KR100667121B1 - 바이러스 감염증 치료를 위한 조성물 및 방법 - Google Patents
바이러스 감염증 치료를 위한 조성물 및 방법 Download PDFInfo
- Publication number
- KR100667121B1 KR100667121B1 KR1020057016920A KR20057016920A KR100667121B1 KR 100667121 B1 KR100667121 B1 KR 100667121B1 KR 1020057016920 A KR1020057016920 A KR 1020057016920A KR 20057016920 A KR20057016920 A KR 20057016920A KR 100667121 B1 KR100667121 B1 KR 100667121B1
- Authority
- KR
- South Korea
- Prior art keywords
- amino acid
- acid residue
- region corresponding
- hiv
- antibody
- 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.)
- Expired - Lifetime
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 77
- 238000011282 treatment Methods 0.000 title claims abstract description 44
- 230000003612 virological effect Effects 0.000 title claims abstract description 18
- 238000000034 method Methods 0.000 title abstract description 73
- 208000035473 Communicable disease Diseases 0.000 title 1
- 241000700605 Viruses Species 0.000 claims abstract description 42
- 230000028993 immune response Effects 0.000 claims abstract description 37
- 208000015181 infectious disease Diseases 0.000 claims abstract description 35
- 241000282412 Homo Species 0.000 claims abstract description 29
- 208000036142 Viral infection Diseases 0.000 claims abstract description 13
- 230000009385 viral infection Effects 0.000 claims abstract description 13
- 108010067390 Viral Proteins Proteins 0.000 claims abstract description 12
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 245
- 125000000539 amino acid group Chemical group 0.000 claims description 200
- 102000004169 proteins and genes Human genes 0.000 claims description 151
- 108090000623 proteins and genes Proteins 0.000 claims description 123
- 241000713772 Human immunodeficiency virus 1 Species 0.000 claims description 88
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 claims description 83
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical group OC(=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)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 claims description 79
- 239000000427 antigen Substances 0.000 claims description 61
- 108091007433 antigens Proteins 0.000 claims description 59
- 102000036639 antigens Human genes 0.000 claims description 59
- 108700004026 gag Genes Proteins 0.000 claims description 41
- 101150098622 gag gene Proteins 0.000 claims description 41
- 102000003886 Glycoproteins Human genes 0.000 claims description 36
- 108090000288 Glycoproteins Proteins 0.000 claims description 36
- 239000006166 lysate Substances 0.000 claims description 35
- 150000001413 amino acids Chemical group 0.000 claims description 34
- 238000003556 assay Methods 0.000 claims description 29
- 108091005804 Peptidases Proteins 0.000 claims description 26
- 239000004365 Protease Substances 0.000 claims description 26
- 101800001690 Transmembrane protein gp41 Proteins 0.000 claims description 26
- 238000006386 neutralization reaction Methods 0.000 claims description 26
- 102000004190 Enzymes Human genes 0.000 claims description 22
- 108090000790 Enzymes Proteins 0.000 claims description 22
- 101710104895 DNA replication protein 17 Proteins 0.000 claims description 19
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 claims description 18
- 101710181863 Structural DNA-binding protein p10 Proteins 0.000 claims description 18
- 101710086987 X protein Proteins 0.000 claims description 18
- 108090000144 Human Proteins Proteins 0.000 claims description 17
- 102000003839 Human Proteins Human genes 0.000 claims description 17
- 239000011859 microparticle Substances 0.000 claims description 17
- 238000003018 immunoassay Methods 0.000 claims description 15
- 108010016626 Dipeptides Proteins 0.000 claims description 14
- 239000000833 heterodimer Substances 0.000 claims description 13
- 230000002779 inactivation Effects 0.000 claims description 13
- 101710167800 Capsid assembly scaffolding protein Proteins 0.000 claims description 11
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 claims description 9
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 claims description 9
- MWTAHJPEYZBMCZ-FLLNTKIGSA-N (2s)-2-aminopropanoic acid;(4r)-4,5-diamino-5-oxopentanoic acid Chemical compound C[C@H](N)C(O)=O.NC(=O)[C@H](N)CCC(O)=O MWTAHJPEYZBMCZ-FLLNTKIGSA-N 0.000 claims description 7
- 230000002349 favourable effect Effects 0.000 claims description 6
- 239000008194 pharmaceutical composition Substances 0.000 claims description 6
- 241000124008 Mammalia Species 0.000 claims description 5
- 210000001124 body fluid Anatomy 0.000 claims description 4
- 230000002401 inhibitory effect Effects 0.000 claims description 3
- 229940126530 T cell activator Drugs 0.000 claims description 2
- 239000013060 biological fluid Substances 0.000 claims description 2
- 239000003053 toxin Substances 0.000 claims description 2
- 231100000765 toxin Toxicity 0.000 claims description 2
- 102100034343 Integrase Human genes 0.000 claims 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 8
- 230000009918 complex formation Effects 0.000 claims 2
- 230000002255 enzymatic effect Effects 0.000 claims 1
- 238000003745 diagnosis Methods 0.000 abstract description 9
- 238000002255 vaccination Methods 0.000 abstract description 6
- 206010061598 Immunodeficiency Diseases 0.000 abstract description 3
- 208000029462 Immunodeficiency disease Diseases 0.000 abstract description 3
- 230000007813 immunodeficiency Effects 0.000 abstract description 3
- 230000017613 viral reproduction Effects 0.000 abstract description 3
- 241000725303 Human immunodeficiency virus Species 0.000 description 254
- 102000004196 processed proteins & peptides Human genes 0.000 description 120
- 235000018102 proteins Nutrition 0.000 description 114
- 230000036436 anti-hiv Effects 0.000 description 64
- 101000716102 Homo sapiens T-cell surface glycoprotein CD4 Proteins 0.000 description 46
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 46
- 230000027455 binding Effects 0.000 description 46
- 150000001720 carbohydrates Chemical group 0.000 description 44
- 108010048209 Human Immunodeficiency Virus Proteins Proteins 0.000 description 42
- 241000283707 Capra Species 0.000 description 40
- 235000014633 carbohydrates Nutrition 0.000 description 38
- 235000001014 amino acid Nutrition 0.000 description 35
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 32
- 239000002243 precursor Substances 0.000 description 32
- 210000003743 erythrocyte Anatomy 0.000 description 30
- 230000003472 neutralizing effect Effects 0.000 description 30
- 210000004698 lymphocyte Anatomy 0.000 description 29
- 208000031886 HIV Infections Diseases 0.000 description 28
- 208000037357 HIV infectious disease Diseases 0.000 description 28
- 125000003275 alpha amino acid group Chemical group 0.000 description 28
- 230000000694 effects Effects 0.000 description 28
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 28
- 230000009257 reactivity Effects 0.000 description 28
- 238000002360 preparation method Methods 0.000 description 27
- 210000004369 blood Anatomy 0.000 description 26
- 239000008280 blood Substances 0.000 description 26
- 230000002163 immunogen Effects 0.000 description 25
- 102100034349 Integrase Human genes 0.000 description 23
- 230000003053 immunization Effects 0.000 description 23
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 22
- 210000002966 serum Anatomy 0.000 description 22
- 238000002649 immunization Methods 0.000 description 21
- 238000000746 purification Methods 0.000 description 19
- 208000030507 AIDS Diseases 0.000 description 17
- 238000007792 addition Methods 0.000 description 17
- 102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 16
- 241001465754 Metazoa Species 0.000 description 16
- 239000002671 adjuvant Substances 0.000 description 16
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 16
- 238000006243 chemical reaction Methods 0.000 description 16
- 238000004519 manufacturing process Methods 0.000 description 16
- 238000012360 testing method Methods 0.000 description 15
- 238000001262 western blot Methods 0.000 description 15
- 210000000612 antigen-presenting cell Anatomy 0.000 description 14
- 239000011324 bead Substances 0.000 description 14
- 102100037904 CD9 antigen Human genes 0.000 description 13
- 239000002158 endotoxin Substances 0.000 description 13
- 229920006008 lipopolysaccharide Polymers 0.000 description 13
- 239000002953 phosphate buffered saline Substances 0.000 description 13
- 241000283973 Oryctolagus cuniculus Species 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 12
- 230000005875 antibody response Effects 0.000 description 12
- 230000034994 death Effects 0.000 description 12
- 231100000517 death Toxicity 0.000 description 12
- 230000001900 immune effect Effects 0.000 description 12
- 230000006872 improvement Effects 0.000 description 12
- 230000001404 mediated effect Effects 0.000 description 12
- 230000009467 reduction Effects 0.000 description 12
- 230000004044 response Effects 0.000 description 12
- 239000000243 solution Substances 0.000 description 12
- 101710147327 Calcineurin B homologous protein 1 Proteins 0.000 description 11
- 101710205625 Capsid protein p24 Proteins 0.000 description 11
- 102000004127 Cytokines Human genes 0.000 description 11
- 108090000695 Cytokines Proteins 0.000 description 11
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 11
- 101710177166 Phosphoprotein Proteins 0.000 description 11
- 101710149279 Small delta antigen Proteins 0.000 description 11
- 230000030741 antigen processing and presentation Effects 0.000 description 11
- 238000004587 chromatography analysis Methods 0.000 description 11
- 230000005847 immunogenicity Effects 0.000 description 11
- 230000001965 increasing effect Effects 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- 238000006467 substitution reaction Methods 0.000 description 11
- 101710121417 Envelope glycoprotein Proteins 0.000 description 10
- 238000005119 centrifugation Methods 0.000 description 10
- 239000000306 component Substances 0.000 description 10
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 10
- 230000007423 decrease Effects 0.000 description 10
- 238000010790 dilution Methods 0.000 description 10
- 239000012895 dilution Substances 0.000 description 10
- 230000001988 toxicity Effects 0.000 description 10
- 231100000419 toxicity Toxicity 0.000 description 10
- 101710104359 F protein Proteins 0.000 description 9
- 108060003951 Immunoglobulin Proteins 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 239000000460 chlorine Substances 0.000 description 9
- 230000000295 complement effect Effects 0.000 description 9
- 238000010168 coupling process Methods 0.000 description 9
- 239000012634 fragment Substances 0.000 description 9
- 210000000987 immune system Anatomy 0.000 description 9
- 102000018358 immunoglobulin Human genes 0.000 description 9
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 9
- 239000007790 solid phase Substances 0.000 description 9
- 230000008685 targeting Effects 0.000 description 9
- 230000001225 therapeutic effect Effects 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 241001430294 unidentified retrovirus Species 0.000 description 9
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 8
- 206010028980 Neoplasm Diseases 0.000 description 8
- 108010047620 Phytohemagglutinins Proteins 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 8
- 230000008878 coupling Effects 0.000 description 8
- 238000005859 coupling reaction Methods 0.000 description 8
- 238000011161 development Methods 0.000 description 8
- 239000000284 extract Substances 0.000 description 8
- 230000001885 phytohemagglutinin Effects 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- -1 KLTK Proteins 0.000 description 7
- 102000003992 Peroxidases Human genes 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 229910052801 chlorine Inorganic materials 0.000 description 7
- 239000000356 contaminant Substances 0.000 description 7
- 230000009089 cytolysis Effects 0.000 description 7
- 231100000433 cytotoxic Toxicity 0.000 description 7
- 230000001472 cytotoxic effect Effects 0.000 description 7
- 238000010828 elution Methods 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 108040007629 peroxidase activity proteins Proteins 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 238000010791 quenching Methods 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 description 6
- 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
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 6
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 6
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 6
- 238000010521 absorption reaction Methods 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 239000012472 biological sample Substances 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 230000037396 body weight Effects 0.000 description 6
- 230000015556 catabolic process Effects 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 238000006731 degradation reaction Methods 0.000 description 6
- 238000001514 detection method Methods 0.000 description 6
- 231100000673 dose–response relationship Toxicity 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 230000002209 hydrophobic effect Effects 0.000 description 6
- 230000016784 immunoglobulin production Effects 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 239000000543 intermediate Substances 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 6
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 6
- 208000033808 peripheral neuropathy Diseases 0.000 description 6
- 238000004445 quantitative analysis Methods 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 235000002639 sodium chloride Nutrition 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 239000000758 substrate Substances 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 6
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 5
- 239000004472 Lysine Substances 0.000 description 5
- 239000004793 Polystyrene Substances 0.000 description 5
- 241000186429 Propionibacterium Species 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 230000000240 adjuvant effect Effects 0.000 description 5
- 125000003277 amino group Chemical group 0.000 description 5
- 230000000890 antigenic effect Effects 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 230000003013 cytotoxicity Effects 0.000 description 5
- 231100000135 cytotoxicity Toxicity 0.000 description 5
- 239000003814 drug Substances 0.000 description 5
- 239000012149 elution buffer Substances 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 150000002632 lipids Chemical class 0.000 description 5
- 235000018977 lysine Nutrition 0.000 description 5
- 230000007246 mechanism Effects 0.000 description 5
- 230000003647 oxidation Effects 0.000 description 5
- 238000007254 oxidation reaction Methods 0.000 description 5
- 229920002223 polystyrene Polymers 0.000 description 5
- 230000000069 prophylactic effect Effects 0.000 description 5
- 230000000171 quenching effect Effects 0.000 description 5
- 208000011580 syndromic disease Diseases 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 210000002845 virion Anatomy 0.000 description 5
- 108010088751 Albumins Proteins 0.000 description 4
- 102000009027 Albumins Human genes 0.000 description 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
- 101710177291 Gag polyprotein Proteins 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- 101710125418 Major capsid protein Proteins 0.000 description 4
- 102000015636 Oligopeptides Human genes 0.000 description 4
- 108010038807 Oligopeptides Proteins 0.000 description 4
- 208000001388 Opportunistic Infections Diseases 0.000 description 4
- 241000712907 Retroviridae Species 0.000 description 4
- 210000001744 T-lymphocyte Anatomy 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
- 108020000999 Viral RNA Proteins 0.000 description 4
- 230000002159 abnormal effect Effects 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 230000000975 bioactive effect Effects 0.000 description 4
- 125000000837 carbohydrate group Chemical group 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 238000002967 competitive immunoassay Methods 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 230000003247 decreasing effect Effects 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000002581 neurotoxin Substances 0.000 description 4
- 231100000618 neurotoxin Toxicity 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 230000002265 prevention Effects 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 238000011268 retreatment Methods 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 210000000582 semen Anatomy 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 125000006850 spacer group Chemical group 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 4
- 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 3
- JYCQQPHGFMYQCF-UHFFFAOYSA-N 4-tert-Octylphenol monoethoxylate Chemical compound CC(C)(C)CC(C)(C)C1=CC=C(OCCO)C=C1 JYCQQPHGFMYQCF-UHFFFAOYSA-N 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 102000015696 Interleukins Human genes 0.000 description 3
- 108010063738 Interleukins Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 229920005654 Sephadex Polymers 0.000 description 3
- 239000012507 Sephadex™ Substances 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 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 3
- OBETXYAYXDNJHR-UHFFFAOYSA-N alpha-ethylcaproic acid Natural products CCCCC(CC)C(O)=O OBETXYAYXDNJHR-UHFFFAOYSA-N 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 230000002860 competitive effect Effects 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 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 3
- 229940079593 drug Drugs 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- 230000007515 enzymatic degradation Effects 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 230000001605 fetal effect Effects 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 230000035931 haemagglutination Effects 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 238000009169 immunotherapy Methods 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000000411 inducer Substances 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000011835 investigation Methods 0.000 description 3
- 229910052740 iodine Inorganic materials 0.000 description 3
- 210000000265 leukocyte Anatomy 0.000 description 3
- 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 3
- 229920002521 macromolecule Polymers 0.000 description 3
- 238000013507 mapping Methods 0.000 description 3
- 201000001441 melanoma Diseases 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 230000003278 mimic effect Effects 0.000 description 3
- 210000005087 mononuclear cell Anatomy 0.000 description 3
- 231100000252 nontoxic Toxicity 0.000 description 3
- 230000003000 nontoxic effect Effects 0.000 description 3
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 3
- 238000010647 peptide synthesis reaction Methods 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 125000006239 protecting group Chemical group 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 229940031439 squalene Drugs 0.000 description 3
- 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 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000013589 supplement Substances 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 239000000304 virulence factor Substances 0.000 description 3
- 230000007923 virulence factor Effects 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 230000004584 weight gain Effects 0.000 description 3
- 235000019786 weight gain Nutrition 0.000 description 3
- SXGZJKUKBWWHRA-UHFFFAOYSA-N 2-(N-morpholiniumyl)ethanesulfonate Chemical compound [O-]S(=O)(=O)CC[NH+]1CCOCC1 SXGZJKUKBWWHRA-UHFFFAOYSA-N 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- RXACEEPNTRHYBQ-UHFFFAOYSA-N 2-[[2-[[2-[(2-sulfanylacetyl)amino]acetyl]amino]acetyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)CNC(=O)CNC(=O)CS RXACEEPNTRHYBQ-UHFFFAOYSA-N 0.000 description 2
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 101100489887 Arabidopsis thaliana ABA2 gene Proteins 0.000 description 2
- 206010003445 Ascites Diseases 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108010041397 CD4 Antigens Proteins 0.000 description 2
- 102100027221 CD81 antigen Human genes 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 241000700198 Cavia Species 0.000 description 2
- 206010057248 Cell death Diseases 0.000 description 2
- 150000008574 D-amino acids Chemical class 0.000 description 2
- AEFLONBTGZFSGQ-GSVOUGTGSA-N D-isoglutamine Chemical compound NC(=O)[C@H](N)CCC(O)=O AEFLONBTGZFSGQ-GSVOUGTGSA-N 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 102100020743 Dipeptidase 1 Human genes 0.000 description 2
- 102100025137 Early activation antigen CD69 Human genes 0.000 description 2
- 101710091045 Envelope protein Proteins 0.000 description 2
- PIICEJLVQHRZGT-UHFFFAOYSA-N Ethylenediamine Chemical compound NCCN PIICEJLVQHRZGT-UHFFFAOYSA-N 0.000 description 2
- 108700024394 Exon Proteins 0.000 description 2
- 108010003471 Fetal Proteins Proteins 0.000 description 2
- 102000004641 Fetal Proteins Human genes 0.000 description 2
- 102100024017 Glycerol-3-phosphate acyltransferase 3 Human genes 0.000 description 2
- 101100404740 Glycine max INR2 gene Proteins 0.000 description 2
- 108010015899 Glycopeptides Proteins 0.000 description 2
- 102000002068 Glycopeptides Human genes 0.000 description 2
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 2
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 2
- 101000914479 Homo sapiens CD81 antigen Proteins 0.000 description 2
- 101000904259 Homo sapiens Glycerol-3-phosphate acyltransferase 3 Proteins 0.000 description 2
- 101001063392 Homo sapiens Lymphocyte function-associated antigen 3 Proteins 0.000 description 2
- 101000844245 Homo sapiens Non-receptor tyrosine-protein kinase TYK2 Proteins 0.000 description 2
- 101001130226 Homo sapiens Phosphatidylcholine-sterol acyltransferase Proteins 0.000 description 2
- 101000973947 Homo sapiens Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase Proteins 0.000 description 2
- 101100356345 Homo sapiens RETREG2 gene Proteins 0.000 description 2
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 102000000585 Interleukin-9 Human genes 0.000 description 2
- 108010002335 Interleukin-9 Proteins 0.000 description 2
- 208000007766 Kaposi sarcoma Diseases 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- 102100035131 Lipopolysaccharide-binding protein Human genes 0.000 description 2
- 101710089435 Lipopolysaccharide-binding protein Proteins 0.000 description 2
- 102000015930 Lon proteases Human genes 0.000 description 2
- 102100030984 Lymphocyte function-associated antigen 3 Human genes 0.000 description 2
- 101150009428 MAG2 gene Proteins 0.000 description 2
- 102000030612 Melanocortin 5 receptor Human genes 0.000 description 2
- 108010088565 Melanocortin 5 receptor Proteins 0.000 description 2
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 2
- 102000029749 Microtubule Human genes 0.000 description 2
- 108091022875 Microtubule Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 101150065082 NRM1 gene Proteins 0.000 description 2
- 102100032028 Non-receptor tyrosine-protein kinase TYK2 Human genes 0.000 description 2
- 101150046160 POL1 gene Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 102100024968 Peptidyl-prolyl cis-trans isomerase C Human genes 0.000 description 2
- 102100039298 Phosphatidylserine synthase 1 Human genes 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 102100022407 Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase Human genes 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 108010023294 Protease La Proteins 0.000 description 2
- 101710188315 Protein X Proteins 0.000 description 2
- 102100024733 Reticulophagy regulator 2 Human genes 0.000 description 2
- 102100037593 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta Human genes 0.000 description 2
- 101100501251 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) ELO3 gene Proteins 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 101710138331 Somatostatin-1 Proteins 0.000 description 2
- 102100039081 Steroid Delta-isomerase Human genes 0.000 description 2
- 101100117436 Thermus aquaticus polA gene Proteins 0.000 description 2
- 102100030951 Tissue factor pathway inhibitor Human genes 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 102100040247 Tumor necrosis factor Human genes 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000010933 acylation Effects 0.000 description 2
- 238000005917 acylation reaction Methods 0.000 description 2
- 150000001299 aldehydes Chemical class 0.000 description 2
- 229940037003 alum Drugs 0.000 description 2
- 230000009435 amidation Effects 0.000 description 2
- 238000007112 amidation reaction Methods 0.000 description 2
- RDOXTESZEPMUJZ-UHFFFAOYSA-N anisole Chemical compound COC1=CC=CC=C1 RDOXTESZEPMUJZ-UHFFFAOYSA-N 0.000 description 2
- 239000002259 anti human immunodeficiency virus agent Substances 0.000 description 2
- 229940124411 anti-hiv antiviral agent Drugs 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 229940124522 antiretrovirals Drugs 0.000 description 2
- 239000003903 antiretrovirus agent Substances 0.000 description 2
- 230000036528 appetite Effects 0.000 description 2
- 235000019789 appetite Nutrition 0.000 description 2
- 239000008365 aqueous carrier Substances 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 239000012298 atmosphere Substances 0.000 description 2
- 230000001363 autoimmune Effects 0.000 description 2
- 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 2
- 230000005540 biological transmission Effects 0.000 description 2
- 239000012503 blood component Substances 0.000 description 2
- 210000000234 capsid Anatomy 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 229910002091 carbon monoxide Inorganic materials 0.000 description 2
- 125000002091 cationic group Chemical group 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000003196 chaotropic effect Effects 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 210000004748 cultured cell Anatomy 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 108010093254 delta(5)-3 beta-hydroxysteroid dehydrogenase Proteins 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000007661 gastrointestinal function Effects 0.000 description 2
- 238000001641 gel filtration chromatography Methods 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000003394 haemopoietic effect Effects 0.000 description 2
- 230000000984 immunochemical effect Effects 0.000 description 2
- 230000028802 immunoglobulin-mediated neutralization Effects 0.000 description 2
- 230000002637 immunotoxin Effects 0.000 description 2
- 239000002596 immunotoxin Substances 0.000 description 2
- 229940051026 immunotoxin Drugs 0.000 description 2
- 231100000608 immunotoxin Toxicity 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 125000005647 linker group Chemical group 0.000 description 2
- 108010013555 lipoprotein-associated coagulation inhibitor Proteins 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- JQAACYUZYRBHGG-QHTZZOMLSA-L magnesium;(2s)-5-oxopyrrolidine-2-carboxylate Chemical compound [Mg+2].[O-]C(=O)[C@@H]1CCC(=O)N1.[O-]C(=O)[C@@H]1CCC(=O)N1 JQAACYUZYRBHGG-QHTZZOMLSA-L 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 210000004688 microtubule Anatomy 0.000 description 2
- 230000002438 mitochondrial effect Effects 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 230000010807 negative regulation of binding Effects 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 230000036963 noncompetitive effect Effects 0.000 description 2
- 238000007427 paired t-test Methods 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 230000002093 peripheral effect Effects 0.000 description 2
- 230000002688 persistence Effects 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 239000000902 placebo Substances 0.000 description 2
- 229940068196 placebo Drugs 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 239000000700 radioactive tracer Substances 0.000 description 2
- 239000012217 radiopharmaceutical Substances 0.000 description 2
- 229940121896 radiopharmaceutical Drugs 0.000 description 2
- 230000002799 radiopharmaceutical effect Effects 0.000 description 2
- 230000001177 retroviral effect Effects 0.000 description 2
- 210000003296 saliva Anatomy 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 229920006395 saturated elastomer Polymers 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000012279 sodium borohydride Substances 0.000 description 2
- 229910000033 sodium borohydride Inorganic materials 0.000 description 2
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 101150036683 sre1 gene Proteins 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- 108010085346 steroid delta-isomerase Proteins 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 208000010648 susceptibility to HIV infection Diseases 0.000 description 2
- 238000011521 systemic chemotherapy Methods 0.000 description 2
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- TUNFSRHWOTWDNC-UHFFFAOYSA-N tetradecanoic acid Chemical compound CCCCCCCCCCCCCC(O)=O TUNFSRHWOTWDNC-UHFFFAOYSA-N 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 229940126585 therapeutic drug Drugs 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 239000003440 toxic substance Substances 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 238000011269 treatment regimen Methods 0.000 description 2
- 235000002374 tyrosine Nutrition 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 210000000605 viral structure Anatomy 0.000 description 2
- DQJCDTNMLBYVAY-ZXXIYAEKSA-N (2S,5R,10R,13R)-16-{[(2R,3S,4R,5R)-3-{[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}-5-(ethylamino)-6-hydroxy-2-(hydroxymethyl)oxan-4-yl]oxy}-5-(4-aminobutyl)-10-carbamoyl-2,13-dimethyl-4,7,12,15-tetraoxo-3,6,11,14-tetraazaheptadecan-1-oic acid Chemical compound NCCCC[C@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)CC[C@H](C(N)=O)NC(=O)[C@@H](C)NC(=O)C(C)O[C@@H]1[C@@H](NCC)C(O)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 DQJCDTNMLBYVAY-ZXXIYAEKSA-N 0.000 description 1
- DHBXNPKRAUYBTH-UHFFFAOYSA-N 1,1-ethanedithiol Chemical compound CC(S)S DHBXNPKRAUYBTH-UHFFFAOYSA-N 0.000 description 1
- BDNKZNFMNDZQMI-UHFFFAOYSA-N 1,3-diisopropylcarbodiimide Chemical compound CC(C)N=C=NC(C)C BDNKZNFMNDZQMI-UHFFFAOYSA-N 0.000 description 1
- FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 1
- 102100027962 2-5A-dependent ribonuclease Human genes 0.000 description 1
- 108010000834 2-5A-dependent ribonuclease Proteins 0.000 description 1
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- 102100033875 3-oxo-5-alpha-steroid 4-dehydrogenase 2 Human genes 0.000 description 1
- 101710169367 3-oxo-5-alpha-steroid 4-dehydrogenase 2 Proteins 0.000 description 1
- LKUOJDGRNKVVFF-UHFFFAOYSA-N 4-(2,5-dioxopyrrol-1-yl)benzoic acid Chemical compound C1=CC(C(=O)O)=CC=C1N1C(=O)C=CC1=O LKUOJDGRNKVVFF-UHFFFAOYSA-N 0.000 description 1
- CYDQOEWLBCCFJZ-UHFFFAOYSA-N 4-(4-fluorophenyl)oxane-4-carboxylic acid Chemical compound C=1C=C(F)C=CC=1C1(C(=O)O)CCOCC1 CYDQOEWLBCCFJZ-UHFFFAOYSA-N 0.000 description 1
- 108010082808 4-1BB Ligand Proteins 0.000 description 1
- 102000002627 4-1BB Ligand Human genes 0.000 description 1
- OOBICGOWICFMIX-POYBYMJQSA-N 4-amino-1-[(2r,5s)-5-(hydroxymethyl)-2,5-dihydrofuran-2-yl]pyrimidin-2-one Chemical compound O=C1N=C(N)C=CN1[C@H]1C=C[C@@H](CO)O1 OOBICGOWICFMIX-POYBYMJQSA-N 0.000 description 1
- NMHGKQRBLJOZEL-UHFFFAOYSA-N 4-methylbenzenecarbodithioic acid Chemical compound CC1=CC=C(C(S)=S)C=C1 NMHGKQRBLJOZEL-UHFFFAOYSA-N 0.000 description 1
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 1
- 101150060184 ACHE gene Proteins 0.000 description 1
- 102100033639 Acetylcholinesterase Human genes 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000239239 Androctonus Species 0.000 description 1
- 102100030988 Angiotensin-converting enzyme Human genes 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 235000011330 Armoracia rusticana Nutrition 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 102100026292 Asialoglycoprotein receptor 1 Human genes 0.000 description 1
- 101710200897 Asialoglycoprotein receptor 1 Proteins 0.000 description 1
- 102000004580 Aspartic Acid Proteases Human genes 0.000 description 1
- 108010017640 Aspartic Acid Proteases Proteins 0.000 description 1
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000711443 Bovine coronavirus Species 0.000 description 1
- 208000014644 Brain disease Diseases 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000222122 Candida albicans Species 0.000 description 1
- 206010007134 Candida infections Diseases 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 101710082754 Carboxypeptidase S1 homolog B Proteins 0.000 description 1
- 102000003908 Cathepsin D Human genes 0.000 description 1
- 108090000258 Cathepsin D Proteins 0.000 description 1
- 241000239327 Centruroides Species 0.000 description 1
- 108010086232 Cobra Neurotoxin Proteins Proteins 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 102100031051 Cysteine and glycine-rich protein 1 Human genes 0.000 description 1
- 102000016842 Cytokine Receptor Common beta Subunit Human genes 0.000 description 1
- 108010067968 Cytokine Receptor Common beta Subunit Proteins 0.000 description 1
- AHCYMLUZIRLXAA-SHYZEUOFSA-N Deoxyuridine 5'-triphosphate Chemical compound O1[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C[C@@H]1N1C(=O)NC(=O)C=C1 AHCYMLUZIRLXAA-SHYZEUOFSA-N 0.000 description 1
- 102100023933 Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Human genes 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- QOSSAOTZNIDXMA-UHFFFAOYSA-N Dicylcohexylcarbodiimide Chemical compound C1CCCCC1N=C=NC1CCCCC1 QOSSAOTZNIDXMA-UHFFFAOYSA-N 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 208000032274 Encephalopathy Diseases 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 102100038982 Exosome complex component RRP40 Human genes 0.000 description 1
- 239000004606 Fillers/Extenders Substances 0.000 description 1
- KRHYYFGTRYWZRS-UHFFFAOYSA-N Fluorane Chemical compound F KRHYYFGTRYWZRS-UHFFFAOYSA-N 0.000 description 1
- 108050001931 Folate receptor alpha Proteins 0.000 description 1
- 206010016936 Folliculitis Diseases 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 108010063907 Glutathione Reductase Proteins 0.000 description 1
- 102100036442 Glutathione reductase, mitochondrial Human genes 0.000 description 1
- 108010001483 Glycogen Synthase Proteins 0.000 description 1
- 102100031547 HLA class II histocompatibility antigen, DO alpha chain Human genes 0.000 description 1
- 102100036242 HLA class II histocompatibility antigen, DQ alpha 2 chain Human genes 0.000 description 1
- 206010019233 Headaches Diseases 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 108010088652 Histocompatibility Antigens Class I Proteins 0.000 description 1
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 1
- 101100005713 Homo sapiens CD4 gene Proteins 0.000 description 1
- 101000922020 Homo sapiens Cysteine and glycine-rich protein 1 Proteins 0.000 description 1
- 101000941690 Homo sapiens Cytochrome P450 1A1 Proteins 0.000 description 1
- 101000934374 Homo sapiens Early activation antigen CD69 Proteins 0.000 description 1
- 101000866278 Homo sapiens HLA class II histocompatibility antigen, DO alpha chain Proteins 0.000 description 1
- 101000930801 Homo sapiens HLA class II histocompatibility antigen, DQ alpha 2 chain Proteins 0.000 description 1
- 101001005711 Homo sapiens MARVEL domain-containing protein 2 Proteins 0.000 description 1
- 101000687115 Homo sapiens Peptidyl-prolyl cis-trans isomerase C Proteins 0.000 description 1
- 101000652433 Homo sapiens Protein SON Proteins 0.000 description 1
- 101000874179 Homo sapiens Syndecan-1 Proteins 0.000 description 1
- 101000740519 Homo sapiens Syndecan-4 Proteins 0.000 description 1
- 101000847107 Homo sapiens Tetraspanin-8 Proteins 0.000 description 1
- 101900297506 Human immunodeficiency virus type 1 group M subtype B Reverse transcriptase/ribonuclease H Proteins 0.000 description 1
- 208000019758 Hypergammaglobulinemia Diseases 0.000 description 1
- 102000009490 IgG Receptors Human genes 0.000 description 1
- 108010073807 IgG Receptors Proteins 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010061833 Integrases Proteins 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 239000004158 L-cystine Substances 0.000 description 1
- AEFLONBTGZFSGQ-VKHMYHEASA-N L-isoglutamine Chemical group NC(=O)[C@@H](N)CCC(O)=O AEFLONBTGZFSGQ-VKHMYHEASA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- 241000713102 La Crosse virus Species 0.000 description 1
- 102100038420 Leukocyte tyrosine kinase receptor Human genes 0.000 description 1
- 101710139457 Leukocyte tyrosine kinase receptor Proteins 0.000 description 1
- 208000008771 Lymphadenopathy Diseases 0.000 description 1
- 102000043131 MHC class II family Human genes 0.000 description 1
- 108091054438 MHC class II family Proteins 0.000 description 1
- 206010025476 Malabsorption Diseases 0.000 description 1
- 208000004155 Malabsorption Syndromes Diseases 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 208000000112 Myalgia Diseases 0.000 description 1
- 201000003793 Myelodysplastic syndrome Diseases 0.000 description 1
- 102000005604 Myosin Heavy Chains Human genes 0.000 description 1
- 108010084498 Myosin Heavy Chains Proteins 0.000 description 1
- JGFZNNIVVJXRND-UHFFFAOYSA-N N,N-diisopropylethylamine Substances CCN(C(C)C)C(C)C JGFZNNIVVJXRND-UHFFFAOYSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 241000272041 Naja Species 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 102100034217 Non-secretory ribonuclease Human genes 0.000 description 1
- 101710118518 Non-secretory ribonuclease Proteins 0.000 description 1
- 230000006179 O-acylation Effects 0.000 description 1
- 108700026244 Open Reading Frames Proteins 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
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 1
- 102100031538 Phosphatidylcholine-sterol acyltransferase Human genes 0.000 description 1
- 102100026918 Phospholipase A2 Human genes 0.000 description 1
- 102000004422 Phospholipase C gamma Human genes 0.000 description 1
- 108010056751 Phospholipase C gamma Proteins 0.000 description 1
- 108010058864 Phospholipases A2 Proteins 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 108010076039 Polyproteins Proteins 0.000 description 1
- 101710152616 Probable major capsid protein gp17 Proteins 0.000 description 1
- 102100030350 Prolactin-inducible protein Human genes 0.000 description 1
- 101710145576 Prostaglandin-H2 D-isomerase Proteins 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 102000003923 Protein Kinase C Human genes 0.000 description 1
- 108090000315 Protein Kinase C Proteins 0.000 description 1
- 108010078762 Protein Precursors Proteins 0.000 description 1
- 102000014961 Protein Precursors Human genes 0.000 description 1
- 102100030232 Protein SON Human genes 0.000 description 1
- 101710149951 Protein Tat Proteins 0.000 description 1
- 102000004669 Protein-Lysine 6-Oxidase Human genes 0.000 description 1
- 108010003894 Protein-Lysine 6-Oxidase Proteins 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 102000044126 RNA-Binding Proteins Human genes 0.000 description 1
- 108700020471 RNA-Binding Proteins Proteins 0.000 description 1
- 239000012979 RPMI medium Substances 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010038910 Retinitis Diseases 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 102000004389 Ribonucleoproteins Human genes 0.000 description 1
- 108010081734 Ribonucleoproteins Proteins 0.000 description 1
- 101100099198 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) TGL3 gene Proteins 0.000 description 1
- 239000002262 Schiff base Substances 0.000 description 1
- 150000004753 Schiff bases Chemical class 0.000 description 1
- 102100037550 Semenogelin-1 Human genes 0.000 description 1
- 101710089345 Semenogelin-1 Proteins 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 102100023153 Sodium- and chloride-dependent creatine transporter 1 Human genes 0.000 description 1
- 101710162246 Sodium- and chloride-dependent creatine transporter 1 Proteins 0.000 description 1
- 101710109667 Spectrin beta chain Proteins 0.000 description 1
- 229930182558 Sterol Natural products 0.000 description 1
- 102100035721 Syndecan-1 Human genes 0.000 description 1
- 102100037220 Syndecan-4 Human genes 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 102100032802 Tetraspanin-8 Human genes 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 230000010530 Virus Neutralization Effects 0.000 description 1
- 244000195452 Wasabia japonica Species 0.000 description 1
- 235000000760 Wasabia japonica Nutrition 0.000 description 1
- 238000001793 Wilcoxon signed-rank test Methods 0.000 description 1
- 102000052556 Wnt-2 Human genes 0.000 description 1
- 108700020986 Wnt-2 Proteins 0.000 description 1
- WREGKURFCTUGRC-POYBYMJQSA-N Zalcitabine Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](CO)CC1 WREGKURFCTUGRC-POYBYMJQSA-N 0.000 description 1
- 102100024670 Zinc finger protein 45 Human genes 0.000 description 1
- 101710160545 Zinc finger protein 45 Proteins 0.000 description 1
- WPQJPSQLCKEBJD-UHFFFAOYSA-N [dichloro-[dichloro(phenyl)methoxy]methyl]benzene Chemical compound C=1C=CC=CC=1C(Cl)(Cl)OC(Cl)(Cl)C1=CC=CC=C1 WPQJPSQLCKEBJD-UHFFFAOYSA-N 0.000 description 1
- 239000002250 absorbent Substances 0.000 description 1
- 230000002745 absorbent Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 210000000677 aggregate cell Anatomy 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229960002684 aminocaproic acid Drugs 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 230000009227 antibody-mediated cytotoxicity Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 230000000386 athletic effect Effects 0.000 description 1
- 201000004339 autoimmune neuropathy Diseases 0.000 description 1
- 238000011888 autopsy Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000012740 beta Adrenergic Receptors Human genes 0.000 description 1
- 108010079452 beta Adrenergic Receptors Proteins 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 238000011953 bioanalysis Methods 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000012267 brine Substances 0.000 description 1
- 210000004900 c-terminal fragment Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 201000003984 candidiasis Diseases 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000034303 cell budding Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000003855 cell nucleus Anatomy 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 210000003850 cellular structure Anatomy 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 210000003756 cervix mucus Anatomy 0.000 description 1
- 125000003636 chemical group Chemical group 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 125000001309 chloro group Chemical group Cl* 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 239000013527 degreasing agent Substances 0.000 description 1
- 238000005237 degreasing agent Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- MHDVGSVTJDSBDK-UHFFFAOYSA-N dibenzyl ether Chemical compound C=1C=CC=CC=1COCC1=CC=CC=C1 MHDVGSVTJDSBDK-UHFFFAOYSA-N 0.000 description 1
- BGRWYRAHAFMIBJ-UHFFFAOYSA-N diisopropylcarbodiimide Natural products CC(C)NC(=O)NC(C)C BGRWYRAHAFMIBJ-UHFFFAOYSA-N 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
- 230000005750 disease progression Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 230000002327 eosinophilic effect Effects 0.000 description 1
- BSGRLBPZSRZQOR-UHFFFAOYSA-N ethene-1,1-diamine Chemical group NC(N)=C BSGRLBPZSRZQOR-UHFFFAOYSA-N 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 101150052370 fol1 gene Proteins 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000007973 glycine-HCl buffer Substances 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 231100000869 headache Toxicity 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 231100000171 higher toxicity Toxicity 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 229910000040 hydrogen fluoride Inorganic materials 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000005965 immune activity Effects 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 206010021654 increased appetite Diseases 0.000 description 1
- 230000008595 infiltration Effects 0.000 description 1
- 238000001764 infiltration Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 210000001821 langerhans cell Anatomy 0.000 description 1
- 230000021633 leukocyte mediated immunity Effects 0.000 description 1
- 239000003446 ligand Substances 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
- 239000002502 liposome Substances 0.000 description 1
- 239000013541 low molecular weight contaminant Substances 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 208000010949 lymph node disease Diseases 0.000 description 1
- 239000006249 magnetic particle Substances 0.000 description 1
- FPYJFEHAWHCUMM-UHFFFAOYSA-N maleic anhydride Chemical compound O=C1OC(=O)C=C1 FPYJFEHAWHCUMM-UHFFFAOYSA-N 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- UZKWTJUDCOPSNM-UHFFFAOYSA-N methoxybenzene Substances CCCCOC=C UZKWTJUDCOPSNM-UHFFFAOYSA-N 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 208000030247 mild fever Diseases 0.000 description 1
- 239000003226 mitogen Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- BSOQXXWZTUDTEL-QAQREVAFSA-N muramyl dipeptide Chemical compound OC(=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 BSOQXXWZTUDTEL-QAQREVAFSA-N 0.000 description 1
- 125000001446 muramyl group Chemical group N[C@@H](C=O)[C@@H](O[C@@H](C(=O)*)C)[C@H](O)[C@H](O)CO 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
- 230000035772 mutation Effects 0.000 description 1
- 229940105132 myristate Drugs 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000012177 negative regulation of immune response Effects 0.000 description 1
- 201000001119 neuropathy Diseases 0.000 description 1
- 230000007823 neuropathy Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 239000002547 new drug Substances 0.000 description 1
- 231100000065 noncytotoxic Toxicity 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 239000012044 organic layer Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 239000013618 particulate matter Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000000149 penetrating effect Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 239000012071 phase Substances 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
- 230000004962 physiological condition Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- PJPOCNJHYFUPCE-UHFFFAOYSA-N picen-1-ol Chemical compound C1=CC=CC2=C(C=CC=3C4=CC=C5C=CC=C(C=35)O)C4=CC=C21 PJPOCNJHYFUPCE-UHFFFAOYSA-N 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 231100000572 poisoning Toxicity 0.000 description 1
- 230000000607 poisoning effect Effects 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920001308 poly(aminoacid) Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 230000009993 protective function Effects 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 239000002516 radical scavenger Substances 0.000 description 1
- 239000000941 radioactive substance Substances 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 108010066490 ribonuclease 4 Proteins 0.000 description 1
- 239000003419 rna directed dna polymerase inhibitor Substances 0.000 description 1
- 239000012898 sample dilution Substances 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000012882 sequential analysis Methods 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 208000026775 severe diarrhea Diseases 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001540 sodium lactate Substances 0.000 description 1
- 229940005581 sodium lactate Drugs 0.000 description 1
- 235000011088 sodium lactate Nutrition 0.000 description 1
- HPALAKNZSZLMCH-UHFFFAOYSA-M sodium;chloride;hydrate Chemical compound O.[Na+].[Cl-] HPALAKNZSZLMCH-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000007103 stamina Effects 0.000 description 1
- 230000003335 steric effect Effects 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 150000003432 sterols Chemical class 0.000 description 1
- 235000003702 sterols Nutrition 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 229940014800 succinic anhydride Drugs 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 210000000225 synapse Anatomy 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 238000011285 therapeutic regimen Methods 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 238000012549 training Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 230000029812 viral genome replication Effects 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- HBOMLICNUCNMMY-XLPZGREQSA-N zidovudine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](N=[N+]=[N-])C1 HBOMLICNUCNMMY-XLPZGREQSA-N 0.000 description 1
- 230000004572 zinc-binding Effects 0.000 description 1
- BVGLZNQZEYAYBJ-QWZQWHGGSA-N α-cobratoxin Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CC(C)C)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)CC1=CC=C(O)C=C1 BVGLZNQZEYAYBJ-QWZQWHGGSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/70—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving virus or bacteriophage
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/39—Medicinal preparations containing antigens or antibodies characterised by the immunostimulating additives, e.g. chemical adjuvants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1054—Lentiviridae, e.g. HIV, FIV, SIV gag-pol, e.g. p17, p24
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- 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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55511—Organic adjuvants
- A61K2039/5555—Muramyl dipeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/06—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Oncology (AREA)
- AIDS & HIV (AREA)
- Hematology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Epidemiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Engineering & Computer Science (AREA)
- Mycology (AREA)
- Zoology (AREA)
- Dermatology (AREA)
- Gastroenterology & Hepatology (AREA)
- Wood Science & Technology (AREA)
- Communicable Diseases (AREA)
- Biotechnology (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Tropical Medicine & Parasitology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US2819496P | 1996-10-10 | 1996-10-10 | |
| US60/028,194 | 1996-10-10 | ||
| KR1019997003052A KR100547049B1 (ko) | 1996-10-10 | 1997-10-10 | 바이러스 감염증 치료를 위한 조성물 및 방법 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019997003052A Division KR100547049B1 (ko) | 1996-10-10 | 1997-10-10 | 바이러스 감염증 치료를 위한 조성물 및 방법 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR20060041157A KR20060041157A (ko) | 2006-05-11 |
| KR100667121B1 true KR100667121B1 (ko) | 2007-01-12 |
Family
ID=21842081
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1020057016920A Expired - Lifetime KR100667121B1 (ko) | 1996-10-10 | 1997-10-10 | 바이러스 감염증 치료를 위한 조성물 및 방법 |
| KR1019997003052A Expired - Lifetime KR100547049B1 (ko) | 1996-10-10 | 1997-10-10 | 바이러스 감염증 치료를 위한 조성물 및 방법 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019997003052A Expired - Lifetime KR100547049B1 (ko) | 1996-10-10 | 1997-10-10 | 바이러스 감염증 치료를 위한 조성물 및 방법 |
Country Status (11)
| Country | Link |
|---|---|
| US (6) | US6043347A (enExample) |
| EP (1) | EP0939835A4 (enExample) |
| JP (2) | JP2001502315A (enExample) |
| KR (2) | KR100667121B1 (enExample) |
| CN (1) | CN1327896C (enExample) |
| AU (1) | AU732809B2 (enExample) |
| BR (1) | BR9712289A (enExample) |
| CA (1) | CA2268372C (enExample) |
| MX (1) | MXPA02010374A (enExample) |
| NZ (1) | NZ334941A (enExample) |
| WO (1) | WO1998015658A1 (enExample) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2268372C (en) * | 1996-10-10 | 2012-11-27 | Probe International | Compositions and methods for treating viral infections |
| US7157091B1 (en) * | 1999-06-18 | 2007-01-02 | Ludwig Institute For Cancer Research | MAGE-A1 peptides presented by HLA class II molecules |
| US6599441B1 (en) * | 2000-07-18 | 2003-07-29 | Emerald Biostructures, Inc. | Crystallization solutions |
| CN1339319A (zh) * | 2000-08-18 | 2002-03-13 | 清华大学 | 一种治疗艾滋病的药物及其制备方法 |
| US6987184B2 (en) * | 2001-02-15 | 2006-01-17 | Signal Pharmaceuticals, Llc | Isothiazoloanthrones, isoxazoloanthrones, isoindolanthrones and derivatives thereof as JNK inhibitors and compositions and methods related |
| JP2007524609A (ja) * | 2003-04-10 | 2007-08-30 | トランスフォーム・ファーマシューティカルズ・インコーポレイテッド | コンフォメーションに関する変種のプロファイリング、抗体組成物 |
| US7206991B2 (en) * | 2003-10-15 | 2007-04-17 | Lsi Logic Corporation | Method, apparatus and program for migrating between striped storage and parity striped storage |
| US7311928B2 (en) * | 2003-12-09 | 2007-12-25 | Briant Burke | Topical compositions containing tea tree oil for treatment of viral lesions |
| US7723063B2 (en) * | 2004-04-28 | 2010-05-25 | Intrinsic Lifesciences | Methods for measuring levels of bioactive human hepcidin |
| US20060110405A1 (en) * | 2004-08-20 | 2006-05-25 | Buckheit Robert W Jr | Plasma or serum fraction for treatment and prevention of viral infections and related conditions |
| NZ587255A (en) * | 2005-01-13 | 2012-03-30 | Novartis Vaccines & Diagnostic | Elisa assays using prion-specific peptide reagents |
| EP1855112A1 (en) * | 2006-05-10 | 2007-11-14 | Inserm | Method for the in vitro screening of compounds inhibiting production of infectious HIV-1 virions |
| US8200520B2 (en) | 2007-10-03 | 2012-06-12 | International Business Machines Corporation | Methods, systems, and apparatuses for automated confirmations of meetings |
| JP5662309B2 (ja) * | 2008-04-01 | 2015-01-28 | イネイト・イムノセラピューティクス・リミテッド | 腫瘍性疾患を治療するための組成物および方法 |
| CA2719252C (en) * | 2008-04-01 | 2016-01-19 | Innate Therapeutics Limited | Anti-infective agents comprising muramyl dipeptide microparticles and uses thereof |
| NZ571665A (en) * | 2008-09-30 | 2011-01-28 | Innate Therapeutics Ltd | Compositions and methods for treatment of radiation exposure utilising cross-linked muramyl dipeptide microparticles |
| JPWO2010134305A1 (ja) | 2009-05-18 | 2012-11-08 | 国立大学法人 東京医科歯科大学 | Ｈｉｖ立体構造認識抗体誘導ペプチド抗原、及びその合成方法 |
| NZ577731A (en) * | 2009-06-16 | 2010-08-27 | Innate Therapeutics Ltd | Compositions and methods for treatment of multiple sclerosis |
| CA2793959C (en) | 2010-03-25 | 2019-06-04 | Oregon Health & Science University | Cmv glycoproteins and recombinant vectors |
| RU2517084C2 (ru) * | 2010-08-06 | 2014-05-27 | Олег Ильич Эпштейн | Способ и средство для ингибирования продукции или усиления элиминации белка р24 |
| CN103502264A (zh) | 2011-04-04 | 2014-01-08 | 国立大学法人东京医科齿科大学 | Hiv立体结构识别抗体诱导肽 |
| PT2691530T (pt) | 2011-06-10 | 2018-05-10 | Univ Oregon Health & Science | Glicoproteínas e vectores recombinantes cmv |
| EP2568289A3 (en) | 2011-09-12 | 2013-04-03 | International AIDS Vaccine Initiative | Immunoselection of recombinant vesicular stomatitis virus expressing hiv-1 proteins by broadly neutralizing antibodies |
| EP2586461A1 (en) | 2011-10-27 | 2013-05-01 | Christopher L. Parks | Viral particles derived from an enveloped virus |
| ES2631608T3 (es) | 2012-06-27 | 2017-09-01 | International Aids Vaccine Initiative | Variante de la glicoproteína Env del VIH-1 |
| US20150065381A1 (en) | 2013-09-05 | 2015-03-05 | International Aids Vaccine Initiative | Methods of identifying novel hiv-1 immunogens |
| EP2873423B1 (en) | 2013-10-07 | 2017-05-31 | International Aids Vaccine Initiative | Soluble hiv-1 envelope glycoprotein trimers |
| US10174292B2 (en) | 2015-03-20 | 2019-01-08 | International Aids Vaccine Initiative | Soluble HIV-1 envelope glycoprotein trimers |
| US9931394B2 (en) | 2015-03-23 | 2018-04-03 | International Aids Vaccine Initiative | Soluble HIV-1 envelope glycoprotein trimers |
| WO2017093985A1 (en) * | 2015-12-05 | 2017-06-08 | Centre Hospitalier Universitaire Vaudois | Hiv binding agents |
| CN108997482B (zh) * | 2018-08-09 | 2025-09-09 | 东莞市朋志生物科技有限公司 | 用于检测hiv-1的合成肽 |
| EP3996815A2 (en) * | 2019-07-15 | 2022-05-18 | Lausanne University Hospital | Hiv binding agents |
| AU2022208435A1 (en) | 2021-01-18 | 2023-08-10 | Conserv Bioscience Limited | Coronavirus immunogenic compositions, methods and uses thereof |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5528933A (en) * | 1978-08-21 | 1980-02-29 | Dai Ichi Seiyaku Co Ltd | Muramyldipeptide dimer |
| CA1341482C (en) * | 1984-10-31 | 2005-05-10 | Paul A. Luciw | Process for preparing fragments of aids-associated retroviruses |
| US4946945A (en) * | 1987-06-23 | 1990-08-07 | Allergy Immuno Technologies, Inc. | Immunotherapy agents for treatment of IgE mediated allergies |
| US5128319A (en) * | 1987-08-28 | 1992-07-07 | Board Of Regents, The University Of Texas System | Prophylaxis and therapy of acquired immunodeficiency syndrome |
| CA2025634A1 (en) * | 1989-09-19 | 1991-03-20 | Thomas Fuerst | Peptides including ctl epitopes of hiv proteins and use thereof |
| US6565842B1 (en) | 1995-06-07 | 2003-05-20 | American Bioscience, Inc. | Crosslinkable polypeptide compositions |
| CA2268372C (en) * | 1996-10-10 | 2012-11-27 | Probe International | Compositions and methods for treating viral infections |
-
1997
- 1997-10-10 CA CA2268372A patent/CA2268372C/en not_active Expired - Lifetime
- 1997-10-10 US US08/948,782 patent/US6043347A/en not_active Expired - Lifetime
- 1997-10-10 KR KR1020057016920A patent/KR100667121B1/ko not_active Expired - Lifetime
- 1997-10-10 CN CNB971987432A patent/CN1327896C/zh not_active Expired - Lifetime
- 1997-10-10 EP EP97910856A patent/EP0939835A4/en not_active Withdrawn
- 1997-10-10 AU AU48131/97A patent/AU732809B2/en not_active Expired
- 1997-10-10 BR BR9712289-0A patent/BR9712289A/pt not_active Application Discontinuation
- 1997-10-10 KR KR1019997003052A patent/KR100547049B1/ko not_active Expired - Lifetime
- 1997-10-10 WO PCT/US1997/018257 patent/WO1998015658A1/en not_active Ceased
- 1997-10-10 NZ NZ334941A patent/NZ334941A/xx not_active IP Right Cessation
- 1997-10-10 MX MXPA02010374A patent/MXPA02010374A/es active IP Right Grant
- 1997-10-10 JP JP10517749A patent/JP2001502315A/ja not_active Ceased
-
2000
- 2000-01-14 US US09/482,612 patent/US6258599B1/en not_active Expired - Lifetime
- 2000-10-02 US US09/677,554 patent/US6335017B1/en not_active Expired - Lifetime
-
2001
- 2001-11-05 US US09/985,581 patent/US6670181B2/en not_active Expired - Lifetime
-
2003
- 2003-10-28 US US10/695,112 patent/US20040141996A1/en not_active Abandoned
-
2006
- 2006-11-28 US US11/605,017 patent/US8110203B2/en not_active Expired - Fee Related
-
2008
- 2008-10-06 JP JP2008259812A patent/JP2009080118A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP0939835A1 (en) | 1999-09-08 |
| CA2268372C (en) | 2012-11-27 |
| KR20060041157A (ko) | 2006-05-11 |
| JP2009080118A (ja) | 2009-04-16 |
| HK1023371A1 (en) | 2000-09-08 |
| US20020086034A1 (en) | 2002-07-04 |
| NZ334941A (en) | 2000-11-24 |
| US6335017B1 (en) | 2002-01-01 |
| AU732809B2 (en) | 2001-05-03 |
| JP2001502315A (ja) | 2001-02-20 |
| AU4813197A (en) | 1998-05-05 |
| MXPA02010374A (es) | 2003-04-25 |
| CN1327896C (zh) | 2007-07-25 |
| BR9712289A (pt) | 1999-08-31 |
| CN1234078A (zh) | 1999-11-03 |
| KR100547049B1 (ko) | 2006-02-01 |
| US6670181B2 (en) | 2003-12-30 |
| US6043347A (en) | 2000-03-28 |
| CA2268372A1 (en) | 1998-04-16 |
| EP0939835A4 (en) | 2004-10-27 |
| WO1998015658A1 (en) | 1998-04-16 |
| US20070154917A1 (en) | 2007-07-05 |
| US6258599B1 (en) | 2001-07-10 |
| KR20000048994A (ko) | 2000-07-25 |
| US20040141996A1 (en) | 2004-07-22 |
| US8110203B2 (en) | 2012-02-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR100667121B1 (ko) | 바이러스 감염증 치료를 위한 조성물 및 방법 | |
| US5166050A (en) | Monoclonal antibodies and peptides useful in treating and diagnosing HIV infections | |
| KR920008744B1 (ko) | Hiv 감염의 치료 및 진단용 모노클로날항체 및 펩티드 | |
| US20030003440A1 (en) | Novel CCR5 epitope and antibodies against it | |
| US5834599A (en) | Immunoconjugates which neutralize HIV-1 infection | |
| JPH04506004A (ja) | Ｈｉｖのｃｄ４結合領域に特異的な抗体 | |
| CA1341391C (en) | Protective peptides derived from human immunodeficiency virus-1 gp160 | |
| JPH05506142A (ja) | Ｈｉｖ蛋白質の非免疫支配エピトープに特異的なモノクローナル抗体 | |
| AU2006200454B2 (en) | Compositions and methods for treating viral infections | |
| US6290963B1 (en) | Anti-HIV compositions containing native and recombinant peptides | |
| MXPA99003380A (en) | Compositions and methods for treating viral infections | |
| HK1023371B (en) | Compositions and methods for treating viral infections | |
| AU2004201322A1 (en) | Compositions and methods for treating viral infections | |
| AU2004208648A1 (en) | Compositions and methods for treating infections | |
| AU2006200455A1 (en) | Compositions and methods for treating viral infections | |
| JP2007534615A (ja) | Ｈｉｖ免疫原性複合体 | |
| PL161520B1 (pl) | Sposób wytwarzania nowego peptydu PL |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A107 | Divisional application of patent | ||
| A201 | Request for examination | ||
| PA0104 | Divisional application for international application |
Comment text: Divisional Application for International Patent Patent event code: PA01041R01D Patent event date: 20050909 |
|
| PA0201 | Request for examination | ||
| PG1501 | Laying open of application | ||
| E902 | Notification of reason for refusal | ||
| PE0902 | Notice of grounds for rejection |
Comment text: Notification of reason for refusal Patent event date: 20060523 Patent event code: PE09021S01D |
|
| E701 | Decision to grant or registration of patent right | ||
| PE0701 | Decision of registration |
Patent event code: PE07011S01D Comment text: Decision to Grant Registration Patent event date: 20061123 |
|
| GRNT | Written decision to grant | ||
| PR0701 | Registration of establishment |
Comment text: Registration of Establishment Patent event date: 20070104 Patent event code: PR07011E01D |
|
| PR1002 | Payment of registration fee |
Payment date: 20070105 End annual number: 3 Start annual number: 1 |
|
| PG1601 | Publication of registration | ||
| PR1001 | Payment of annual fee |
Payment date: 20100210 Start annual number: 4 End annual number: 4 |
|
| PR1001 | Payment of annual fee |
Payment date: 20101222 Start annual number: 5 End annual number: 5 |
|
| PR1001 | Payment of annual fee |
Payment date: 20120104 Start annual number: 6 End annual number: 6 |
|
| FPAY | Annual fee payment |
Payment date: 20130103 Year of fee payment: 7 |
|
| PR1001 | Payment of annual fee |
Payment date: 20130103 Start annual number: 7 End annual number: 7 |
|
| FPAY | Annual fee payment |
Payment date: 20140103 Year of fee payment: 8 |
|
| PR1001 | Payment of annual fee |
Payment date: 20140103 Start annual number: 8 End annual number: 8 |
|
| FPAY | Annual fee payment |
Payment date: 20150102 Year of fee payment: 9 |
|
| PR1001 | Payment of annual fee |
Payment date: 20150102 Start annual number: 9 End annual number: 9 |
|
| FPAY | Annual fee payment |
Payment date: 20160104 Year of fee payment: 10 |
|
| PR1001 | Payment of annual fee |
Payment date: 20160104 Start annual number: 10 End annual number: 10 |
|
| FPAY | Annual fee payment |
Payment date: 20170102 Year of fee payment: 11 |
|
| PR1001 | Payment of annual fee |
Payment date: 20170102 Start annual number: 11 End annual number: 11 |
|
| EXPY | Expiration of term | ||
| PC1801 | Expiration of term |
Termination date: 20180410 Termination category: Expiration of duration |