ES2655701T3 - Composiciones y métodos relacionados con variantes de la proteína A (SpA) - Google Patents
Composiciones y métodos relacionados con variantes de la proteína A (SpA) Download PDFInfo
- Publication number
- ES2655701T3 ES2655701T3 ES11801511.4T ES11801511T ES2655701T3 ES 2655701 T3 ES2655701 T3 ES 2655701T3 ES 11801511 T ES11801511 T ES 11801511T ES 2655701 T3 ES2655701 T3 ES 2655701T3
- Authority
- ES
- Spain
- Prior art keywords
- protein
- spa
- staphylococcal
- polypeptide
- composition
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 420
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 393
- 239000000203 mixture Substances 0.000 title claims description 185
- 238000000034 method Methods 0.000 title description 58
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 300
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 232
- 229920001184 polypeptide Polymers 0.000 claims abstract description 190
- 230000027455 binding Effects 0.000 claims abstract description 104
- 238000009739 binding Methods 0.000 claims abstract description 96
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 69
- 238000006467 substitution reaction Methods 0.000 claims abstract description 59
- 230000002163 immunogen Effects 0.000 claims abstract description 57
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims abstract description 35
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims abstract description 4
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims abstract description 3
- 239000000427 antigen Substances 0.000 claims description 104
- 108091007433 antigens Proteins 0.000 claims description 104
- 102000036639 antigens Human genes 0.000 claims description 104
- 241000894006 Bacteria Species 0.000 claims description 101
- 230000028993 immune response Effects 0.000 claims description 80
- 150000007523 nucleic acids Chemical class 0.000 claims description 78
- 229960005486 vaccine Drugs 0.000 claims description 74
- 102000039446 nucleic acids Human genes 0.000 claims description 51
- 108020004707 nucleic acids Proteins 0.000 claims description 51
- 150000004676 glycans Chemical class 0.000 claims description 42
- 229920001282 polysaccharide Polymers 0.000 claims description 39
- 239000005017 polysaccharide Substances 0.000 claims description 38
- 206010041925 Staphylococcal infections Diseases 0.000 claims description 32
- 239000002671 adjuvant Substances 0.000 claims description 31
- 238000011282 treatment Methods 0.000 claims description 30
- 230000001681 protective effect Effects 0.000 claims description 27
- 210000005084 renal tissue Anatomy 0.000 claims description 23
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 108700035708 EsaB Proteins 0.000 claims description 15
- 239000003446 ligand Substances 0.000 claims description 12
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 10
- 229920001542 oligosaccharide Polymers 0.000 claims description 7
- 150000002482 oligosaccharides Chemical class 0.000 claims description 7
- 102100024222 B-lymphocyte antigen CD19 Human genes 0.000 claims description 5
- 101000980825 Homo sapiens B-lymphocyte antigen CD19 Proteins 0.000 claims description 5
- 241000124008 Mammalia Species 0.000 claims description 5
- RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 claims description 5
- 229960003085 meticillin Drugs 0.000 claims description 5
- 210000000952 spleen Anatomy 0.000 claims description 5
- 108010071134 CRM197 (non-toxic variant of diphtheria toxin) Proteins 0.000 claims description 4
- 241000606768 Haemophilus influenzae Species 0.000 claims description 4
- 241000607142 Salmonella Species 0.000 claims description 4
- 230000001413 cellular effect Effects 0.000 claims description 4
- 238000002156 mixing Methods 0.000 claims description 4
- 102100037840 Dehydrogenase/reductase SDR family member 2, mitochondrial Human genes 0.000 claims description 3
- 102000057297 Pepsin A Human genes 0.000 claims description 3
- 108090000284 Pepsin A Proteins 0.000 claims description 3
- 101710188053 Protein D Proteins 0.000 claims description 3
- 101710132893 Resolvase Proteins 0.000 claims description 3
- 238000004587 chromatography analysis Methods 0.000 claims description 3
- 210000000805 cytoplasm Anatomy 0.000 claims description 3
- 229940047650 haemophilus influenzae Drugs 0.000 claims description 3
- 239000012528 membrane Substances 0.000 claims description 3
- 229940111202 pepsin Drugs 0.000 claims description 3
- 101710183389 Pneumolysin Proteins 0.000 claims description 2
- 229960003983 diphtheria toxoid Drugs 0.000 claims description 2
- 230000002085 persistent effect Effects 0.000 claims description 2
- 238000004088 simulation Methods 0.000 claims description 2
- 229960000814 tetanus toxoid Drugs 0.000 claims description 2
- 102000035195 Peptidases Human genes 0.000 claims 2
- 108091005804 Peptidases Proteins 0.000 claims 2
- 235000019833 protease Nutrition 0.000 claims 2
- RSPISYXLHRIGJD-UHFFFAOYSA-N OOOO Chemical compound OOOO RSPISYXLHRIGJD-UHFFFAOYSA-N 0.000 claims 1
- 230000011164 ossification Effects 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 381
- 108010088160 Staphylococcal Protein A Proteins 0.000 description 172
- 235000001014 amino acid Nutrition 0.000 description 81
- 208000015181 infectious disease Diseases 0.000 description 67
- 229940024606 amino acid Drugs 0.000 description 62
- 150000001413 amino acids Chemical class 0.000 description 62
- 210000004027 cell Anatomy 0.000 description 61
- 206010000269 abscess Diseases 0.000 description 56
- 239000012634 fragment Substances 0.000 description 48
- 108060003951 Immunoglobulin Proteins 0.000 description 47
- 102000018358 immunoglobulin Human genes 0.000 description 47
- 229940027941 immunoglobulin g Drugs 0.000 description 47
- 210000003719 b-lymphocyte Anatomy 0.000 description 44
- 241000295644 Staphylococcaceae Species 0.000 description 37
- 230000003993 interaction Effects 0.000 description 34
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 33
- 102000018697 Membrane Proteins Human genes 0.000 description 32
- 108010052285 Membrane Proteins Proteins 0.000 description 32
- 239000013598 vector Substances 0.000 description 31
- 230000001580 bacterial effect Effects 0.000 description 30
- 150000002632 lipids Chemical class 0.000 description 29
- 210000001519 tissue Anatomy 0.000 description 29
- 102000014914 Carrier Proteins Human genes 0.000 description 28
- 230000015572 biosynthetic process Effects 0.000 description 28
- 230000006870 function Effects 0.000 description 27
- 108010047303 von Willebrand Factor Proteins 0.000 description 27
- 102100036537 von Willebrand factor Human genes 0.000 description 27
- 229960001134 von willebrand factor Drugs 0.000 description 27
- 241000699670 Mus sp. Species 0.000 description 25
- 239000000243 solution Substances 0.000 description 24
- 241001465754 Metazoa Species 0.000 description 22
- 230000003053 immunization Effects 0.000 description 22
- 238000002649 immunization Methods 0.000 description 21
- 230000028327 secretion Effects 0.000 description 21
- 210000001744 T-lymphocyte Anatomy 0.000 description 20
- 230000000694 effects Effects 0.000 description 20
- 102000040430 polynucleotide Human genes 0.000 description 20
- 108091033319 polynucleotide Proteins 0.000 description 20
- 239000002157 polynucleotide Substances 0.000 description 20
- 102000005962 receptors Human genes 0.000 description 20
- 108020003175 receptors Proteins 0.000 description 20
- 231100000033 toxigenic Toxicity 0.000 description 20
- 230000001551 toxigenic effect Effects 0.000 description 20
- 108010078791 Carrier Proteins Proteins 0.000 description 19
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 19
- 231100000776 exotoxin Toxicity 0.000 description 19
- 239000002095 exotoxin Substances 0.000 description 19
- 230000036039 immunity Effects 0.000 description 19
- 230000003902 lesion Effects 0.000 description 19
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 18
- 108091028043 Nucleic acid sequence Proteins 0.000 description 18
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 18
- 201000010099 disease Diseases 0.000 description 18
- 230000035772 mutation Effects 0.000 description 18
- 108010065152 Coagulase Proteins 0.000 description 17
- 108091008324 binding proteins Proteins 0.000 description 17
- 210000002421 cell wall Anatomy 0.000 description 17
- 235000004554 glutamine Nutrition 0.000 description 17
- 239000000463 material Substances 0.000 description 17
- 239000000304 virulence factor Substances 0.000 description 17
- 230000007923 virulence factor Effects 0.000 description 17
- 239000004471 Glycine Substances 0.000 description 16
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 16
- 241000191967 Staphylococcus aureus Species 0.000 description 16
- 108010031318 Vitronectin Proteins 0.000 description 16
- 102100035140 Vitronectin Human genes 0.000 description 16
- 150000001875 compounds Chemical class 0.000 description 16
- 230000009467 reduction Effects 0.000 description 16
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 15
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 15
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 15
- 235000004279 alanine Nutrition 0.000 description 15
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 15
- 210000003734 kidney Anatomy 0.000 description 15
- 230000004044 response Effects 0.000 description 15
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 14
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 14
- 239000004472 Lysine Substances 0.000 description 14
- 238000000338 in vitro Methods 0.000 description 14
- 239000000047 product Substances 0.000 description 14
- 239000000758 substrate Substances 0.000 description 14
- -1 vWbp or vWh Proteins 0.000 description 14
- 239000003981 vehicle Substances 0.000 description 14
- 102000005416 ATP-Binding Cassette Transporters Human genes 0.000 description 13
- 108010006533 ATP-Binding Cassette Transporters Proteins 0.000 description 13
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 13
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 13
- 206010041917 Staphylococcal abscess Diseases 0.000 description 13
- 241000191940 Staphylococcus Species 0.000 description 13
- 101710187743 Tumor necrosis factor receptor superfamily member 1A Proteins 0.000 description 13
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 description 13
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 13
- 238000009472 formulation Methods 0.000 description 13
- 229960000310 isoleucine Drugs 0.000 description 13
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 13
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 12
- 241000191963 Staphylococcus epidermidis Species 0.000 description 12
- 210000000224 granular leucocyte Anatomy 0.000 description 12
- 229940072221 immunoglobulins Drugs 0.000 description 12
- 239000003550 marker Substances 0.000 description 12
- 230000008506 pathogenesis Effects 0.000 description 12
- 238000002360 preparation method Methods 0.000 description 12
- 108090000250 sortase A Proteins 0.000 description 12
- 239000004474 valine Substances 0.000 description 12
- 238000003556 assay Methods 0.000 description 11
- 210000000056 organ Anatomy 0.000 description 11
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 10
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 10
- 230000003213 activating effect Effects 0.000 description 10
- 239000003242 anti bacterial agent Substances 0.000 description 10
- 210000004899 c-terminal region Anatomy 0.000 description 10
- 102000037865 fusion proteins Human genes 0.000 description 10
- 108020001507 fusion proteins Proteins 0.000 description 10
- 230000002265 prevention Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 238000013518 transcription Methods 0.000 description 10
- 230000035897 transcription Effects 0.000 description 10
- 238000013519 translation Methods 0.000 description 10
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 9
- 108010077805 Bacterial Proteins Proteins 0.000 description 9
- 108020004705 Codon Proteins 0.000 description 9
- 102000004127 Cytokines Human genes 0.000 description 9
- 108090000695 Cytokines Proteins 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 9
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 9
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 9
- 240000005499 Sasa Species 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 238000007792 addition Methods 0.000 description 9
- 235000003704 aspartic acid Nutrition 0.000 description 9
- 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 9
- 238000011161 development Methods 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 235000014304 histidine Nutrition 0.000 description 9
- 244000052769 pathogen Species 0.000 description 9
- 230000037361 pathway Effects 0.000 description 9
- 239000002953 phosphate buffered saline Substances 0.000 description 9
- 150000003839 salts Chemical group 0.000 description 9
- 241000894007 species Species 0.000 description 9
- 230000014616 translation Effects 0.000 description 9
- 108700023418 Amidases Proteins 0.000 description 8
- 239000004475 Arginine Substances 0.000 description 8
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 8
- 102100026189 Beta-galactosidase Human genes 0.000 description 8
- 108091026890 Coding region Proteins 0.000 description 8
- 101710128530 Fibrinogen-binding protein Proteins 0.000 description 8
- 241000192125 Firmicutes Species 0.000 description 8
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 8
- 241000282412 Homo Species 0.000 description 8
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 8
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 8
- 101710087657 Manganese ABC transporter substrate-binding lipoprotein Proteins 0.000 description 8
- 241000404883 Pisa Species 0.000 description 8
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 8
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 8
- 101000815632 Streptococcus suis (strain 05ZYH33) Rqc2 homolog RqcH Proteins 0.000 description 8
- 239000004480 active ingredient Substances 0.000 description 8
- 102000005922 amidase Human genes 0.000 description 8
- 125000000539 amino acid group Chemical group 0.000 description 8
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 8
- 235000009582 asparagine Nutrition 0.000 description 8
- 229960001230 asparagine Drugs 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 101150043616 cna gene Proteins 0.000 description 8
- 108010064033 elastin-binding proteins Proteins 0.000 description 8
- 239000013604 expression vector Substances 0.000 description 8
- 102000025748 fibrinogen binding proteins Human genes 0.000 description 8
- 102000036072 fibronectin binding proteins Human genes 0.000 description 8
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 8
- 230000028996 humoral immune response Effects 0.000 description 8
- 230000000521 hyperimmunizing effect Effects 0.000 description 8
- 238000003018 immunoassay Methods 0.000 description 8
- 230000001939 inductive effect Effects 0.000 description 8
- 229940039716 prothrombin Drugs 0.000 description 8
- 239000007787 solid Substances 0.000 description 8
- 230000001225 therapeutic effect Effects 0.000 description 8
- 238000002560 therapeutic procedure Methods 0.000 description 8
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 8
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 7
- 101710187798 60S ribosomal protein L23 Proteins 0.000 description 7
- 101000822677 Clostridium perfringens (strain 13 / Type A) Small, acid-soluble spore protein 1 Proteins 0.000 description 7
- 108010049003 Fibrinogen Proteins 0.000 description 7
- 102000008946 Fibrinogen Human genes 0.000 description 7
- 102000006395 Globulins Human genes 0.000 description 7
- 108010044091 Globulins Proteins 0.000 description 7
- 102000002268 Hexosaminidases Human genes 0.000 description 7
- 108010000540 Hexosaminidases Proteins 0.000 description 7
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 7
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 7
- 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 7
- 108010000851 Laminin Receptors Proteins 0.000 description 7
- 102000002297 Laminin Receptors Human genes 0.000 description 7
- 102000004882 Lipase Human genes 0.000 description 7
- 108090001060 Lipase Proteins 0.000 description 7
- 239000004367 Lipase Substances 0.000 description 7
- CPLXHLVBOLITMK-UHFFFAOYSA-N Magnesium oxide Chemical compound [Mg]=O CPLXHLVBOLITMK-UHFFFAOYSA-N 0.000 description 7
- 101000576806 Protobothrops flavoviridis Small serum protein 1 Proteins 0.000 description 7
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 7
- 239000004473 Threonine Substances 0.000 description 7
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 7
- 125000003277 amino group Chemical group 0.000 description 7
- 229940088710 antibiotic agent Drugs 0.000 description 7
- 230000000890 antigenic effect Effects 0.000 description 7
- 230000002238 attenuated effect Effects 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 7
- 229940012952 fibrinogen Drugs 0.000 description 7
- 230000008348 humoral response Effects 0.000 description 7
- 230000005847 immunogenicity Effects 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 230000015788 innate immune response Effects 0.000 description 7
- 235000019421 lipase Nutrition 0.000 description 7
- 229930182817 methionine Natural products 0.000 description 7
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 7
- 239000000725 suspension Substances 0.000 description 7
- 230000001988 toxicity Effects 0.000 description 7
- 231100000419 toxicity Toxicity 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 6
- 108020004684 Internal Ribosome Entry Sites Proteins 0.000 description 6
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 6
- 241001529936 Murinae Species 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 102100027287 Serpin H1 Human genes 0.000 description 6
- 108050008290 Serpin H1 Proteins 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- 238000010171 animal model Methods 0.000 description 6
- 230000008901 benefit Effects 0.000 description 6
- 210000004369 blood Anatomy 0.000 description 6
- 239000008280 blood Substances 0.000 description 6
- 230000021615 conjugation Effects 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 239000006185 dispersion Substances 0.000 description 6
- 230000008030 elimination Effects 0.000 description 6
- 238000003379 elimination reaction Methods 0.000 description 6
- 230000002327 eosinophilic effect Effects 0.000 description 6
- 150000002148 esters Chemical class 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 230000006698 induction Effects 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000001990 intravenous administration Methods 0.000 description 6
- 239000007788 liquid Substances 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 239000008194 pharmaceutical composition Substances 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 230000035755 proliferation Effects 0.000 description 6
- 230000001105 regulatory effect Effects 0.000 description 6
- 210000003491 skin Anatomy 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 230000004936 stimulating effect Effects 0.000 description 6
- 230000032258 transport Effects 0.000 description 6
- 101710166488 6 kDa early secretory antigenic target Proteins 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 5
- 101000822695 Clostridium perfringens (strain 13 / Type A) Small, acid-soluble spore protein C1 Proteins 0.000 description 5
- 206010011409 Cross infection Diseases 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 108010073385 Fibrin Proteins 0.000 description 5
- 102000009123 Fibrin Human genes 0.000 description 5
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 5
- 101000576807 Protobothrops flavoviridis Small serum protein 2 Proteins 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 229940098773 bovine serum albumin Drugs 0.000 description 5
- 230000036755 cellular response Effects 0.000 description 5
- 239000000839 emulsion Substances 0.000 description 5
- 239000003623 enhancer Substances 0.000 description 5
- 229950003499 fibrin Drugs 0.000 description 5
- 235000013922 glutamic acid Nutrition 0.000 description 5
- 239000004220 glutamic acid Substances 0.000 description 5
- 239000000367 immunologic factor Substances 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 229940079322 interferon Drugs 0.000 description 5
- 239000010410 layer Substances 0.000 description 5
- 231100000518 lethal Toxicity 0.000 description 5
- 230000001665 lethal effect Effects 0.000 description 5
- 210000004698 lymphocyte Anatomy 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 102000035118 modified proteins Human genes 0.000 description 5
- 108091005573 modified proteins Proteins 0.000 description 5
- 230000001338 necrotic effect Effects 0.000 description 5
- 230000007935 neutral effect Effects 0.000 description 5
- 230000036963 noncompetitive effect Effects 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- 230000002035 prolonged effect Effects 0.000 description 5
- 239000002904 solvent Substances 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 238000002255 vaccination Methods 0.000 description 5
- 230000001018 virulence Effects 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 4
- 108091008875 B cell receptors Proteins 0.000 description 4
- 101100478373 Bacillus subtilis (strain 168) srtD gene Proteins 0.000 description 4
- 208000035143 Bacterial infection Diseases 0.000 description 4
- 241000701022 Cytomegalovirus Species 0.000 description 4
- 238000012286 ELISA Assay Methods 0.000 description 4
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 4
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 4
- 108010002350 Interleukin-2 Proteins 0.000 description 4
- 102000000588 Interleukin-2 Human genes 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- 108091030066 RNAIII Proteins 0.000 description 4
- 102100040247 Tumor necrosis factor Human genes 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 230000033289 adaptive immune response Effects 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 230000006907 apoptotic process Effects 0.000 description 4
- 208000022362 bacterial infectious disease Diseases 0.000 description 4
- 230000003115 biocidal effect Effects 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 239000011248 coating agent Substances 0.000 description 4
- 238000000576 coating method Methods 0.000 description 4
- 239000000470 constituent Substances 0.000 description 4
- 230000007547 defect Effects 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 239000003937 drug carrier Substances 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 230000036541 health Effects 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- 230000002458 infectious effect Effects 0.000 description 4
- 239000004615 ingredient Substances 0.000 description 4
- 238000007918 intramuscular administration Methods 0.000 description 4
- 210000000265 leukocyte Anatomy 0.000 description 4
- 230000000670 limiting effect Effects 0.000 description 4
- 230000001717 pathogenic effect Effects 0.000 description 4
- 230000002093 peripheral effect Effects 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 230000003393 splenic effect Effects 0.000 description 4
- 101150087718 srtA gene Proteins 0.000 description 4
- 238000007920 subcutaneous administration Methods 0.000 description 4
- 231100000617 superantigen Toxicity 0.000 description 4
- 239000003053 toxin Substances 0.000 description 4
- 231100000765 toxin Toxicity 0.000 description 4
- 108700012359 toxins Proteins 0.000 description 4
- 239000013603 viral vector Substances 0.000 description 4
- 102000009027 Albumins Human genes 0.000 description 3
- 108010088751 Albumins Proteins 0.000 description 3
- 102100034278 Annexin A6 Human genes 0.000 description 3
- 108090000656 Annexin A6 Proteins 0.000 description 3
- 208000031729 Bacteremia Diseases 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 3
- 102000014150 Interferons Human genes 0.000 description 3
- 108010050904 Interferons Proteins 0.000 description 3
- 102000013462 Interleukin-12 Human genes 0.000 description 3
- 108010065805 Interleukin-12 Proteins 0.000 description 3
- 206010028851 Necrosis Diseases 0.000 description 3
- 206010057249 Phagocytosis Diseases 0.000 description 3
- 206010035734 Pneumonia staphylococcal Diseases 0.000 description 3
- 108010029485 Protein Isoforms Proteins 0.000 description 3
- 102000001708 Protein Isoforms Human genes 0.000 description 3
- 108010094028 Prothrombin Proteins 0.000 description 3
- 102100027378 Prothrombin Human genes 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 206010040047 Sepsis Diseases 0.000 description 3
- 102000054727 Serum Amyloid A Human genes 0.000 description 3
- 108700028909 Serum Amyloid A Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 238000000692 Student's t-test Methods 0.000 description 3
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 3
- 102220500923 Telomerase reverse transcriptase_K35D_mutation Human genes 0.000 description 3
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 3
- 239000002776 alpha toxin Substances 0.000 description 3
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000004873 anchoring Methods 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 229940009098 aspartate Drugs 0.000 description 3
- 239000002585 base Substances 0.000 description 3
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 3
- 239000002775 capsule Substances 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 230000015271 coagulation Effects 0.000 description 3
- 238000005345 coagulation Methods 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 206010014665 endocarditis Diseases 0.000 description 3
- 101150079015 esxB gene Proteins 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 230000003325 follicular Effects 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 229960002442 glucosamine Drugs 0.000 description 3
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 3
- 108060003552 hemocyanin Proteins 0.000 description 3
- 210000002865 immune cell Anatomy 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 238000010253 intravenous injection Methods 0.000 description 3
- 230000009545 invasion Effects 0.000 description 3
- 229910052742 iron Inorganic materials 0.000 description 3
- 210000002540 macrophage Anatomy 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 230000017074 necrotic cell death Effects 0.000 description 3
- 238000007911 parenteral administration Methods 0.000 description 3
- 230000002688 persistence Effects 0.000 description 3
- 210000001539 phagocyte Anatomy 0.000 description 3
- 230000008782 phagocytosis Effects 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 208000004048 staphylococcal pneumonia Diseases 0.000 description 3
- 229940031626 subunit vaccine Drugs 0.000 description 3
- 239000000829 suppository Substances 0.000 description 3
- 230000001629 suppression Effects 0.000 description 3
- 150000003505 terpenes Chemical class 0.000 description 3
- 235000007586 terpenes Nutrition 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 2
- OTLLEIBWKHEHGU-UHFFFAOYSA-N 2-[5-[[5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy]-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-4-phosphonooxyhexanedioic acid Chemical compound C1=NC=2C(N)=NC=NC=2N1C(C(C1O)O)OC1COC1C(CO)OC(OC(C(O)C(OP(O)(O)=O)C(O)C(O)=O)C(O)=O)C(O)C1O OTLLEIBWKHEHGU-UHFFFAOYSA-N 0.000 description 2
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 2
- RADQQIMFQHYCBI-UHFFFAOYSA-N 6-[[4-[2-[2-[2-acetamido-4-[3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-5,6-dihydroxy-1-oxohexan-3-yl]oxypropanoylamino]propanoylamino]-4-carboxybutanoyl]amino]-2-amino-7-(1-carboxyethylamino)-7-oxoheptanoic acid Chemical compound OC(=O)C(N)CCCC(C(=O)NC(C)C(O)=O)NC(=O)CCC(C(O)=O)NC(=O)C(C)NC(=O)C(C)OC(C(NC(C)=O)C=O)C(C(O)CO)OC1OC(CO)C(O)C(O)C1NC(C)=O RADQQIMFQHYCBI-UHFFFAOYSA-N 0.000 description 2
- 102220510663 APC membrane recruitment protein 1_Y18F_mutation Human genes 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 101710092462 Alpha-hemolysin Proteins 0.000 description 2
- 101710197219 Alpha-toxin Proteins 0.000 description 2
- 230000024704 B cell apoptotic process Effects 0.000 description 2
- 101100128225 Bacillus subtilis (strain 168) licT gene Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 108010039939 Cell Wall Skeleton Proteins 0.000 description 2
- 102100029057 Coagulation factor XIII A chain Human genes 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- 102000008186 Collagen Human genes 0.000 description 2
- 108060005980 Collagenase Proteins 0.000 description 2
- 102000029816 Collagenase Human genes 0.000 description 2
- 102220554118 Cyclic GMP-AMP synthase_L21H_mutation Human genes 0.000 description 2
- 102220570828 Deoxynucleotidyltransferase terminal-interacting protein 1_Y14A_mutation Human genes 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 241000283086 Equidae Species 0.000 description 2
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 2
- 101100010809 Geobacillus thermodenitrificans (strain NG80-2) eccC gene Proteins 0.000 description 2
- 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 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 101000918352 Homo sapiens Coagulation factor XIII A chain Proteins 0.000 description 2
- 101000651439 Homo sapiens Prothrombin Proteins 0.000 description 2
- 102000004157 Hydrolases Human genes 0.000 description 2
- 108090000604 Hydrolases Proteins 0.000 description 2
- 206010061598 Immunodeficiency Diseases 0.000 description 2
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 2
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000004388 Interleukin-4 Human genes 0.000 description 2
- 108090000978 Interleukin-4 Proteins 0.000 description 2
- 102000043136 MAP kinase family Human genes 0.000 description 2
- 108091054455 MAP kinase family Proteins 0.000 description 2
- 102000043129 MHC class I family Human genes 0.000 description 2
- 108091054437 MHC class I family Proteins 0.000 description 2
- 102000043131 MHC class II family Human genes 0.000 description 2
- 108091054438 MHC class II family Proteins 0.000 description 2
- 102220641747 Metalloproteinase inhibitor 1_Q32A_mutation Human genes 0.000 description 2
- 102000003792 Metallothionein Human genes 0.000 description 2
- 108090000157 Metallothionein Proteins 0.000 description 2
- 102100035971 Molybdopterin molybdenumtransferase Human genes 0.000 description 2
- 101710119577 Molybdopterin molybdenumtransferase Proteins 0.000 description 2
- 241000713333 Mouse mammary tumor virus Species 0.000 description 2
- 101000686985 Mouse mammary tumor virus (strain C3H) Protein PR73 Proteins 0.000 description 2
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 2
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 2
- 125000003047 N-acetyl group Chemical group 0.000 description 2
- 102220532965 NEDD8-conjugating enzyme Ubc12_F5A_mutation Human genes 0.000 description 2
- 238000005481 NMR spectroscopy Methods 0.000 description 2
- 238000011887 Necropsy Methods 0.000 description 2
- 102100021852 Neuronal cell adhesion molecule Human genes 0.000 description 2
- 101710130688 Neuronal cell adhesion molecule Proteins 0.000 description 2
- 102220580238 Non-receptor tyrosine-protein kinase TYK2_Q13A_mutation Human genes 0.000 description 2
- 241001452677 Ogataea methanolica Species 0.000 description 2
- 102220566933 Oligosaccharyltransferase complex subunit OSTC_L17A_mutation Human genes 0.000 description 2
- 102220566947 Oligosaccharyltransferase complex subunit OSTC_N28A_mutation Human genes 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 101100103787 Oryza sativa subsp. japonica Y14A gene Proteins 0.000 description 2
- 108010013639 Peptidoglycan Proteins 0.000 description 2
- 108090000279 Peptidyltransferases Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 101710124951 Phospholipase C Proteins 0.000 description 2
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 2
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 2
- 206010035664 Pneumonia Diseases 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 2
- 108010071690 Prealbumin Proteins 0.000 description 2
- 102000007584 Prealbumin Human genes 0.000 description 2
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 108010071390 Serum Albumin Proteins 0.000 description 2
- 102000007562 Serum Albumin Human genes 0.000 description 2
- 101100233392 Staphylococcus aureus (strain Mu50 / ATCC 700699) isdA gene Proteins 0.000 description 2
- 101100019123 Staphylococcus aureus (strain Mu50 / ATCC 700699) isdB gene Proteins 0.000 description 2
- 101000794214 Staphylococcus aureus Toxic shock syndrome toxin-1 Proteins 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- 102000040945 Transcription factor Human genes 0.000 description 2
- 108091023040 Transcription factor Proteins 0.000 description 2
- 102220575134 Uncharacterized protein MISP3_I31A_mutation Human genes 0.000 description 2
- 108010059993 Vancomycin Proteins 0.000 description 2
- 102220497186 WD repeat domain phosphoinositide-interacting protein 4_N15A_mutation Human genes 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 230000000240 adjuvant effect Effects 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 230000000844 anti-bacterial effect Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 239000012736 aqueous medium Substances 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 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 2
- 230000033228 biological regulation Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 230000032823 cell division Effects 0.000 description 2
- 210000004520 cell wall skeleton Anatomy 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- MYSWGUAQZAJSOK-UHFFFAOYSA-N ciprofloxacin Chemical compound C12=CC(N3CCNCC3)=C(F)C=C2C(=O)C(C(=O)O)=CN1C1CC1 MYSWGUAQZAJSOK-UHFFFAOYSA-N 0.000 description 2
- 229920001436 collagen Polymers 0.000 description 2
- 229960002424 collagenase Drugs 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 230000001268 conjugating effect Effects 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 239000003431 cross linking reagent Substances 0.000 description 2
- WZHCOOQXZCIUNC-UHFFFAOYSA-N cyclandelate Chemical compound C1C(C)(C)CC(C)CC1OC(=O)C(O)C1=CC=CC=C1 WZHCOOQXZCIUNC-UHFFFAOYSA-N 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 210000004443 dendritic cell Anatomy 0.000 description 2
- 206010013023 diphtheria Diseases 0.000 description 2
- 108700033544 disaccharide tetrapeptide Proteins 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000002158 endotoxin Substances 0.000 description 2
- 101150043366 essB gene Proteins 0.000 description 2
- 101150018154 essC gene Proteins 0.000 description 2
- 101150016690 esxA gene Proteins 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 108010017007 glucose-regulated proteins Proteins 0.000 description 2
- 150000002309 glutamines Chemical class 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000005745 host immune response Effects 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 229940039715 human prothrombin Drugs 0.000 description 2
- 235000011167 hydrochloric acid Nutrition 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 230000007124 immune defense Effects 0.000 description 2
- 230000003308 immunostimulating effect Effects 0.000 description 2
- 238000002513 implantation Methods 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- 238000011081 inoculation Methods 0.000 description 2
- 238000007689 inspection Methods 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 230000002452 interceptive effect Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 230000021633 leukocyte mediated immunity Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000006194 liquid suspension Substances 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 208000004396 mastitis Diseases 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 238000000386 microscopy Methods 0.000 description 2
- 230000003278 mimic effect Effects 0.000 description 2
- 150000007522 mineralic acids Chemical class 0.000 description 2
- 230000000116 mitigating effect Effects 0.000 description 2
- 230000004001 molecular interaction Effects 0.000 description 2
- 210000000440 neutrophil Anatomy 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 238000000399 optical microscopy Methods 0.000 description 2
- 150000007524 organic acids Chemical class 0.000 description 2
- 235000005985 organic acids Nutrition 0.000 description 2
- 230000008520 organization Effects 0.000 description 2
- 235000011007 phosphoric acid Nutrition 0.000 description 2
- 150000003016 phosphoric acids Chemical class 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 230000003449 preventive effect Effects 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 102220278552 rs1554434768 Human genes 0.000 description 2
- 102220050582 rs193920899 Human genes 0.000 description 2
- 125000006850 spacer group Chemical group 0.000 description 2
- 208000010110 spontaneous platelet aggregation Diseases 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 239000003826 tablet Substances 0.000 description 2
- 229960002180 tetracycline Drugs 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 150000003522 tetracyclines Chemical class 0.000 description 2
- 229960004072 thrombin Drugs 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 description 2
- 229960001082 trimethoprim Drugs 0.000 description 2
- GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 2
- 229960003165 vancomycin Drugs 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- JSPNNZKWADNWHI-PNANGNLXSA-N (2r)-2-hydroxy-n-[(2s,3r,4e,8e)-3-hydroxy-9-methyl-1-[(2r,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoctadeca-4,8-dien-2-yl]heptadecanamide Chemical compound CCCCCCCCCCCCCCC[C@@H](O)C(=O)N[C@H]([C@H](O)\C=C\CC\C=C(/C)CCCCCCCCC)CO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O JSPNNZKWADNWHI-PNANGNLXSA-N 0.000 description 1
- PSLCKQYQNVNTQI-BHFSHLQUSA-N (2s)-2-aminobutanedioic acid;(2s)-2-aminopentanedioic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O.OC(=O)[C@@H](N)CCC(O)=O PSLCKQYQNVNTQI-BHFSHLQUSA-N 0.000 description 1
- SGKRLCUYIXIAHR-AKNGSSGZSA-N (4s,4ar,5s,5ar,6r,12ar)-4-(dimethylamino)-1,5,10,11,12a-pentahydroxy-6-methyl-3,12-dioxo-4a,5,5a,6-tetrahydro-4h-tetracene-2-carboxamide Chemical compound C1=CC=C2[C@H](C)[C@@H]([C@H](O)[C@@H]3[C@](C(O)=C(C(N)=O)C(=O)[C@H]3N(C)C)(O)C3=O)C3=C(O)C2=C1O SGKRLCUYIXIAHR-AKNGSSGZSA-N 0.000 description 1
- YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 1
- QZCJOXAIQXPLNS-UHFFFAOYSA-N 1,1,2,2,3,3,4,4,4a,5,5,6,6,7,7,8,8,8a-octadecafluoronaphthalene 4-(2-aminoethyl)benzene-1,2-diol Chemical compound NCCc1ccc(O)c(O)c1.FC1(F)C(F)(F)C(F)(F)C2(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C2(F)C1(F)F QZCJOXAIQXPLNS-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-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
- 101150094949 APRT gene Proteins 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical group CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241001156739 Actinobacteria <phylum> Species 0.000 description 1
- 108010024223 Adenine phosphoribosyltransferase Proteins 0.000 description 1
- UMHJEEQLYBKSAN-UHFFFAOYSA-N Adipaldehyde Chemical compound O=CCCCCC=O UMHJEEQLYBKSAN-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 206010053555 Arthritis bacterial Diseases 0.000 description 1
- 241000711404 Avian avulavirus 1 Species 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 241001260012 Bursa Species 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 101710163595 Chaperone protein DnaK Proteins 0.000 description 1
- 241000238586 Cirripedia Species 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 241000037164 Collema parvum Species 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 101150074155 DHFR gene Proteins 0.000 description 1
- 102220557633 DNA-directed RNA polymerase I subunit RPA12_Q14H_mutation Human genes 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
- 229940032046 DTaP vaccine Drugs 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 206010013801 Duchenne Muscular Dystrophy Diseases 0.000 description 1
- 235000019227 E-number Nutrition 0.000 description 1
- 239000004243 E-number Substances 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108700041152 Endoplasmic Reticulum Chaperone BiP Proteins 0.000 description 1
- 102100021451 Endoplasmic reticulum chaperone BiP Human genes 0.000 description 1
- 102100039328 Endoplasmin Human genes 0.000 description 1
- 241001495410 Enterococcus sp. Species 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 102220508665 Ephrin type-A receptor 4_Q40A_mutation Human genes 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
- 241000283074 Equus asinus Species 0.000 description 1
- 229920002444 Exopolysaccharide Polymers 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- 206010016275 Fear Diseases 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 206010016952 Food poisoning Diseases 0.000 description 1
- 208000019331 Foodborne disease Diseases 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010062347 HLA-DQ Antigens Proteins 0.000 description 1
- 108010067802 HLA-DR alpha-Chains Proteins 0.000 description 1
- 101150112743 HSPA5 gene Proteins 0.000 description 1
- 101001015673 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) Glycerophosphodiester phosphodiesterase Proteins 0.000 description 1
- 101710178376 Heat shock 70 kDa protein Proteins 0.000 description 1
- 101710152018 Heat shock cognate 70 kDa protein Proteins 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 1
- 108010088652 Histocompatibility Antigens Class I Proteins 0.000 description 1
- 102220637909 Histone chaperone ASF1B_D36A_mutation Human genes 0.000 description 1
- 102220637910 Histone chaperone ASF1B_D37A_mutation Human genes 0.000 description 1
- 108010033040 Histones Proteins 0.000 description 1
- 101001050288 Homo sapiens Transcription factor Jun Proteins 0.000 description 1
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 1
- 241001135569 Human adenovirus 5 Species 0.000 description 1
- 229920002153 Hydroxypropyl cellulose Polymers 0.000 description 1
- 241000282620 Hylobates sp. Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 208000004575 Infectious Arthritis Diseases 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102100025306 Integrin alpha-IIb Human genes 0.000 description 1
- 101710149643 Integrin alpha-IIb Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 102000000589 Interleukin-1 Human genes 0.000 description 1
- 108090000174 Interleukin-10 Proteins 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- 108010002586 Interleukin-7 Proteins 0.000 description 1
- 102000000704 Interleukin-7 Human genes 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
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- UPYKUZBSLRQECL-UKMVMLAPSA-N Lycopene Natural products CC(=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1C(=C)CCCC1(C)C)C=CC=C(/C)C=CC2C(=C)CCCC2(C)C UPYKUZBSLRQECL-UKMVMLAPSA-N 0.000 description 1
- JEVVKJMRZMXFBT-XWDZUXABSA-N Lycophyll Natural products OC/C(=C/CC/C(=C\C=C\C(=C/C=C/C(=C\C=C\C=C(/C=C/C=C(\C=C\C=C(/CC/C=C(/CO)\C)\C)/C)\C)/C)\C)/C)/C JEVVKJMRZMXFBT-XWDZUXABSA-N 0.000 description 1
- 108010059343 MM Form Creatine Kinase Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102000000422 Matrix Metalloproteinase 3 Human genes 0.000 description 1
- 101710201349 Metallothionein B Proteins 0.000 description 1
- 102100031347 Metallothionein-2 Human genes 0.000 description 1
- 101710094505 Metallothionein-2 Proteins 0.000 description 1
- 208000037942 Methicillin-resistant Staphylococcus aureus infection Diseases 0.000 description 1
- 101001057048 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) ESAT-6-like protein EsxB Proteins 0.000 description 1
- 101100445609 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) espC gene Proteins 0.000 description 1
- 102220532634 NEDD8-conjugating enzyme Ubc12_Q10A_mutation Human genes 0.000 description 1
- 101100257820 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) ssp-1 gene Proteins 0.000 description 1
- 108091005461 Nucleic proteins Chemical group 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 206010031252 Osteomyelitis Diseases 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001631646 Papillomaviridae Species 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 102000007568 Proto-Oncogene Proteins c-fos Human genes 0.000 description 1
- 108010071563 Proto-Oncogene Proteins c-fos Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 101000868151 Rattus norvegicus Somatotropin Proteins 0.000 description 1
- 208000021326 Ritter disease Diseases 0.000 description 1
- 102000018673 SEC Translocation Channels Human genes 0.000 description 1
- 108010091732 SEC Translocation Channels Proteins 0.000 description 1
- 101100111629 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) KAR2 gene Proteins 0.000 description 1
- 206010053879 Sepsis syndrome Diseases 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- 108090000251 Sortase B Proteins 0.000 description 1
- 206010041929 Staphylococcal scalded skin syndrome Diseases 0.000 description 1
- 101100439912 Staphylococcus aureus (strain Mu50 / ATCC 700699) clfA gene Proteins 0.000 description 1
- 101100439920 Staphylococcus aureus (strain Mu50 / ATCC 700699) clfB gene Proteins 0.000 description 1
- 101100280079 Staphylococcus aureus (strain Mu50 / ATCC 700699) esxA gene Proteins 0.000 description 1
- 101100280095 Staphylococcus aureus (strain Mu50 / ATCC 700699) esxB gene Proteins 0.000 description 1
- 101100227483 Staphylococcus aureus (strain Mu50 / ATCC 700699) fnbA gene Proteins 0.000 description 1
- 101100072797 Staphylococcus aureus (strain Mu50 / ATCC 700699) isdC gene Proteins 0.000 description 1
- 101100397212 Staphylococcus aureus (strain Mu50 / ATCC 700699) isdH gene Proteins 0.000 description 1
- 101100532861 Staphylococcus aureus (strain Mu50 / ATCC 700699) sdrC gene Proteins 0.000 description 1
- 101100532870 Staphylococcus aureus (strain Mu50 / ATCC 700699) sdrD gene Proteins 0.000 description 1
- 101100148963 Staphylococcus aureus (strain Mu50 / ATCC 700699) sdrE gene Proteins 0.000 description 1
- 101100096296 Staphylococcus aureus (strain Mu50 / ATCC 700699) spa gene Proteins 0.000 description 1
- 101100257675 Staphylococcus aureus (strain Mu50 / ATCC 700699) sraP gene Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 208000002847 Surgical Wound Diseases 0.000 description 1
- 208000031650 Surgical Wound Infection Diseases 0.000 description 1
- 206010051379 Systemic Inflammatory Response Syndrome Diseases 0.000 description 1
- 230000024932 T cell mediated immunity Effects 0.000 description 1
- 230000029662 T-helper 1 type immune response Effects 0.000 description 1
- 108090000925 TNF receptor-associated factor 2 Proteins 0.000 description 1
- 102100034779 TRAF family member-associated NF-kappa-B activator Human genes 0.000 description 1
- 102220500149 Target of EGR1 protein 1_Q9A_mutation Human genes 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 206010043376 Tetanus Diseases 0.000 description 1
- BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 229940122388 Thrombin inhibitor Drugs 0.000 description 1
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 1
- 102000006601 Thymidine Kinase Human genes 0.000 description 1
- 108020004440 Thymidine kinase Proteins 0.000 description 1
- 102220470366 Thymosin beta-10_F30A_mutation Human genes 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- 101150009046 Tnfrsf1a gene Proteins 0.000 description 1
- 206010044248 Toxic shock syndrome Diseases 0.000 description 1
- 231100000650 Toxic shock syndrome Toxicity 0.000 description 1
- 102100023132 Transcription factor Jun Human genes 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 102000013394 Troponin I Human genes 0.000 description 1
- 108010065729 Troponin I Proteins 0.000 description 1
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 1
- 101710117021 Tyrosine-protein phosphatase YopH Proteins 0.000 description 1
- 102220549960 Usher syndrome type-1C protein-binding protein 1_N21A_mutation Human genes 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 102100035071 Vimentin Human genes 0.000 description 1
- 108010065472 Vimentin Proteins 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- VRGWBRLULZUWAJ-XFFXIZSCSA-N [(2s)-2-[(1r,3z,5s,8z,12z,15s)-5,17-dihydroxy-4,8,12,15-tetramethyl-16-oxo-18-bicyclo[13.3.0]octadeca-3,8,12,17-tetraenyl]propyl] acetate Chemical compound C1\C=C(C)/CC\C=C(C)/CC[C@H](O)\C(C)=C/C[C@@H]2C([C@@H](COC(C)=O)C)=C(O)C(=O)[C@]21C VRGWBRLULZUWAJ-XFFXIZSCSA-N 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
- 238000002835 absorbance Methods 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 108091006088 activator proteins Proteins 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 230000025845 adhesion to host Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- NWMHDZMRVUOQGL-CZEIJOLGSA-N almurtide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)CO[C@@H]([C@H](O)[C@H](O)CO)[C@@H](NC(C)=O)C=O NWMHDZMRVUOQGL-CZEIJOLGSA-N 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 229940126575 aminoglycoside Drugs 0.000 description 1
- 235000011114 ammonium hydroxide Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 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 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000001399 anti-metabolic effect Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 238000011203 antimicrobial therapy Methods 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 description 1
- 210000001130 astrocyte Anatomy 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000003637 basic solution Substances 0.000 description 1
- 210000003651 basophil Anatomy 0.000 description 1
- HFACYLZERDEVSX-UHFFFAOYSA-N benzidine Chemical compound C1=CC(N)=CC=C1C1=CC=C(N)C=C1 HFACYLZERDEVSX-UHFFFAOYSA-N 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 208000037815 bloodstream infection Diseases 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 229940087373 calcium oxide Drugs 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000010351 cardiac pulsation Effects 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 210000004970 cd4 cell Anatomy 0.000 description 1
- 230000020411 cell activation Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000004709 cell invasion Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000001516 cell proliferation assay Methods 0.000 description 1
- 230000017455 cell-cell adhesion Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 229930183167 cerebroside Natural products 0.000 description 1
- RIZIAUKTHDLMQX-UHFFFAOYSA-N cerebroside D Natural products CCCCCCCCCCCCCCCCC(O)C(=O)NC(C(O)C=CCCC=C(C)CCCCCCCCC)COC1OC(CO)C(O)C(O)C1O RIZIAUKTHDLMQX-UHFFFAOYSA-N 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 150000005829 chemical entities Chemical class 0.000 description 1
- 239000012707 chemical precursor Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- CCGSUNCLSOWKJO-UHFFFAOYSA-N cimetidine Chemical compound N#CNC(=N/C)\NCCSCC1=NC=N[C]1C CCGSUNCLSOWKJO-UHFFFAOYSA-N 0.000 description 1
- 229960001380 cimetidine Drugs 0.000 description 1
- 229960003405 ciprofloxacin Drugs 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000006448 coagulant property Effects 0.000 description 1
- 230000005757 colony formation Effects 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 230000002301 combined effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000011443 conventional therapy Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 229960003722 doxycycline Drugs 0.000 description 1
- 238000002283 elective surgery Methods 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 101150022827 esaA gene Proteins 0.000 description 1
- 101150079475 esaB gene Proteins 0.000 description 1
- 101150102084 essA gene Proteins 0.000 description 1
- 101150026034 esxC gene Proteins 0.000 description 1
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 239000003925 fat Substances 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
- 229960004887 ferric hydroxide Drugs 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- VRGWBRLULZUWAJ-UHFFFAOYSA-N fusaproliferin Natural products C1C=C(C)CCC=C(C)CCC(O)C(C)=CCC2C(C(COC(C)=O)C)=C(O)C(=O)C21C VRGWBRLULZUWAJ-UHFFFAOYSA-N 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000012224 gene deletion Methods 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 229960002518 gentamicin Drugs 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 239000003862 glucocorticoid Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 150000002327 glycerophospholipids Chemical class 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 101150028578 grp78 gene Proteins 0.000 description 1
- 210000003709 heart valve Anatomy 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 108010037896 heparin-binding hemagglutinin Proteins 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 230000009215 host defense mechanism Effects 0.000 description 1
- 229940106780 human fibrinogen Drugs 0.000 description 1
- 229940098197 human immunoglobulin g Drugs 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000001863 hydroxypropyl cellulose Substances 0.000 description 1
- 235000010977 hydroxypropyl cellulose Nutrition 0.000 description 1
- 239000012642 immune effector Substances 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 238000013115 immunohistochemical detection Methods 0.000 description 1
- 229940088592 immunologic factor Drugs 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 229960001438 immunostimulant agent Drugs 0.000 description 1
- 239000003022 immunostimulating agent Substances 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 208000037800 influenza D Diseases 0.000 description 1
- 230000004941 influx Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 150000007529 inorganic bases Chemical class 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 239000013067 intermediate product Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- IEECXTSVVFWGSE-UHFFFAOYSA-M iron(3+);oxygen(2-);hydroxide Chemical compound [OH-].[O-2].[Fe+3] IEECXTSVVFWGSE-UHFFFAOYSA-M 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- JJWLVOIRVHMVIS-UHFFFAOYSA-N isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 1
- 239000007951 isotonicity adjuster Substances 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- OTQCKZUSUGYWBD-BRHMIFOHSA-N lepirudin Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)C(C)C)[C@@H](C)O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(C)C)[C@@H](C)O)C1=CC=C(O)C=C1 OTQCKZUSUGYWBD-BRHMIFOHSA-N 0.000 description 1
- 229960004408 lepirudin Drugs 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- GZQKNULLWNGMCW-PWQABINMSA-N lipid A (E. coli) Chemical compound O1[C@H](CO)[C@@H](OP(O)(O)=O)[C@H](OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC)[C@@H](NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC)[C@@H]1OC[C@@H]1[C@@H](O)[C@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OP(O)(O)=O)O1 GZQKNULLWNGMCW-PWQABINMSA-N 0.000 description 1
- ULXTYUPMJXVUHQ-OVTFQNCVSA-N lipid II Chemical compound OC(=O)[C@@H](C)NC(=O)[C@@H](C)NC(=O)[C@H](CCCCN)NC(=O)CC[C@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@@H]1[C@@H](NC(C)=O)[C@@H](OP(O)(=O)OP(O)(=O)OC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(\C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O)[C@@H](CO)O1 ULXTYUPMJXVUHQ-OVTFQNCVSA-N 0.000 description 1
- 229920006008 lipopolysaccharide Polymers 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 229960004999 lycopene Drugs 0.000 description 1
- OAIJSZIZWZSQBC-GYZMGTAESA-N lycopene Chemical compound CC(C)=CCC\C(C)=C\C=C\C(\C)=C\C=C\C(\C)=C\C=C\C=C(/C)\C=C\C=C(/C)\C=C\C=C(/C)CCC=C(C)C OAIJSZIZWZSQBC-GYZMGTAESA-N 0.000 description 1
- 235000012661 lycopene Nutrition 0.000 description 1
- 239000001751 lycopene Substances 0.000 description 1
- 238000002794 lymphocyte assay Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- ZLNQQNXFFQJAID-UHFFFAOYSA-L magnesium carbonate Chemical compound [Mg+2].[O-]C([O-])=O ZLNQQNXFFQJAID-UHFFFAOYSA-L 0.000 description 1
- 239000001095 magnesium carbonate Substances 0.000 description 1
- 229910000021 magnesium carbonate Inorganic materials 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 210000003622 mature neutrocyte Anatomy 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 208000015688 methicillin-resistant staphylococcus aureus infectious disease Diseases 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 210000000274 microglia Anatomy 0.000 description 1
- JMUHBNWAORSSBD-WKYWBUFDSA-N mifamurtide Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@@H](OC(=O)CCCCCCCCCCCCCCC)COP(O)(=O)OCCNC(=O)[C@H](C)NC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1NC(C)=O JMUHBNWAORSSBD-WKYWBUFDSA-N 0.000 description 1
- 229960005225 mifamurtide Drugs 0.000 description 1
- 230000001617 migratory effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 231100000324 minimal toxicity Toxicity 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 239000002324 mouth wash Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 101150008049 mx gene Proteins 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 231100000956 nontoxicity Toxicity 0.000 description 1
- 230000000269 nucleophilic effect Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 229940049964 oleate Drugs 0.000 description 1
- 244000039328 opportunistic pathogen Species 0.000 description 1
- 230000001662 opsonic effect Effects 0.000 description 1
- 230000000625 opsonophagocytic effect Effects 0.000 description 1
- 150000007530 organic bases Chemical class 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000000399 orthopedic effect Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 230000000242 pagocytic effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 210000004303 peritoneum Anatomy 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001515 polyalkylene glycol Polymers 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 235000008476 powdered milk Nutrition 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 238000009117 preventive therapy Methods 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
- 229960004919 procaine Drugs 0.000 description 1
- 230000008741 proinflammatory signaling process Effects 0.000 description 1
- 229930185346 proliferin Natural products 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 229940023143 protein vaccine Drugs 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000007420 reactivation Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000002787 reinforcement Effects 0.000 description 1
- 206010038351 renal abscess Diseases 0.000 description 1
- 230000002940 repellent Effects 0.000 description 1
- 239000005871 repellent Substances 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 239000003340 retarding agent Substances 0.000 description 1
- 210000000574 retroperitoneal space Anatomy 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 102220198146 rs1057519886 Human genes 0.000 description 1
- 102220002405 rs121908660 Human genes 0.000 description 1
- 102220313688 rs367768055 Human genes 0.000 description 1
- 102220117512 rs886041928 Human genes 0.000 description 1
- CVHZOJJKTDOEJC-UHFFFAOYSA-N saccharin Chemical compound C1=CC=C2C(=O)NS(=O)(=O)C2=C1 CVHZOJJKTDOEJC-UHFFFAOYSA-N 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 201000001223 septic arthritis Diseases 0.000 description 1
- 208000013223 septicemia Diseases 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 230000009919 sequestration Effects 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 239000008159 sesame oil Substances 0.000 description 1
- 235000011803 sesame oil Nutrition 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 210000004872 soft tissue Anatomy 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 229940075582 sorbic acid Drugs 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000009331 sowing Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000004988 splenocyte Anatomy 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 229940031439 squalene Drugs 0.000 description 1
- TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 239000000021 stimulant Substances 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 108091007196 stromelysin Proteins 0.000 description 1
- 238000010613 succinylation reaction Methods 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 229960005404 sulfamethoxazole Drugs 0.000 description 1
- JLKIGFTWXXRPMT-UHFFFAOYSA-N sulphamethoxazole Chemical compound O1C(C)=CC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1 JLKIGFTWXXRPMT-UHFFFAOYSA-N 0.000 description 1
- 230000002325 super-antigenic effect Effects 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 229940037128 systemic glucocorticoids Drugs 0.000 description 1
- TXEYQDLBPFQVAA-UHFFFAOYSA-N tetrafluoromethane Chemical compound FC(F)(F)F TXEYQDLBPFQVAA-UHFFFAOYSA-N 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 150000007970 thio esters Chemical group 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 239000003868 thrombin inhibitor Substances 0.000 description 1
- 239000005495 thyroid hormone Substances 0.000 description 1
- 229940036555 thyroid hormone Drugs 0.000 description 1
- ZCIHMQAPACOQHT-ZGMPDRQDSA-N trans-isorenieratene Natural products CC(=C/C=C/C=C(C)/C=C/C=C(C)/C=C/c1c(C)ccc(C)c1C)C=CC=C(/C)C=Cc2c(C)ccc(C)c2C ZCIHMQAPACOQHT-ZGMPDRQDSA-N 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 229960001005 tuberculin Drugs 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 1
- 231100000588 tumorigenic Toxicity 0.000 description 1
- 230000000381 tumorigenic effect Effects 0.000 description 1
- 230000029069 type 2 immune response Effects 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 208000019206 urinary tract infection Diseases 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 210000005048 vimentin Anatomy 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- 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
- A61K39/02—Bacterial antigens
- A61K39/085—Staphylococcus
-
- 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
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1271—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Micrococcaceae (F), e.g. Staphylococcus
-
- 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
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US36121810P | 2010-07-02 | 2010-07-02 | |
| US361218P | 2010-07-02 | ||
| US37072510P | 2010-08-04 | 2010-08-04 | |
| US370725P | 2010-08-04 | ||
| PCT/US2011/042845 WO2012003474A2 (en) | 2010-07-02 | 2011-07-01 | Compositions and methods related to protein a (spa) variants |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2655701T3 true ES2655701T3 (es) | 2018-02-21 |
Family
ID=45402686
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES11801511.4T Active ES2655701T3 (es) | 2010-07-02 | 2011-07-01 | Composiciones y métodos relacionados con variantes de la proteína A (SpA) |
Country Status (12)
| Country | Link |
|---|---|
| US (8) | US8821894B2 (enExample) |
| EP (1) | EP2588120B1 (enExample) |
| JP (1) | JP6002128B2 (enExample) |
| KR (1) | KR20130093084A (enExample) |
| CN (1) | CN103037885B (enExample) |
| AU (1) | AU2011274367B2 (enExample) |
| BR (1) | BR112013000097B1 (enExample) |
| CA (1) | CA2803298C (enExample) |
| ES (1) | ES2655701T3 (enExample) |
| SG (1) | SG186290A1 (enExample) |
| WO (1) | WO2012003474A2 (enExample) |
| ZA (1) | ZA201209561B (enExample) |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9181329B2 (en) * | 2007-08-31 | 2015-11-10 | The University Of Chicago | Methods and compositions related to immunizing against Staphylococcal lung diseases and conditions |
| SMT202000246T1 (it) * | 2009-04-03 | 2020-07-08 | Univ Chicago | Composizioni e metodi relativi a varianti della proteina a (spa) |
| BR122019005883A8 (pt) * | 2009-10-30 | 2022-10-04 | Novartis Ag | Método para liberação de polissacarídeo capsular, processo de purificação de sacarídeos capsulares tipo 5 e tipo 8 de staphylococcus aureus e composição |
| ES2655701T3 (es) | 2010-07-02 | 2018-02-21 | The University Of Chicago | Composiciones y métodos relacionados con variantes de la proteína A (SpA) |
| EP3578205A1 (en) | 2010-08-06 | 2019-12-11 | ModernaTX, Inc. | A pharmaceutical formulation comprising engineered nucleic acids and medical use thereof |
| WO2012034067A1 (en) * | 2010-09-09 | 2012-03-15 | The University Of Chicago | Methods and compositions involving protective staphylococcal antigens |
| HUE069586T2 (hu) | 2010-10-01 | 2025-03-28 | Modernatx Inc | Módosított nukleozidok, nukleotidok és nukleinsavak, valamint ezek felhasználása |
| JP2014511687A (ja) | 2011-03-31 | 2014-05-19 | モデルナ セラピューティクス インコーポレイテッド | 工学操作された核酸の送達および製剤 |
| AU2012296576B2 (en) | 2011-08-15 | 2017-09-07 | The University Of Chicago | Compositions and methods related to antibodies to staphylococcal protein a |
| US9464124B2 (en) | 2011-09-12 | 2016-10-11 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| DK3682905T3 (da) | 2011-10-03 | 2022-02-28 | Modernatx Inc | Modificerede nukleosider, nukleotider og nukleinsyrer og anvendelser deraf |
| HRP20220717T1 (hr) | 2011-12-16 | 2022-07-22 | Modernatx, Inc. | Modificirani pripravci mrna |
| US10501512B2 (en) | 2012-04-02 | 2019-12-10 | Modernatx, Inc. | Modified polynucleotides |
| US9283287B2 (en) | 2012-04-02 | 2016-03-15 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of nuclear proteins |
| US9572897B2 (en) | 2012-04-02 | 2017-02-21 | Modernatx, Inc. | Modified polynucleotides for the production of cytoplasmic and cytoskeletal proteins |
| JP6189415B2 (ja) | 2012-04-02 | 2017-08-30 | モデルナティエックス インコーポレイテッドＭｏｄｅｒｎａＴＸ，Ｉｎｃ． | 細胞質および細胞骨格タンパク質の産生のための修飾ポリヌクレオチド |
| CN104703622B (zh) | 2012-04-26 | 2017-05-24 | 芝加哥大学 | 与金黄色葡萄球菌疾病期间抵消凝固酶活性的抗体相关的组合物和方法 |
| JP6670106B2 (ja) * | 2012-04-26 | 2020-03-18 | ザ・ユニバーシティ・オブ・シカゴＴｈｅ Ｕｎｉｖｅｒｓｉｔｙ Ｏｆ Ｃｈｉｃａｇｏ | ブドウ球菌コアグラーゼ抗原およびその使用方法 |
| EP2922554B1 (en) | 2012-11-26 | 2022-02-23 | ModernaTX, Inc. | Terminally modified rna |
| US8980864B2 (en) | 2013-03-15 | 2015-03-17 | Moderna Therapeutics, Inc. | Compositions and methods of altering cholesterol levels |
| GB201310008D0 (en) * | 2013-06-05 | 2013-07-17 | Glaxosmithkline Biolog Sa | Immunogenic composition for use in therapy |
| EP3052106A4 (en) | 2013-09-30 | 2017-07-19 | ModernaTX, Inc. | Polynucleotides encoding immune modulating polypeptides |
| KR20160067219A (ko) | 2013-10-03 | 2016-06-13 | 모더나 세라퓨틱스, 인코포레이티드 | 저밀도 지단백질 수용체를 암호화하는 폴리뉴클레오타이드 |
| ES2704860T3 (es) * | 2013-12-09 | 2019-03-20 | Olymvax Biopharmaceuticals Inc | Mutante SpA5 de Staphylococcus aureus, composición que comprende el mutante y procedimiento de preparación y utilización del mismo |
| WO2015103545A1 (en) * | 2014-01-03 | 2015-07-09 | Bio-Rad Laboratories, Inc. | Removal of impurities from protein a eluates |
| WO2016152946A1 (ja) * | 2015-03-26 | 2016-09-29 | Jsr株式会社 | イムノグロブリン結合タンパク質およびそれを用いたアフィニティー担体 |
| EP3416979A4 (en) * | 2016-02-12 | 2019-09-11 | The University of Chicago | COMPOSITIONS AND METHODS RELATED TO ANTIBODIES FOR NEUTRALIZING COAGULASE ACTIVITY IN STAPHYLOCOCCUS AUREUS DISEASE |
| US10738338B2 (en) | 2016-10-18 | 2020-08-11 | The Research Foundation for the State University | Method and composition for biocatalytic protein-oligonucleotide conjugation and protein-oligonucleotide conjugate |
| KR102798502B1 (ko) | 2017-08-07 | 2025-04-23 | 리플리겐 코포레이션 | C-말단 나선형 영역에 시스테인을 갖는 fc 결합 단백질 |
| EP3521304B9 (en) | 2018-02-01 | 2023-10-04 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| GB201802339D0 (en) * | 2018-02-13 | 2018-03-28 | Glaxosmithkline Biologicals Sa | Immunogenic composition |
| CN114340652B (zh) | 2019-05-14 | 2025-02-14 | 芝加哥大学 | 包含葡萄球菌蛋白A(SpA)变体的方法和组合物 |
| EP3777884A1 (en) | 2019-08-15 | 2021-02-17 | GlaxoSmithKline Biologicals S.A. | Immunogenic composition |
| CN115151559A (zh) * | 2019-10-02 | 2022-10-04 | 扬森疫苗与预防公司 | 葡萄球菌肽和使用方法 |
| CN117700501A (zh) * | 2022-09-13 | 2024-03-15 | 普米斯生物技术(珠海)有限公司 | 免疫球蛋白结合蛋白及其应用 |
Family Cites Families (188)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL154600B (nl) | 1971-02-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van specifiek bindende eiwitten en hun corresponderende bindbare stoffen. |
| US3949064A (en) | 1973-10-26 | 1976-04-06 | Baxter Laboratories, Inc. | Method of detecting antigens or antibodies |
| GB1499035A (en) | 1975-04-10 | 1978-01-25 | Ts Nii Gematologii I Perelivan | Antistaphylococcus human immune globulin and method of preparing same |
| US4174384A (en) | 1975-06-30 | 1979-11-13 | Syva Company | Fluorescence quenching with immunological pairs in immunoassays |
| US4367110A (en) | 1979-07-02 | 1983-01-04 | Toppan Printing Co. | Decorative laminate and a manufacturing method therefor |
| US4327082A (en) | 1979-07-12 | 1982-04-27 | Adcock-Ingram Laboratories Limited | Mastitis vaccination |
| US4372945A (en) | 1979-11-13 | 1983-02-08 | Likhite Vilas V | Antigen compounds |
| US4452901A (en) | 1980-03-20 | 1984-06-05 | Ciba-Geigy Corporation | Electrophoretically transferring electropherograms to nitrocellulose sheets for immuno-assays |
| US4338298A (en) | 1980-04-04 | 1982-07-06 | Endowment And Research Foundation At Montana State University | Vaccine for passive immunization against enteric colibacillosis and method of use |
| US4554101A (en) | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| IL61904A (en) | 1981-01-13 | 1985-07-31 | Yeda Res & Dev | Synthetic vaccine against influenza virus infections comprising a synthetic peptide and process for producing same |
| US4356170A (en) | 1981-05-27 | 1982-10-26 | Canadian Patents & Development Ltd. | Immunogenic polysaccharide-protein conjugates |
| US4596792A (en) | 1981-09-04 | 1986-06-24 | The Regents Of The University Of California | Safe vaccine for hepatitis containing polymerized serum albumin |
| NL8200523A (nl) | 1982-02-11 | 1983-09-01 | Univ Leiden | Werkwijze voor het in vitro transformeren van planteprotoplasten met plasmide-dna. |
| US4748018A (en) | 1984-02-07 | 1988-05-31 | Stolle Research & Development Corp. | Method of passive immunization of mammals using avian antibody |
| JPS5938877A (ja) | 1982-08-30 | 1984-03-02 | Musashi Eng Kk | 紙葉判別方法 |
| US5151350A (en) | 1982-10-27 | 1992-09-29 | Repligen Corporation | Cloned genes encoding recombinant protein a |
| US4599230A (en) | 1984-03-09 | 1986-07-08 | Scripps Clinic And Research Foundation | Synthetic hepatitis B virus vaccine including both T cell and B cell determinants |
| US4599231A (en) | 1984-03-09 | 1986-07-08 | Scripps Clinic And Research Foundation | Synthetic hepatitis B virus vaccine including both T cell and B cell determinants |
| US4879236A (en) | 1984-05-16 | 1989-11-07 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
| US5189015A (en) | 1984-05-30 | 1993-02-23 | Alfa-Laval Agri International Ab | Method for prophylactic treatment of the colonization of a Staphylococcus aureus bacterial strain by bacterial cell surface protein with fibronectin and fibrinogen binding ability |
| US5238808A (en) | 1984-10-31 | 1993-08-24 | Igen, Inc. | Luminescent metal chelate labels and means for detection |
| US5310687A (en) | 1984-10-31 | 1994-05-10 | Igen, Inc. | Luminescent metal chelate labels and means for detection |
| US5221605A (en) | 1984-10-31 | 1993-06-22 | Igen, Inc. | Luminescent metal chelate labels and means for detection |
| US4608251A (en) | 1984-11-09 | 1986-08-26 | Pitman-Moore, Inc. | LHRH analogues useful in stimulating anti-LHRH antibodies and vaccines containing such analogues |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4601903A (en) | 1985-05-01 | 1986-07-22 | The United States Of America As Represented By The Department Of Health And Human Services | Vaccine against Neisseria meningitidis Group B serotype 2 invasive disease |
| US4690915A (en) | 1985-08-08 | 1987-09-01 | The United States Of America As Represented By The Department Of Health And Human Services | Adoptive immunotherapy as a treatment modality in humans |
| US4800159A (en) | 1986-02-07 | 1989-01-24 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences |
| US5084269A (en) | 1986-11-06 | 1992-01-28 | Kullenberg Fred W | Adjuvant for dose treatment with antigens |
| AU622104B2 (en) | 1987-03-11 | 1992-04-02 | Sangtec Molecular Diagnostics Ab | Method of assaying of nucleic acids, a reagent combination and kit therefore |
| US5320951A (en) | 1987-06-01 | 1994-06-14 | Hoeoek Magnus | Fibronectin binding protein as well as its preparation |
| FR2619122B1 (fr) | 1987-08-03 | 1990-03-09 | Pasteur Institut | Procede d'obtention de polyosides capsulaires de staphylocoques, polyosides obtenus, applications de ces polyosides et souches pour la mise en oeuvre du procede |
| US4952500A (en) | 1988-02-01 | 1990-08-28 | University Of Georgia Research Foundation, Inc. | Cloning systems for Rhodococcus and related bacteria |
| US5858652A (en) | 1988-08-30 | 1999-01-12 | Abbott Laboratories | Detection and amplification of target nucleic acid sequences |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| SE8901687D0 (sv) | 1989-05-11 | 1989-05-11 | Alfa Laval Agri Int | Fibronectin binding protein as well as its preparation |
| US5302523A (en) | 1989-06-21 | 1994-04-12 | Zeneca Limited | Transformation of plant cells |
| US7705215B1 (en) | 1990-04-17 | 2010-04-27 | Dekalb Genetics Corporation | Methods and compositions for the production of stably transformed, fertile monocot plants and cells thereof |
| US5550318A (en) | 1990-04-17 | 1996-08-27 | Dekalb Genetics Corporation | Methods and compositions for the production of stably transformed, fertile monocot plants and cells thereof |
| US5322783A (en) | 1989-10-17 | 1994-06-21 | Pioneer Hi-Bred International, Inc. | Soybean transformation by microparticle bombardment |
| US5484956A (en) | 1990-01-22 | 1996-01-16 | Dekalb Genetics Corporation | Fertile transgenic Zea mays plant comprising heterologous DNA encoding Bacillus thuringiensis endotoxin |
| SE466259B (sv) | 1990-05-31 | 1992-01-20 | Arne Forsgren | Protein d - ett igd-bindande protein fraan haemophilus influenzae, samt anvaendning av detta foer analys, vacciner och uppreningsaendamaal |
| US5384253A (en) | 1990-12-28 | 1995-01-24 | Dekalb Genetics Corporation | Genetic transformation of maize cells by electroporation of cells pretreated with pectin degrading enzymes |
| CA2059693C (en) | 1991-01-28 | 2003-08-19 | Peter J. Kniskern | Polysaccharide antigens from streptococcus pneumoniae |
| CA2059692C (en) | 1991-01-28 | 2004-11-16 | Peter J. Kniskern | Pneumoccoccal polysaccharide conjugate vaccine |
| US5199942A (en) | 1991-06-07 | 1993-04-06 | Immunex Corporation | Method for improving autologous transplantation |
| WO1993004169A1 (en) | 1991-08-20 | 1993-03-04 | Genpharm International, Inc. | Gene targeting in animal cells using isogenic dna constructs |
| US5610042A (en) | 1991-10-07 | 1997-03-11 | Ciba-Geigy Corporation | Methods for stable transformation of wheat |
| US5620896A (en) | 1992-03-23 | 1997-04-15 | University Of Massachusetts Medical Center | DNA vaccines against rotavirus infections |
| CA2132953C (en) | 1992-03-26 | 2001-01-30 | Howard C. Krivan | Monospecific polyclonal antibodies to shiga-like toxins |
| US5217277A (en) | 1992-05-11 | 1993-06-08 | The Berkline Corporation | Seat arm with concealed table |
| EP1983056A1 (en) | 1992-07-07 | 2008-10-22 | Japan Tobacco Inc. | Method for transforming monocotyledons |
| US5702932A (en) | 1992-07-20 | 1997-12-30 | University Of Florida | Microinjection methods to transform arthropods with exogenous DNA |
| WO1994002620A2 (en) | 1992-07-27 | 1994-02-03 | Pioneer Hi-Bred International, Inc. | An improved method of agrobacterium-mediated transformation of cultured soybean cells |
| DE4228457A1 (de) | 1992-08-27 | 1994-04-28 | Beiersdorf Ag | Herstellung von heterodimerem PDGF-AB mit Hilfe eines bicistronischen Vektorsystems in Säugerzellen |
| EP0621875B1 (en) | 1992-09-21 | 2002-03-27 | Alfa-Laval Agri International Ab | Fibrinogen binding protein |
| GB9222888D0 (en) | 1992-10-30 | 1992-12-16 | British Tech Group | Tomography |
| US5846709A (en) | 1993-06-15 | 1998-12-08 | Imclone Systems Incorporated | Chemical process for amplifying and detecting nucleic acid sequences |
| FR2708288B1 (fr) | 1993-07-26 | 1995-09-01 | Bio Merieux | Procédé d'amplification d'acides nucléiques par transcription utilisant le déplacement, réactifs et nécessaire pour la mise en Óoeuvre de ce procédé. |
| EP0720485B1 (en) | 1993-09-22 | 2003-11-19 | Henry M. Jackson Foundation For The Advancement Of Military Medicine | Method of activating soluble carbohydrate using novel cyanylating reagents for the production of immunogenic constructs |
| US5928905A (en) | 1995-04-18 | 1999-07-27 | Glaxo Group Limited | End-complementary polymerase reaction |
| US5648240A (en) | 1994-05-24 | 1997-07-15 | Texas A&M University | MHC II analog from Staphylococcus aureus |
| EP0763135B1 (en) | 1994-05-28 | 2002-07-10 | Tepnel Medical Limited | Producing copies of nucleic acids |
| US5656610A (en) | 1994-06-21 | 1997-08-12 | University Of Southern California | Producing a protein in a mammal by injection of a DNA-sequence into the tongue |
| US5942391A (en) | 1994-06-22 | 1999-08-24 | Mount Sinai School Of Medicine | Nucleic acid amplification method: ramification-extension amplification method (RAM) |
| FR2722208B1 (fr) | 1994-07-05 | 1996-10-04 | Inst Nat Sante Rech Med | Nouveau site interne d'entree des ribosomes, vecteur le contenant et utilisation therapeutique |
| US6008341A (en) | 1994-08-22 | 1999-12-28 | The Provost, Fellows And Scholars Of The College Of The Holy And Undivided Trinity Of Queen Elizabeth Near Dublin | S. aureus fibrinogen binding protein gene |
| US5871986A (en) | 1994-09-23 | 1999-02-16 | The General Hospital Corporation | Use of a baculovirus to express and exogenous gene in a mammalian cell |
| US5736524A (en) | 1994-11-14 | 1998-04-07 | Merck & Co.,. Inc. | Polynucleotide tuberculosis vaccine |
| US5935825A (en) | 1994-11-18 | 1999-08-10 | Shimadzu Corporation | Process and reagent for amplifying nucleic acid sequences |
| US6770278B1 (en) | 1994-12-02 | 2004-08-03 | Central Biomedia, Inc. | Methods of making and using immunoglobulin (Ig) compositions |
| US5548066A (en) | 1994-12-02 | 1996-08-20 | Central Biomedia, Inc. | Failure of passive transfer immune serum and method of making same |
| US5843650A (en) | 1995-05-01 | 1998-12-01 | Segev; David | Nucleic acid detection and amplification by chemical linkage of oligonucleotides |
| US5700928A (en) | 1995-10-16 | 1997-12-23 | Smithkline Beecham, P.L.C. | Polynucleotide encoding saliva binding protein |
| US5780448A (en) | 1995-11-07 | 1998-07-14 | Ottawa Civic Hospital Loeb Research | DNA-based vaccination of fish |
| US6833253B2 (en) | 1996-01-05 | 2004-12-21 | Human Genome Sciences, Inc. | Staphylococcus aureus polynucleotides and polypeptides |
| US6737248B2 (en) | 1996-01-05 | 2004-05-18 | Human Genome Sciences, Inc. | Staphylococcus aureus polynucleotides and sequences |
| US6403337B1 (en) | 1996-01-05 | 2002-06-11 | Human Genome Sciences, Inc. | Staphylococcus aureus genes and polypeptides |
| US6593114B1 (en) | 1996-01-05 | 2003-07-15 | Human Genome Sciences, Inc. | Staphylococcus aureus polynucleotides and sequences |
| US5612473A (en) | 1996-01-16 | 1997-03-18 | Gull Laboratories | Methods, kits and solutions for preparing sample material for nucleic acid amplification |
| FR2746398B1 (fr) | 1996-03-21 | 1998-04-30 | Bio Merieux | Anticorps specifique de staphylococcus aureaus, et utilisations |
| US5928906A (en) | 1996-05-09 | 1999-07-27 | Sequenom, Inc. | Process for direct sequencing during template amplification |
| CA2255669A1 (en) | 1996-05-16 | 1997-11-20 | The Texas A & M University System | Collagen binding protein compositions and methods of use |
| US6013763A (en) | 1996-06-04 | 2000-01-11 | Genentech, Inc. | Peptide variants of protein A |
| US5939291A (en) | 1996-06-14 | 1999-08-17 | Sarnoff Corporation | Microfluidic method for nucleic acid amplification |
| US5945100A (en) | 1996-07-31 | 1999-08-31 | Fbp Corporation | Tumor delivery vehicles |
| US6294177B1 (en) | 1996-09-11 | 2001-09-25 | Nabi | Staphylococcus aureus antigen-containing whole cell vaccine |
| US5849546A (en) | 1996-09-13 | 1998-12-15 | Epicentre Technologies Corporation | Methods for using mutant RNA polymerases with reduced discrimination between non-canonical and canonical nucleoside triphosphates |
| US5981274A (en) | 1996-09-18 | 1999-11-09 | Tyrrell; D. Lorne J. | Recombinant hepatitis virus vectors |
| EP0958373A4 (en) | 1996-10-23 | 2001-11-28 | American Home Prod | Vaccines. |
| US5849497A (en) | 1997-04-03 | 1998-12-15 | The Research Foundation Of State University Of New York | Specific inhibition of the polymerase chain reaction using a non-extendable oligonucleotide blocker |
| US6610293B1 (en) | 1997-06-16 | 2003-08-26 | The Henry M. Jackson Foundation For The Advancement Of Military Medicine | Opsonic and protective monoclonal and chimeric antibodies specific for lipoteichoic acid of gram positive bacteria |
| US5866366A (en) | 1997-07-01 | 1999-02-02 | Smithkline Beecham Corporation | gidB |
| US5916776A (en) | 1997-08-27 | 1999-06-29 | Sarnoff Corporation | Amplification method for a polynucleotide |
| US6756361B1 (en) | 1997-10-14 | 2004-06-29 | Nabi | Enterococcus antigens and vaccines |
| US5994624A (en) | 1997-10-20 | 1999-11-30 | Cotton Incorporated | In planta method for the production of transgenic plants |
| US5932451A (en) | 1997-11-19 | 1999-08-03 | Incyte Pharmaceuticals, Inc. | Method for unbiased mRNA amplification |
| EP1034277B1 (en) | 1997-11-26 | 2012-06-27 | Inhibitex, Inc. | Extracellular matrix-binding proteins from Staphylococcus aureus |
| US6680195B1 (en) | 1997-11-26 | 2004-01-20 | Inhibitex, Inc. | Extracellular matrix-binding proteins from staphylococcus aureus |
| CA2337966A1 (en) | 1998-07-10 | 2000-01-20 | U.S. Medical Research Institute Of Infectious Diseases | Vaccine against staphylococcus intoxication |
| IL141691A0 (en) | 1998-08-31 | 2002-03-10 | Trinity College Dublin | Polypeptides and polynucleotides from coagulase-negative staphylococci |
| US6703025B1 (en) | 1998-08-31 | 2004-03-09 | Inhibitex, Inc. | Multicomponent vaccines |
| CA2341177A1 (en) | 1998-08-31 | 2000-03-09 | Inhibitex, Inc. | Staphylococcal immunotherapeutics via donor selection and donor stimulation |
| CN1314450C (zh) | 1998-08-31 | 2007-05-09 | 英希比泰克斯公司 | 多组分疫苗 |
| US6692739B1 (en) | 1998-08-31 | 2004-02-17 | Inhibitex, Inc. | Staphylococcal immunotherapeutics via donor selection and donor stimulation |
| AU6131999A (en) | 1998-09-01 | 2000-03-21 | Human Genome Sciences, Inc. | (staphylococcus aureus) genes and polypeptides |
| WO2000015238A1 (en) | 1998-09-14 | 2000-03-23 | Nabi | COMPOSITIONS OF β-GLUCANS AND SPECIFIC IGIV |
| AU769539B2 (en) | 1999-01-29 | 2004-01-29 | Zoetis Services Llc | Adjuvants for use in vaccines |
| US6936258B1 (en) | 1999-03-19 | 2005-08-30 | Nabi Biopharmaceuticals | Staphylococcus antigen and vaccine |
| CA2367830A1 (en) | 1999-04-28 | 2000-11-02 | The Texas A & M University System | Method of inhibiting leukocyte adhesion to fibrinogen |
| AU5867100A (en) | 1999-05-03 | 2000-12-12 | Medarex, Inc. | Human antibodies to staphylococcus aureus |
| JP2002544237A (ja) * | 1999-05-15 | 2002-12-24 | ユニバーシティ オブ カリフォルニア，サン ディエゴ | 望ましい活性を有するプロテインａに基づく結合ドメイン |
| WO2001034809A2 (en) | 1999-11-09 | 2001-05-17 | Glaxo Group Limited | Staphylococcus epidermidis nucleic acids and proteins |
| US6703492B1 (en) | 1999-11-09 | 2004-03-09 | Smithkline Beecham Corporation | Staphylococcus epidermidis nucleic acids and proteins |
| AU1813701A (en) | 1999-12-03 | 2001-06-12 | Celltech Chiroscience Limited | Interleukin-1 muteins useful as vaccine adjuvants |
| US6651655B1 (en) | 2000-01-18 | 2003-11-25 | Quadrant Technologies Limited | Inhaled vaccines |
| SE0000514D0 (sv) | 2000-02-17 | 2000-02-17 | Biostapro Ab | A 52 kDa protein from coagulase negative staphylococci and fragments |
| AU2001256958A1 (en) | 2000-03-17 | 2001-10-03 | Inhibitex, Inc. | Cross-reactive displacing antibodies from collagen-binding proteins and method of identification and use |
| KR20020097200A (ko) | 2000-03-21 | 2002-12-31 | 엘리트라 파마슈티컬즈, 인코포레이티드 | 원핵세포에서의 필수유전자의 동정 |
| GB0014907D0 (en) | 2000-06-20 | 2000-08-09 | Univ Sheffield | Antigenic polypeptides |
| SE0003573D0 (sv) | 2000-10-04 | 2000-10-04 | Bengt Guss | Method and means for producing novel von Willebrand factor binding proteins and their use in biotechnology |
| WO2002038175A1 (en) | 2000-11-07 | 2002-05-16 | Immunovaccine Technologies Inc. | Vaccines with enhanced immune response and methods for their preparation |
| AT410798B (de) | 2001-01-26 | 2003-07-25 | Cistem Biotechnologies Gmbh | Verfahren zur identifizierung, isolierung und herstellung von antigenen gegen ein spezifisches pathogen |
| US20020169288A1 (en) | 2001-03-15 | 2002-11-14 | Magnus Hook | Collagen-binding adhesin from staphylococcus epidermidis and method of use |
| GB0107661D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Staphylococcus aureus |
| CA2446294A1 (en) | 2001-05-08 | 2002-11-14 | Yi Xu | Surface proteins from gram-positive bacteria having highly conserved motifs and antibodies that recognize them |
| EP1423701B1 (en) | 2001-06-15 | 2012-07-25 | Inhibitex, Inc. | Cross-reactive monoclonal and polyclonal antibodies which recognize surface proteins from coagulase-negative staphylococci and staphylococcus aureus |
| CA2351018A1 (en) | 2001-07-09 | 2003-01-09 | Universite De Sherbrooke | Dna vaccine against staphylococcus aureus |
| US7410647B2 (en) | 2001-08-02 | 2008-08-12 | University Of Sheffield | Antigenic polypeptides |
| US20030113350A1 (en) | 2001-09-19 | 2003-06-19 | Fattom Ali I. | Glycoconjugate vaccines for use in immune-compromised populations |
| US7115264B2 (en) | 2001-11-05 | 2006-10-03 | Inhibitex | Monoclonal antibodies to the fibronectin binding protein and method of use in treating or preventing infections |
| WO2003041726A1 (en) | 2001-11-16 | 2003-05-22 | Biostapro Ab | Use of an extracellular adherence protein for the manufacture of an anti-inflammatory drug |
| EP1455817B1 (en) | 2001-12-11 | 2008-12-31 | Merck & Co., Inc. | Staphylococcus aureus exopolysaccharide and process |
| AU2003216487A1 (en) | 2002-03-05 | 2003-09-22 | Inhibitex, Inc. | Monoclonal and polyclonal antibodies recognizing coagulase-negative staphylococcal proteins |
| US7736652B2 (en) | 2002-03-21 | 2010-06-15 | The Regents Of The University Of California | Antibody fusion proteins: effective adjuvants of protein vaccination |
| US6984381B2 (en) | 2002-07-05 | 2006-01-10 | The United States Of America As Represented By The Secretary Of Agriculture | Vaccine for the prevention of bacterial infection of the bovine mammary gland |
| JP4686188B2 (ja) | 2002-09-13 | 2011-05-18 | ザ テキサス エイ アンド エム ユニバースティ システム | グラム陽性菌由来の表面固定化タンパク質を同定するためのバイオインフォマティクス法及びそれによって得られるタンパク質 |
| JP2006510353A (ja) | 2002-10-03 | 2006-03-30 | インターツェル・アクチェンゲゼルシャフト | ハプトグロビン受容体リガンド結合と相互作用する分子の使用 |
| PL229487B1 (pl) | 2002-11-12 | 2018-07-31 | Brigham & Womens Hospital Inc | Kompozycja zawierająca polimer β-1,6-glukozaminy, kompozycja zawierająca przeciwciało, kompozycja farmaceutyczna, sposób wytwarzania wyodrębnionego polisacharydu, sposób identyfikacji obecności deacetylowanej poli-N-acetyloglukozaminy (dPNAG) i/ lub poli-N-acetyloglukozaminy (PNAG), wyodrębniony polisacharyd do zastosowania w leczeniu lub profilaktyce zakażenia, wyodrębniony polisacharyd do zastosowania do wytwarzania przeciwciał, w tym przeciwciał monoklonalnych, wyodrębniony polisacharyd do zastosowania w identyfikacji przeciwciała monoklonalnego |
| US7723087B2 (en) | 2002-11-12 | 2010-05-25 | The Brigham And Women's Hospital, Inc. | Nucleic acid molecules for enhanced production of a bacterial polysaccharide and methods of use thereof |
| JPWO2004048975A1 (ja) | 2002-11-22 | 2006-03-23 | 第一化学薬品株式会社 | 黄色ブドウ球菌の検査方法 |
| US20050031625A1 (en) | 2003-03-28 | 2005-02-10 | Elusys Therapeutics, Inc. | Methods and compositions for conversion of antibody activity |
| CA2522400A1 (en) | 2003-04-16 | 2004-11-04 | The Texas A & M University System | Staphylococcus aureus efb protein and c3 binding region which inhibit complement activation |
| US20060188515A1 (en) | 2003-07-24 | 2006-08-24 | Anderson Annaliesa S | Polypeptides for inducing a protective immune response against staphylococcus aureus |
| KR20060065643A (ko) | 2003-07-24 | 2006-06-14 | 머크 앤드 캄파니 인코포레이티드 | 스타필로코쿠스 아우레우스에 대한 방어 면역 반응을유도하는 폴리펩타이드 |
| US20080160089A1 (en) | 2003-10-14 | 2008-07-03 | Medivas, Llc | Vaccine delivery compositions and methods of use |
| JP2007528217A (ja) | 2004-02-18 | 2007-10-11 | メルク エンド カムパニー インコーポレーテッド | スタヒロコッカス・アウレウスに対する防御免疫応答を誘導するためのポリペプチド |
| US7284284B2 (en) | 2004-06-15 | 2007-10-23 | James Wysopal | Headgear article incorporating a bottle opener |
| EP1791560A4 (en) | 2004-09-17 | 2009-01-14 | Merck & Co Inc | POLYPEPTIDES FOR INDUCING A PROTECTIVE IMMUNE RESPONSE AGAINST STAPHYLOCOCCUS AUREUS |
| ES2540770T3 (es) | 2004-09-22 | 2015-07-13 | Glaxosmithkline Biologicals Sa | Composición inmunógena para uso en vacunación contra estafilococos |
| AU2005310981A1 (en) | 2004-10-25 | 2006-06-08 | The University Of Western Ontario | Vaccines, compositions and methods based on Staphylococcus aureus iron-regulated surface determinants IsdA, IsdB, and IsdC |
| CA2585849A1 (en) | 2004-10-29 | 2006-05-11 | Elusys Therapeutics, Inc. | Use of cr1-binding molecules in clearance and induction of immune responses |
| US20060134141A1 (en) | 2004-12-14 | 2006-06-22 | Nabi Biopharmaceuticals | Glycoconjugate vaccines containing peptidoglycan |
| CN101107009B (zh) | 2005-01-20 | 2014-08-06 | 伊斯克诺瓦公司 | 包含纤连蛋白结合蛋白或纤连蛋白结合肽的疫苗组合物 |
| US20060228368A1 (en) | 2005-04-07 | 2006-10-12 | Nabi Biopharmaceuticals | Method of protecting against staphylococcal infection |
| US8398991B2 (en) | 2005-06-22 | 2013-03-19 | Institut Pasteur | Modified ESAT-6 molecules and improved vaccine strains of Mycobacterium bovis BCG |
| GB0526038D0 (en) | 2005-12-21 | 2006-02-01 | Glaxosmithkline Biolog Sa | Immunogenic composition |
| CA2637598A1 (en) | 2006-01-18 | 2007-02-14 | University Of Chicago | Compositions and methods related to staphylococcal bacterium proteins |
| US20110091480A1 (en) | 2006-01-27 | 2011-04-21 | Brown Martha J | Antigen-Binding Proteins Targeting S. Aureus Orf0657n |
| WO2007095057A2 (en) | 2006-02-10 | 2007-08-23 | Government Of The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Use of eap protein for treating and preventing autoimmune neuroinflammatory diseases |
| AU2007221321B2 (en) | 2006-02-22 | 2012-06-28 | The Texas A & M University System | Antibodies recognizing a highly expressed putative antigen of CA-MRSA and methods of use |
| AR060187A1 (es) | 2006-03-30 | 2008-05-28 | Glaxosmithkline Biolog Sa | Composicion inmunogenica |
| EA020459B1 (ru) | 2006-03-30 | 2014-11-28 | Глаксосмитклайн Байолоджикалс С.А. | Иммуногенная композиция |
| KR20090019007A (ko) | 2006-06-12 | 2009-02-24 | 나비 바이오파마슈티컬즈 | 스타필로코쿠스 감염증을 치료 및 예방하기 위한 알파-독소의 용도 |
| WO2008152447A2 (en) | 2006-10-30 | 2008-12-18 | The University Of Western Ontario | Staphylococcus aureus specific anti-infectives |
| WO2008140487A2 (en) | 2006-11-14 | 2008-11-20 | Elusys Therapeutics, Inc. | Improved staphylococcal protein a mono- and bispecific antibodies and methods of their use |
| US20100047252A1 (en) | 2006-11-22 | 2010-02-25 | 3M Innovative Properties Company | Antibody with protein a selectivity |
| US7488807B2 (en) | 2006-11-22 | 2009-02-10 | 3M Innovative Properties Company | Antibody with protein A selectivity |
| GB0700136D0 (en) | 2007-01-04 | 2007-02-14 | Glaxosmithkline Biolog Sa | Process for manufacturing vaccines |
| MX2009012891A (es) | 2007-05-31 | 2009-12-10 | Merck & Co Inc | Proteinas de union a antigeno dirigidas a staphylococcus aureus orf0657n. |
| US9181329B2 (en) | 2007-08-31 | 2015-11-10 | The University Of Chicago | Methods and compositions related to immunizing against Staphylococcal lung diseases and conditions |
| WO2009029831A1 (en) | 2007-08-31 | 2009-03-05 | University Of Chicago | Methods and compositions related to immunizing against staphylococcal lung diseases and conditions |
| CA2760493A1 (en) | 2008-05-12 | 2009-11-19 | Strox Biopharmaceuticals, Llc | Staphylococcus aureus-specific antibody preparations |
| US8758765B2 (en) | 2008-07-29 | 2014-06-24 | The University Of Chicago | Compositions and methods related to Staphylococcal bacterium proteins |
| US8592555B2 (en) | 2008-08-11 | 2013-11-26 | Emd Millipore Corporation | Immunoglobulin-binding proteins with improved specificity |
| WO2010042481A1 (en) | 2008-10-06 | 2010-04-15 | University Of Chicago | Compositions and methods related to bacterial eap, emp, and/or adsa proteins |
| MX2011006870A (es) | 2008-12-23 | 2011-07-19 | Genentech Inc | Variantes de inmunoglobulina con union alterada a proteina a. |
| SMT202000246T1 (it) * | 2009-04-03 | 2020-07-08 | Univ Chicago | Composizioni e metodi relativi a varianti della proteina a (spa) |
| HUE036372T2 (hu) | 2009-06-22 | 2018-07-30 | Wyeth Llc | Staphylococcus aureus antigének immunogén készítményei |
| WO2012122533A2 (en) | 2011-03-10 | 2012-09-13 | The University Of Chicago | Compositions and methods related to antibodies to staphylococcal proteins isda or isdb |
| FR2957821B1 (fr) | 2010-03-24 | 2014-08-29 | Inst Francais Du Petrole | Nouvelle zone de regeneration du catalyseur divisee en secteurs pour unites catalytiques regeneratives |
| EP2555794A4 (en) * | 2010-04-05 | 2014-01-15 | Univ Chicago | COMPOSITIONS AND METHODS RELATING TO PROTEIN A (SPA) ANTIBODIES AS IMMUNE REACTION AMPLIFIERS |
| ES2655701T3 (es) * | 2010-07-02 | 2018-02-21 | The University Of Chicago | Composiciones y métodos relacionados con variantes de la proteína A (SpA) |
| WO2012034077A2 (en) | 2010-09-09 | 2012-03-15 | The University Of Chicago | Compositions and methods related to attenuated staphylococcal strains |
| WO2012034067A1 (en) * | 2010-09-09 | 2012-03-15 | The University Of Chicago | Methods and compositions involving protective staphylococcal antigens |
| US8945588B2 (en) | 2011-05-06 | 2015-02-03 | The University Of Chicago | Methods and compositions involving protective staphylococcal antigens, such as EBH polypeptides |
-
2011
- 2011-07-01 ES ES11801511.4T patent/ES2655701T3/es active Active
- 2011-07-01 SG SG2012091104A patent/SG186290A1/en unknown
- 2011-07-01 US US13/807,598 patent/US8821894B2/en active Active
- 2011-07-01 CN CN201180032798.2A patent/CN103037885B/zh active Active
- 2011-07-01 AU AU2011274367A patent/AU2011274367B2/en active Active
- 2011-07-01 KR KR1020137002673A patent/KR20130093084A/ko not_active Abandoned
- 2011-07-01 BR BR112013000097-0A patent/BR112013000097B1/pt active IP Right Grant
- 2011-07-01 EP EP11801511.4A patent/EP2588120B1/en active Active
- 2011-07-01 WO PCT/US2011/042845 patent/WO2012003474A2/en not_active Ceased
- 2011-07-01 JP JP2013518766A patent/JP6002128B2/ja active Active
- 2011-07-01 CA CA2803298A patent/CA2803298C/en active Active
-
2012
- 2012-12-14 ZA ZA2012/09561A patent/ZA201209561B/en unknown
-
2014
- 2014-08-22 US US14/466,514 patent/US9315554B2/en active Active
-
2016
- 2016-03-04 US US15/060,861 patent/US20160194363A1/en not_active Abandoned
-
2017
- 2017-09-12 US US15/702,037 patent/US10464971B2/en active Active
-
2019
- 2019-10-23 US US16/661,155 patent/US11059866B2/en active Active
-
2021
- 2021-06-07 US US17/340,532 patent/US11939358B2/en active Active
-
2024
- 2024-02-21 US US18/583,180 patent/US20240190927A1/en not_active Abandoned
- 2024-10-07 US US18/908,562 patent/US20250236649A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| BR112013000097B1 (pt) | 2022-02-01 |
| CN103037885B (zh) | 2015-08-26 |
| WO2012003474A2 (en) | 2012-01-05 |
| US11939358B2 (en) | 2024-03-26 |
| US20160194363A1 (en) | 2016-07-07 |
| CA2803298C (en) | 2020-07-14 |
| ZA201209561B (en) | 2016-10-26 |
| AU2011274367A1 (en) | 2013-01-10 |
| EP2588120B1 (en) | 2017-11-15 |
| WO2012003474A3 (en) | 2012-04-05 |
| CN103037885A (zh) | 2013-04-10 |
| US20250236649A1 (en) | 2025-07-24 |
| US20240190927A1 (en) | 2024-06-13 |
| JP6002128B2 (ja) | 2016-10-05 |
| AU2011274367B2 (en) | 2015-04-23 |
| BR112013000097A2 (pt) | 2017-05-16 |
| US11059866B2 (en) | 2021-07-13 |
| CA2803298A1 (en) | 2012-01-05 |
| SG186290A1 (en) | 2013-01-30 |
| US20130171183A1 (en) | 2013-07-04 |
| EP2588120A2 (en) | 2013-05-08 |
| US20210290748A1 (en) | 2021-09-23 |
| JP2013534532A (ja) | 2013-09-05 |
| US20200140494A1 (en) | 2020-05-07 |
| EP2588120A4 (en) | 2014-03-26 |
| KR20130093084A (ko) | 2013-08-21 |
| US8821894B2 (en) | 2014-09-02 |
| US20150056240A1 (en) | 2015-02-26 |
| US20170369536A1 (en) | 2017-12-28 |
| US10464971B2 (en) | 2019-11-05 |
| US9315554B2 (en) | 2016-04-19 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2655701T3 (es) | Composiciones y métodos relacionados con variantes de la proteína A (SpA) | |
| JP6042574B2 (ja) | 免疫反応のエンハンサーとしてのプロテインＡ（ＳｐＡ）抗体に関連する組成物および方法 | |
| JP5793194B2 (ja) | 感染防御ブドウ球菌抗原が関与する方法および組成物 | |
| JP5789250B2 (ja) | プロテインＡ（ＳｐＡ）変種に関連する組成物および方法 | |
| US10857220B2 (en) | Staphylococcal coagulase antigens and methods of their use | |
| HK1207571B (en) | Staphylococcal coagulase antigens and methods of their use |