | BR112014000263B1 (enExample) |
| CA (1) | CA2838999C (enExample) |
| DK (1) | DK2731967T3 (enExample) |
| EA (1) | EA027054B1 (enExample) |
| ES (1) | ES2608321T3 (enExample) |
| HR (1) | HRP20161740T1 (enExample) |
| IL (1) | IL230222A (enExample) |
| IN (1) | IN2014CN00953A (enExample) |
| MX (1) | MX346206B (enExample) |
| MY (1) | MY166282A (enExample) |
| PH (1) | PH12013502479A1 (enExample) |
| WO (1) | WO2013007770A1 (enExample) |
Families Citing this family (50)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK2731967T3 (en) | 2011-07-14 | 2017-01-16 | Janssen Vaccines & Prevention Bv | HUMAN BINDING MOLECULES CAPABLE OF NEUTRALIZING INFLUENZA A VIRUS FROM PHYLOGENETIC GROUP 1 AND PHYLOGENETIC GROUP 2 AND INFLUENZA B VIRUS |
| JP6294828B2 (ja) | 2011-11-28 | 2018-03-14 | ヤンセン ファッシンズ アンド プリベンション ベーフェーＪａｎｓｓｅｎ Ｖａｃｃｉｎｅｓ ＆ Ｐｒｅｖｅｎｔｉｏｎ Ｂ．Ｖ． | インフルエンザウイルスワクチンおよびその使用 |
| US10654915B2 (en) | 2011-12-05 | 2020-05-19 | Trellis Bioscience, Llc | Antibodies useful in passive influenza immunization |
| US9969794B2 (en) | 2012-05-10 | 2018-05-15 | Visterra, Inc. | HA binding agents |
| US9649375B2 (en) * | 2013-03-14 | 2017-05-16 | The Administrators Of The Tulane Educational Fund | Immunogenic peptide conjugate and method for inducing an anti-influenza therapeutic antibody response therewith |
| BR112015022623A2 (pt) * | 2013-03-14 | 2017-07-18 | Contrafect Corp | composição e métodos baseados em anticorpos neutralizantes, administrados por via intranasal para eficácia terapêutica melhorada |
| KR20140118682A (ko) * | 2013-03-29 | 2014-10-08 | (주)셀트리온 | 2 이상의 인플루엔자 ａ 바이러스 중화 결합 분자를 포함하는 조성물 |
| MY190097A (en) | 2013-05-30 | 2022-03-28 | Janssen Vaccines & Prevention Bv | Influenza virus vaccines and uses thereof |
| DK3052192T3 (da) | 2013-10-02 | 2020-09-28 | Medimmune Llc | Neutraliserende anti-influenza a-antistoffer og anvendelser deraf |
| RU2682049C2 (ru) * | 2014-01-27 | 2019-03-14 | Дженентек, Инк. | Лечение вируса гриппа а h7n9 |
| US10639370B2 (en) | 2014-02-04 | 2020-05-05 | Contrafect Corporation | Antibodies useful in passive influenza immunization, and compositions, combinations and methods for use thereof |
| CN106795216B (zh) * | 2014-02-04 | 2021-04-20 | 抗非特公司 | 可用于被动流感免疫的抗体及其组合物、组合和使用方法 |
| CN105992772A (zh) * | 2014-02-10 | 2016-10-05 | Igm生命科学股份有限公司 | IgA多特异性结合分子 |
| MX2016012530A (es) | 2014-03-27 | 2017-01-05 | Genentech Inc | Anticuerpos de hemaglutinina contra el virus de la influenza b y metodos de uso. |
| KR101628331B1 (ko) * | 2014-03-28 | 2016-06-08 | 주식회사 녹십자엠에스 | 인플루엔자 a 바이러스 특이적 단클론 항체 및 이를 이용한 인플루엔자 감염 치료 및 진단 방법 |
| CN106661091B (zh) | 2014-07-10 | 2020-10-30 | 扬森疫苗与预防公司 | 流行性感冒病毒疫苗及其用途 |
| BR112016030577A8 (pt) | 2014-07-10 | 2021-07-20 | Janssen Vaccines & Prevention Bv | polipeptídeos multiméricos do domínio de haste da hemaglutinina da gripe, molécula de ácido nucleico, vetor, composição e usos destes |
| CA2954780A1 (en) * | 2014-07-15 | 2016-01-21 | Medimmune, Llc | Neutralizing anti-influenza b antibodies and uses thereof |
| TWI701258B (zh) | 2014-12-19 | 2020-08-11 | 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 |
| PH12017501216B1 (en) * | 2015-02-05 | 2023-05-24 | Janssen Vaccines And Prevention B V | Binding molecules directed against influenza hemagglutinin and uses thereof |
| EP3253787B1 (en) | 2015-02-05 | 2020-10-07 | Janssen Vaccines & Prevention B.V. | Human neutralizing antibodies binding to influenza neuraminidase |
| JP6960856B2 (ja) * | 2015-04-08 | 2021-11-05 | デイナ ファーバー キャンサー インスティチュート，インコーポレイテッド | ヒト化インフルエンザモノクローナル抗体およびその使用方法 |
| EP3294753A1 (en) | 2015-05-11 | 2018-03-21 | Janssen Vaccines & Prevention B.V. | Influenza virus neutralizing peptidomimetic compounds |
| EP3307310A2 (en) | 2015-05-13 | 2018-04-18 | The Trustees Of The University Of Pennsylvania | Aav-mediated expression of anti-influenza antibodies and methods of use thereof |
| SMT202100591T1 (it) * | 2015-06-01 | 2021-11-12 | Medimmune Llc | Molecole di legame anti-influenza neutralizzanti e loro usi |
| EP3374390A1 (en) | 2015-11-13 | 2018-09-19 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| AU2017207330C1 (en) | 2016-01-13 | 2022-06-09 | Medimmune, Llc | Method of treating influenza A |
| AU2017222564A1 (en) | 2016-02-24 | 2018-09-06 | Visterra, Inc. | Formulations of antibody molecules to influenza virus |
| EP3423484B1 (en) | 2016-03-01 | 2021-01-13 | Janssen Vaccines & Prevention B.V. | Human neutralizing antibodies binding to influenza b neuraminidase |
| WO2017192589A1 (en) * | 2016-05-02 | 2017-11-09 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Neutralizing antibodies to influenza ha and their use and identification |
| WO2018038096A1 (ja) * | 2016-08-23 | 2018-03-01 | 国立大学法人東京大学 | モノクローナル抗体又はその抗原結合フラグメント及びその使用 |
| KR20190071714A (ko) | 2016-10-27 | 2019-06-24 | 얀센 백신스 앤드 프리벤션 비.브이. | 인플루엔자 바이러스 중화 화합물 |
| US11566064B2 (en) | 2017-01-27 | 2023-01-31 | National Research Council Of Canada | Hemagglutinin-specific antibodies and uses thereof |
| WO2018141854A1 (en) | 2017-02-02 | 2018-08-09 | Janssen Vaccines & Prevention B.V. | Piperazine derivatives for influenza virus inhibition |
| AU2018216954B2 (en) | 2017-02-02 | 2022-04-14 | Janssen Vaccines & Prevention B.V. | Piperazine derivatives for influenza virus inhibition |
| CN118956781A (zh) | 2017-02-28 | 2024-11-15 | 宾夕法尼亚州大学信托人 | 腺相关病毒(aav)进化枝f载体及其用途 |
| KR20190135000A (ko) | 2017-02-28 | 2019-12-05 | 더 트러스티스 오브 더 유니버시티 오브 펜실바니아 | Aav 벡터를 기반으로 하는 인플루엔자 백신 |
| JOP20190200A1 (ar) | 2017-02-28 | 2019-08-27 | Univ Pennsylvania | تركيبات نافعة في معالجة ضمور العضل النخاعي |
| BR112020014343A2 (pt) | 2018-01-23 | 2020-12-08 | Janssen Vaccines & Prevention B.V. | Vacinas contra o vírus da influenza e seus usos |
| MX2020007772A (es) | 2018-01-26 | 2020-09-18 | Regeneron Pharma | Anticuerpos humanos contra hemaglutinina de influenza. |
| US11230593B2 (en) | 2019-03-25 | 2022-01-25 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| AU2020342463A1 (en) | 2019-09-05 | 2022-03-24 | Janssen Vaccines & Prevention B.V. | Influenza virus vaccines and uses thereof |
| WO2021173965A1 (en) | 2020-02-28 | 2021-09-02 | Massachusetts Institute Of Technology | Identification of variable influenza residues and uses thereof |
| WO2021201677A1 (en) | 2020-04-01 | 2021-10-07 | Kiadis Pharma Intellectual Property B.V. | Compositions and methods targeting influenza |
| US11175293B1 (en) | 2021-01-04 | 2021-11-16 | University Of Utah Research Foundation | Rapid assay for detection of SARS-CoV-2 antibodies |
| JP2024506000A (ja) | 2021-02-04 | 2024-02-08 | 四川海思科制▲薬▼有限公司 | Ｈａ阻害剤化合物の塩及び結晶形 |
| JP2025512515A (ja) * | 2022-04-14 | 2025-04-17 | インビジシールド テクノロジーズ リミテッド | インフルエンザ感染症を予防又は治療するための組成物 |
| CN120202213A (zh) | 2022-11-14 | 2025-06-24 | 扬森疫苗与预防有限公司 | 乙型流感病毒疫苗及其用途 |
| CN116589566A (zh) * | 2022-11-18 | 2023-08-15 | 昆明医科大学第一附属医院 | 一种HIV-1中和抗体的改造重组单克隆IgM抗体及其应用 |
| WO2025051975A1 (en) | 2023-09-06 | 2025-03-13 | Sanofi | Modified influenza b hemagglutinin polypeptides and nucleic acids and uses thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008028946A2 (en) * | 2006-09-07 | 2008-03-13 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| US20090092620A1 (en) * | 2007-10-08 | 2009-04-09 | Sanofi Pasteur | Flu virus hemagglutinin specific monoclonal antibodies |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ207394A (en) | 1983-03-08 | 1987-03-06 | Commw Serum Lab Commission | Detecting or determining sequence of amino acids |
| NL9101953A (nl) | 1991-11-21 | 1993-06-16 | Seed Capital Investments | Testinrichting omvattende een plaat met een veelvoud van putjes met een bijbehorende doseerinrichting, alsmede een kit die deze inrichtingen omvat en toepassing van de inrichtingen. |
| US6265150B1 (en) | 1995-06-07 | 2001-07-24 | Becton Dickinson & Company | Phage antibodies |
| AU4474497A (en) | 1996-10-08 | 1998-05-05 | U-Bisys B.V. | Methods and means for selecting peptides and proteins having specific affinity for a target |
| IL145849A0 (en) | 1999-04-15 | 2002-07-25 | Crucell Holland Bv | Recombinant protein production in a human cell using sequences encoding adenovirus e1 protein |
| DK1402025T3 (da) | 2001-06-15 | 2006-06-06 | Crucell Holland Bv | Kimære fager |
| RU2553325C2 (ru) | 2008-07-25 | 2015-06-10 | Институт Фо Ресёч Ин Биомедицин | Нейтрализующие антитела против вируса гриппа а и их использование |
| EP2168987A1 (en) * | 2008-09-22 | 2010-03-31 | Mucosis B.V. | Multifunctional linker protein containing an antibody against hemagglutinin, a conserved influenza antigen and an immunostimulating carrier binding domain |
| CN102448986B (zh) | 2009-05-11 | 2015-11-25 | 克鲁塞尔荷兰公司 | 能中和流感病毒h3n2的人结合分子及其应用 |
| DK2731967T3 (en) | 2011-07-14 | 2017-01-16 | Janssen Vaccines & Prevention Bv | HUMAN BINDING MOLECULES CAPABLE OF NEUTRALIZING INFLUENZA A VIRUS FROM PHYLOGENETIC GROUP 1 AND PHYLOGENETIC GROUP 2 AND INFLUENZA B VIRUS |
-
2012
- 2012-07-12 DK DK12735516.2T patent/DK2731967T3/en active
- 2012-07-12 EA EA201490288A patent/EA027054B1/ru not_active IP Right Cessation
- 2012-07-12 JP JP2014519551A patent/JP5683752B2/ja active Active
- 2012-07-12 BR BR112014000263-0A patent/BR112014000263B1/pt active IP Right Grant
- 2012-07-12 IN IN953CHN2014 patent/IN2014CN00953A/en unknown
- 2012-07-12 EP EP12735516.2A patent/EP2731967B1/en active Active
- 2012-07-12 US US14/126,404 patent/US8961978B2/en active Active
- 2012-07-12 KR KR1020137035132A patent/KR101941724B1/ko active Active
- 2012-07-12 PH PH1/2013/502479A patent/PH12013502479A1/en unknown
- 2012-07-12 MY MYPI2014700068A patent/MY166282A/en unknown
- 2012-07-12 HR HRP20161740TT patent/HRP20161740T1/hr unknown
- 2012-07-12 MX MX2014000373A patent/MX346206B/es active IP Right Grant
- 2012-07-12 WO PCT/EP2012/063637 patent/WO2013007770A1/en not_active Ceased
- 2012-07-12 CN CN201280034558.0A patent/CN103906763B/zh active Active
- 2012-07-12 ES ES12735516.2T patent/ES2608321T3/es active Active
- 2012-07-12 AU AU2012282504A patent/AU2012282504B2/en active Active
- 2012-07-12 CA CA2838999A patent/CA2838999C/en active Active
-
2013
- 2013-12-29 IL IL230222A patent/IL230222A/en active IP Right Grant
-
2015
- 2015-01-14 US US14/597,016 patent/US9593159B2/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008028946A2 (en) * | 2006-09-07 | 2008-03-13 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| US20090092620A1 (en) * | 2007-10-08 | 2009-04-09 | Sanofi Pasteur | Flu virus hemagglutinin specific monoclonal antibodies |
Non-Patent Citations (7)
| Title |
|---|
| CORTI DAVIDE; SUGUITAN AMORSOLO L JR; PINNA DEBORA; SILACCI CHIARA; FERNANDEZ-RODRIGUEZ BLANCA M; VANZETTA FABRIZIA; SANTOS CELIA;: "Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine", JOURNAL OF CLINICAL INVESTIGATION, AMERICAN SOCIETY FOR CLINICAL INVESTIGATION, US, vol. 120, no. 5, 3 May 2010 (2010-05-03), US, pages 1663 - 1673, XP009154686, ISSN: 0021-9738, DOI: 10.1172/JCI41902 * |
| EKIERT DAMIAN C; BHABHA GIRA; ELSLIGER MARC-ANDRE; FRIESEN ROBERT H E; JONGENEELEN MANDY; THROSBY MARK; GOUDSMIT JAAP; WILSON IAN : "Antibody Recognition of a Highly Conserved Influenza Virus Epitope", SCIENCE, AMERICAN ASSOCIATION FOR THE ADVANCEMENT OF SCIENCE, vol. 324, no. 5924, 1 April 2009 (2009-04-01), pages 246 - 251, XP009144786, ISSN: 0036-8075 * |
| LERNER RICHARD A: "Rare antibodies from combinatorial libraries suggests an SOS component of the human immunological repertoire", MOLECULAR BIOSYSTEMS, ROYAL SOCIETY OF CHEMISTRY, GB, vol. 7, no. 4, 1 January 2011 (2011-01-01), GB, pages 1004 - 1012, XP009154610, ISSN: 1742-206X, DOI: 10.1039/c0mb00310g * |
| OKUNO Y, ET AL.: "A COMMON NEUTRALIZING EPITOPE CONSERVED BETWEEN THE HEMAGGLUTIININS OF INFLUENZA A VIRUS H1 AND H2 STRAINS", JOURNAL OF VIROLOGY., THE AMERICAN SOCIETY FOR MICROBIOLOGY., US, vol. 67, no. 05, 1 May 1993 (1993-05-01), US, pages 2552 - 2558, XP001005475, ISSN: 0022-538X * |
| RUDIKOFF S, ET AL.: "Single amino acid substitution altering antigen-binding specificity", PROCEEDINGS NATIONAL ACADEMY OF SCIENCES PNAS, NATIONAL ACADEMY OF SCIENCES, US, vol. 79, 1 March 1982 (1982-03-01), US, pages 1979 - 1983, XP007901436, ISSN: 0027-8424, DOI: 10.1073/pnas.79.6.1979 * |
| SMIRNOV Y A; LIPATOV A S; GITELMAN A K; OKUNO Y; VAN BEEK R; OSTERHAUS A D ME; CLAAS E C J: "An epitope shared by the hemagglutinins of H1, H2, H5, and H6 subtypes of influenza A virus", ACTA VIROLOGICA., ACADEMIA PRAGUE, PRAGUE., CS, vol. 43, no. 4, 1 August 1999 (1999-08-01), CS, pages 237 - 244, XP009095964, ISSN: 0001-723X * |
| SUI JIANHUA, ET AL: "Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses", NAT. STRUCT. MOL. BIOL., vol. 16, no. 3, 1 March 2009 (2009-03-01), pages 265 - 273, XP002538005, ISSN: 1545-9993, DOI: 10.1038/nsmb.1566 * |
Also Published As
| Publication number | Publication date |
|---|---|
| DK2731967T3 (en) | 2017-01-16 |
| WO2013007770A1 (en) | 2013-01-17 |
| CA2838999A1 (en) | 2013-01-17 |
| JP5683752B2 (ja) | 2015-03-11 |
| EA201490288A1 (ru) | 2014-05-30 |
| ES2608321T3 (es) | 2017-04-07 |
| BR112014000263B1 (pt) | 2022-01-18 |
| NZ618530A (en) | 2016-05-27 |
| US9593159B2 (en) | 2017-03-14 |
| US20150274811A1 (en) | 2015-10-01 |
| CN103906763A (zh) | 2014-07-02 |
| PH12013502479A1 (en) | 2014-01-20 |
| AU2012282504B2 (en) | 2017-07-20 |
| HRP20161740T1 (hr) | 2017-02-10 |
| MX346206B (es) | 2017-03-09 |
| MX2014000373A (es) | 2014-03-31 |
| IN2014CN00953A (enExample) | 2015-04-10 |
| CN103906763B (zh) | 2016-10-12 |
| JP2014527403A (ja) | 2014-10-16 |
| KR101941724B1 (ko) | 2019-01-23 |
| MY166282A (en) | 2018-06-25 |
| IL230222A (en) | 2017-09-28 |
| US20140120113A1 (en) | 2014-05-01 |
| EP2731967B1 (en) | 2016-10-12 |
| CA2838999C (en) | 2021-02-16 |
| AU2012282504A1 (en) | 2014-02-06 |
| KR20140095017A (ko) | 2014-07-31 |
| EP2731967A1 (en) | 2014-05-21 |
| US8961978B2 (en) | 2015-02-24 |
| BR112014000263A2 (pt) | 2017-02-14 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EA027054B1 (ru) | Связывающие молекулы человека, способные нейтрализовать вирусы гриппа a филогенетической группы 1 и филогенетической группы 2 и вирусы гриппа b | |
| AU2013229488B2 (en) | Human binding molecules capable of binding to and neutralizing influenza B viruses and uses thereof | |
| EP2430046B1 (en) | Human binding molecules capable of neutralizing influenza virus h3n2 and uses thereof | |
| US10005831B2 (en) | Human binding molecules capable of neutralizing influenza virus H5N1 and uses thereof | |
| RS52688B (sr) | Humani vezni molekuli sposobni da neutrališu virus influence h5n1 i njihova upotreba | |
| HK1200176B (en) | Human binding molecules capable of binding to and neutralizing influenza b viruses and uses thereof | |
| NZ729856B2 (en) | Human binding molecules capable of binding to and neutralizing influenza b viruses and uses thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): AM AZ KZ KG TJ TM |