JP2002507391A - 繊維ノブのｈｉループに異種ペプチドエピトープを含有するアデノウイルスベクター - Google Patents
繊維ノブのｈｉループに異種ペプチドエピトープを含有するアデノウイルスベクターInfo
- Publication number
- JP2002507391A JP2002507391A JP2000530231A JP2000530231A JP2002507391A JP 2002507391 A JP2002507391 A JP 2002507391A JP 2000530231 A JP2000530231 A JP 2000530231A JP 2000530231 A JP2000530231 A JP 2000530231A JP 2002507391 A JP2002507391 A JP 2002507391A
- Authority
- JP
- Japan
- Prior art keywords
- fiber
- cells
- adenovirus
- gene
- knob
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 239000000835 fiber Substances 0.000 title claims abstract description 233
- 241000701161 unidentified adenovirus Species 0.000 title claims abstract description 194
- 239000013598 vector Substances 0.000 title claims abstract description 140
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 44
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 247
- 238000000034 method Methods 0.000 claims abstract description 67
- 230000010415 tropism Effects 0.000 claims abstract description 27
- 210000004027 cell Anatomy 0.000 claims description 369
- 238000012546 transfer Methods 0.000 claims description 84
- 239000003446 ligand Substances 0.000 claims description 50
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 claims description 49
- 206010028980 Neoplasm Diseases 0.000 claims description 35
- 230000004048 modification Effects 0.000 claims description 22
- 238000012986 modification Methods 0.000 claims description 22
- 238000001415 gene therapy Methods 0.000 claims description 19
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 16
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 claims description 15
- 238000001727 in vivo Methods 0.000 claims description 13
- 230000001965 increasing effect Effects 0.000 claims description 13
- 210000004881 tumor cell Anatomy 0.000 claims description 12
- 238000000338 in vitro Methods 0.000 claims description 9
- 229920001184 polypeptide Polymers 0.000 claims description 9
- 230000001225 therapeutic effect Effects 0.000 claims description 9
- 238000007910 systemic administration Methods 0.000 claims description 8
- 201000011510 cancer Diseases 0.000 claims description 7
- 201000010099 disease Diseases 0.000 claims description 7
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 7
- 229940104230 thymidine Drugs 0.000 claims description 5
- 208000009889 Herpes Simplex Diseases 0.000 claims description 4
- 108091000080 Phosphotransferase Proteins 0.000 claims description 4
- 230000001851 biosynthetic effect Effects 0.000 claims description 3
- 230000002147 killing effect Effects 0.000 claims description 3
- 201000003883 Cystic fibrosis Diseases 0.000 claims description 2
- IRSCQMHQWWYFCW-UHFFFAOYSA-N ganciclovir Chemical compound O=C1NC(N)=NC2=C1N=CN2COC(CO)CO IRSCQMHQWWYFCW-UHFFFAOYSA-N 0.000 claims description 2
- 229960002963 ganciclovir Drugs 0.000 claims description 2
- 206010013801 Duchenne Muscular Dystrophy Diseases 0.000 claims 1
- 108700026758 Adenovirus hexon capsid Proteins 0.000 abstract description 11
- 230000002068 genetic effect Effects 0.000 abstract description 10
- 102000014914 Carrier Proteins Human genes 0.000 abstract 1
- 108091008324 binding proteins Proteins 0.000 abstract 1
- 241000700605 Viruses Species 0.000 description 94
- 235000018102 proteins Nutrition 0.000 description 90
- 102000004169 proteins and genes Human genes 0.000 description 90
- 108060001084 Luciferase Proteins 0.000 description 74
- 239000005089 Luciferase Substances 0.000 description 68
- 230000014509 gene expression Effects 0.000 description 68
- 208000015181 infectious disease Diseases 0.000 description 55
- 230000000694 effects Effects 0.000 description 52
- 108010044426 integrins Proteins 0.000 description 51
- 102000006495 integrins Human genes 0.000 description 51
- 108020004414 DNA Proteins 0.000 description 45
- 238000002474 experimental method Methods 0.000 description 45
- 230000001404 mediated effect Effects 0.000 description 44
- 210000002845 virion Anatomy 0.000 description 44
- 239000013612 plasmid Substances 0.000 description 42
- 206010061535 Ovarian neoplasm Diseases 0.000 description 41
- 101710145505 Fiber protein Proteins 0.000 description 40
- 206010033128 Ovarian cancer Diseases 0.000 description 38
- 230000003993 interaction Effects 0.000 description 33
- 239000012634 fragment Substances 0.000 description 32
- 210000001519 tissue Anatomy 0.000 description 29
- 238000003556 assay Methods 0.000 description 27
- 239000000499 gel Substances 0.000 description 26
- 102000005962 receptors Human genes 0.000 description 26
- 108020003175 receptors Proteins 0.000 description 26
- 230000008685 targeting Effects 0.000 description 26
- 238000004458 analytical method Methods 0.000 description 25
- 238000010348 incorporation Methods 0.000 description 25
- 201000000459 head and neck squamous cell carcinoma Diseases 0.000 description 24
- 238000010361 transduction Methods 0.000 description 24
- 230000026683 transduction Effects 0.000 description 24
- 210000000056 organ Anatomy 0.000 description 22
- 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 21
- 238000000684 flow cytometry Methods 0.000 description 21
- 239000002609 medium Substances 0.000 description 21
- 239000002953 phosphate buffered saline Substances 0.000 description 21
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 20
- 108091026890 Coding region Proteins 0.000 description 19
- 238000001476 gene delivery Methods 0.000 description 19
- 239000000523 sample Substances 0.000 description 19
- 108010020195 FLAG peptide Proteins 0.000 description 18
- 238000011534 incubation Methods 0.000 description 18
- 238000013459 approach Methods 0.000 description 17
- 230000005764 inhibitory process Effects 0.000 description 17
- 239000002245 particle Substances 0.000 description 17
- 206010003445 Ascites Diseases 0.000 description 15
- XZWYTXMRWQJBGX-VXBMVYAYSA-N FLAG peptide Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)CC1=CC=C(O)C=C1 XZWYTXMRWQJBGX-VXBMVYAYSA-N 0.000 description 15
- 108700019146 Transgenes Proteins 0.000 description 15
- 210000004185 liver Anatomy 0.000 description 15
- 239000013638 trimer Substances 0.000 description 14
- 241000701447 unidentified baculovirus Species 0.000 description 14
- 102000004190 Enzymes Human genes 0.000 description 13
- 108090000790 Enzymes Proteins 0.000 description 13
- 230000001413 cellular effect Effects 0.000 description 13
- 229940088598 enzyme Drugs 0.000 description 13
- 238000005259 measurement Methods 0.000 description 13
- 230000037361 pathway Effects 0.000 description 13
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 12
- 230000015572 biosynthetic process Effects 0.000 description 12
- 238000000746 purification Methods 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 11
- 230000000903 blocking effect Effects 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 239000006166 lysate Substances 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 241000588724 Escherichia coli Species 0.000 description 10
- 241000238631 Hexapoda Species 0.000 description 10
- 108091028043 Nucleic acid sequence Proteins 0.000 description 10
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 229940098773 bovine serum albumin Drugs 0.000 description 10
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 10
- 238000000159 protein binding assay Methods 0.000 description 10
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 9
- 210000004899 c-terminal region Anatomy 0.000 description 9
- 238000012239 gene modification Methods 0.000 description 9
- 230000002611 ovarian Effects 0.000 description 9
- CXURGFRDGROIKG-UHFFFAOYSA-N 3,3-bis(chloromethyl)oxetane Chemical compound ClCC1(CCl)COC1 CXURGFRDGROIKG-UHFFFAOYSA-N 0.000 description 8
- 230000008901 benefit Effects 0.000 description 8
- 238000005119 centrifugation Methods 0.000 description 8
- 239000012091 fetal bovine serum Substances 0.000 description 8
- 230000005017 genetic modification Effects 0.000 description 8
- 235000013617 genetically modified food Nutrition 0.000 description 8
- 238000007901 in situ hybridization Methods 0.000 description 8
- 230000010076 replication Effects 0.000 description 8
- 239000006228 supernatant Substances 0.000 description 8
- 230000003612 virological effect Effects 0.000 description 8
- 102000053602 DNA Human genes 0.000 description 7
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 7
- 101710173835 Penton protein Proteins 0.000 description 7
- 238000009835 boiling Methods 0.000 description 7
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 7
- 239000000463 material Substances 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 238000005215 recombination Methods 0.000 description 7
- 230000006798 recombination Effects 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 230000009885 systemic effect Effects 0.000 description 7
- 201000002743 tongue squamous cell carcinoma Diseases 0.000 description 7
- 208000010370 Adenoviridae Infections Diseases 0.000 description 6
- 206010060931 Adenovirus infection Diseases 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 108090000331 Firefly luciferases Proteins 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 239000007995 HEPES buffer Substances 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 6
- 108091034117 Oligonucleotide Proteins 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 6
- 208000011589 adenoviridae infectious disease Diseases 0.000 description 6
- 238000012512 characterization method Methods 0.000 description 6
- 238000012217 deletion Methods 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 210000005260 human cell Anatomy 0.000 description 6
- 238000009396 hybridization Methods 0.000 description 6
- 230000001976 improved effect Effects 0.000 description 6
- 239000013642 negative control Substances 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- 238000013518 transcription Methods 0.000 description 6
- 230000035897 transcription Effects 0.000 description 6
- 241000283707 Capra Species 0.000 description 5
- 102000000844 Cell Surface Receptors Human genes 0.000 description 5
- 108010001857 Cell Surface Receptors Proteins 0.000 description 5
- 238000012270 DNA recombination Methods 0.000 description 5
- 108700008625 Reporter Genes Proteins 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- 230000002950 deficient Effects 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 239000012530 fluid Substances 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 238000001114 immunoprecipitation Methods 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 239000012139 lysis buffer Substances 0.000 description 5
- 230000007246 mechanism Effects 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 230000009385 viral infection Effects 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- 108090000565 Capsid Proteins Proteins 0.000 description 4
- 102100023321 Ceruloplasmin Human genes 0.000 description 4
- 108091035707 Consensus sequence Proteins 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 4
- 108010067770 Endopeptidase K Proteins 0.000 description 4
- 241000598171 Human adenovirus sp. Species 0.000 description 4
- 108010047852 Integrin alphaVbeta3 Proteins 0.000 description 4
- 108700019961 Neoplasm Genes Proteins 0.000 description 4
- 102000048850 Neoplasm Genes Human genes 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 238000002105 Southern blotting Methods 0.000 description 4
- 208000036142 Viral infection Diseases 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000008827 biological function Effects 0.000 description 4
- 210000000170 cell membrane Anatomy 0.000 description 4
- 210000000349 chromosome Anatomy 0.000 description 4
- 238000013461 design Methods 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 230000002458 infectious effect Effects 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 239000000178 monomer Substances 0.000 description 4
- 210000002200 mouth mucosa Anatomy 0.000 description 4
- 230000009919 sequestration Effects 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 239000013605 shuttle vector Substances 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 238000005829 trimerization reaction Methods 0.000 description 4
- 239000013603 viral vector Substances 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- 101710132601 Capsid protein Proteins 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 3
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 3
- 238000012286 ELISA Assay Methods 0.000 description 3
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 108020005202 Viral DNA Proteins 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- -1 and therefore Substances 0.000 description 3
- 102000005936 beta-Galactosidase Human genes 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 210000004748 cultured cell Anatomy 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical group O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 230000006801 homologous recombination Effects 0.000 description 3
- 238000002744 homologous recombination Methods 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 238000000464 low-speed centrifugation Methods 0.000 description 3
- 201000005296 lung carcinoma Diseases 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 3
- 238000002731 protein assay Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 201000009410 rhabdomyosarcoma Diseases 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000001356 surgical procedure Methods 0.000 description 3
- 231100001274 therapeutic index Toxicity 0.000 description 3
- 230000009261 transgenic effect Effects 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 101710094648 Coat protein Proteins 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 108091006010 FLAG-tagged proteins Proteins 0.000 description 2
- 229920001917 Ficoll Polymers 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 102000004862 Gastrin releasing peptide Human genes 0.000 description 2
- 108090001053 Gastrin releasing peptide Proteins 0.000 description 2
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 2
- 101710094396 Hexon protein Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 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
- 108091092195 Intron Proteins 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 101710125418 Major capsid protein Proteins 0.000 description 2
- NTIZESTWPVYFNL-UHFFFAOYSA-N Methyl isobutyl ketone Chemical compound CC(C)CC(C)=O NTIZESTWPVYFNL-UHFFFAOYSA-N 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 238000000636 Northern blotting Methods 0.000 description 2
- 101710141454 Nucleoprotein Proteins 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 108010039918 Polylysine Proteins 0.000 description 2
- 101710083689 Probable capsid protein Proteins 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 239000007984 Tris EDTA buffer Substances 0.000 description 2
- 108010067390 Viral Proteins Proteins 0.000 description 2
- 108010084938 adenovirus receptor Proteins 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 239000012148 binding buffer Substances 0.000 description 2
- 239000007975 buffered saline Substances 0.000 description 2
- 235000011089 carbon dioxide Nutrition 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 2
- 235000021240 caseins Nutrition 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000013599 cloning vector Substances 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 239000005547 deoxyribonucleotide Substances 0.000 description 2
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 238000001952 enzyme assay Methods 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 108010074605 gamma-Globulins Proteins 0.000 description 2
- PUBCCFNQJQKCNC-XKNFJVFFSA-N gastrin-releasingpeptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)C(C)C)[C@@H](C)O)C(C)C)[C@@H](C)O)C(C)C)C1=CNC=N1 PUBCCFNQJQKCNC-XKNFJVFFSA-N 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 210000002216 heart Anatomy 0.000 description 2
- JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 210000003292 kidney cell Anatomy 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 239000007758 minimum essential medium Substances 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 239000004570 mortar (masonry) Substances 0.000 description 2
- 238000007899 nucleic acid hybridization Methods 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 229920000656 polylysine Polymers 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 238000011533 pre-incubation Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 2
- ILXAOQAXSHVHTM-UHFFFAOYSA-M sodium;2-amino-2-(hydroxymethyl)propane-1,3-diol;chloride Chemical compound [Na+].[Cl-].OCC(N)(CO)CO ILXAOQAXSHVHTM-UHFFFAOYSA-M 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 230000008093 supporting effect Effects 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 239000003656 tris buffered saline Substances 0.000 description 2
- 210000003462 vein Anatomy 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- BHNQPLPANNDEGL-UHFFFAOYSA-N 2-(4-octylphenoxy)ethanol Chemical compound CCCCCCCCC1=CC=C(OCCO)C=C1 BHNQPLPANNDEGL-UHFFFAOYSA-N 0.000 description 1
- HQFLTUZKIRYQSP-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole-6-sulfonic acid Chemical compound OS(=O)(=O)C1=CC=C2N(CC)CSC2=C1 HQFLTUZKIRYQSP-UHFFFAOYSA-N 0.000 description 1
- 101150072006 33 gene Proteins 0.000 description 1
- VOUAQYXWVJDEQY-QENPJCQMSA-N 33017-11-7 Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)CCC1 VOUAQYXWVJDEQY-QENPJCQMSA-N 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 102100022524 Alpha-1-antichymotrypsin Human genes 0.000 description 1
- 101001093708 Autographa californica nuclear polyhedrosis virus Per os infectivity factor 6 Proteins 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 241000120506 Bluetongue virus Species 0.000 description 1
- 241000283725 Bos Species 0.000 description 1
- 241000283730 Bos primigenius Species 0.000 description 1
- 238000009010 Bradford assay Methods 0.000 description 1
- 210000003771 C cell Anatomy 0.000 description 1
- 108010075254 C-Peptide Proteins 0.000 description 1
- 101710197658 Capsid protein VP1 Proteins 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 101710115643 Cathelicidin-1 Proteins 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 102100033779 Collagen alpha-4(IV) chain Human genes 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 1
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- 108010024212 E-Selectin Proteins 0.000 description 1
- 102100023471 E-selectin Human genes 0.000 description 1
- 241000702374 Enterobacteria phage fd Species 0.000 description 1
- 241000991587 Enterovirus C Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108091029865 Exogenous DNA Proteins 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 101100321670 Fagopyrum esculentum FA18 gene Proteins 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 102000053187 Glucuronidase Human genes 0.000 description 1
- 108010060309 Glucuronidase Proteins 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102100036738 Guanine nucleotide-binding protein subunit alpha-11 Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000678026 Homo sapiens Alpha-1-antichymotrypsin Proteins 0.000 description 1
- 101000710870 Homo sapiens Collagen alpha-4(IV) chain Proteins 0.000 description 1
- 101100283445 Homo sapiens GNA11 gene Proteins 0.000 description 1
- 101000603882 Homo sapiens Nuclear receptor subfamily 1 group I member 3 Proteins 0.000 description 1
- 101000879758 Homo sapiens Sjoegren syndrome nuclear autoantigen 1 Proteins 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 102100022337 Integrin alpha-V Human genes 0.000 description 1
- 108010040765 Integrin alphaV Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- 206010025538 Malignant ascites Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 101000858032 Mus musculus Coxsackievirus and adenovirus receptor homolog Proteins 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 244000061176 Nicotiana tabacum Species 0.000 description 1
- 239000012124 Opti-MEM Substances 0.000 description 1
- 102000004264 Osteopontin Human genes 0.000 description 1
- 108010081689 Osteopontin Proteins 0.000 description 1
- 208000007571 Ovarian Epithelial Carcinoma Diseases 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 229930040373 Paraformaldehyde Natural products 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 101710149951 Protein Tat Proteins 0.000 description 1
- 101710118046 RNA-directed RNA polymerase Proteins 0.000 description 1
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 102100037330 Sjoegren syndrome nuclear autoantigen 1 Human genes 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 241000256251 Spodoptera frugiperda Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 229910000831 Steel Inorganic materials 0.000 description 1
- 102000002938 Thrombospondin Human genes 0.000 description 1
- 108060008245 Thrombospondin Proteins 0.000 description 1
- GYDJEQRTZSCIOI-UHFFFAOYSA-N Tranexamic acid Chemical compound NCC1CCC(C(O)=O)CC1 GYDJEQRTZSCIOI-UHFFFAOYSA-N 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108010092464 Urate Oxidase Proteins 0.000 description 1
- 108700005077 Viral Genes Proteins 0.000 description 1
- 101710108545 Viral protein 1 Proteins 0.000 description 1
- 108010066342 Virus Receptors Proteins 0.000 description 1
- 108010031318 Vitronectin Proteins 0.000 description 1
- 102100035140 Vitronectin Human genes 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- JPIYZTWMUGTEHX-UHFFFAOYSA-N auramine O free base Chemical compound C1=CC(N(C)C)=CC=C1C(=N)C1=CC=C(N(C)C)C=C1 JPIYZTWMUGTEHX-UHFFFAOYSA-N 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 239000002981 blocking agent Substances 0.000 description 1
- 230000036770 blood supply Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- HFNQLYDPNAZRCH-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O.OC(O)=O HFNQLYDPNAZRCH-UHFFFAOYSA-N 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 108091092356 cellular DNA Proteins 0.000 description 1
- 208000019065 cervical carcinoma Diseases 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000011097 chromatography purification Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000007822 cytometric assay Methods 0.000 description 1
- 230000000120 cytopathologic effect Effects 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- 125000005442 diisocyanate group Chemical group 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 230000001819 effect on gene Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 230000008029 eradication Effects 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 102000054767 gene variant Human genes 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 208000014829 head and neck neoplasm Diseases 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 229940094991 herring sperm dna Drugs 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229960000890 hydrocortisone Drugs 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 229940027941 immunoglobulin g Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002540 isothiocyanates Chemical class 0.000 description 1
- 210000005229 liver cell Anatomy 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 230000007762 localization of cell Effects 0.000 description 1
- DLBFLQKQABVKGT-UHFFFAOYSA-L lucifer yellow dye Chemical compound [Li+].[Li+].[O-]S(=O)(=O)C1=CC(C(N(C(=O)NN)C2=O)=O)=C3C2=CC(S([O-])(=O)=O)=CC3=C1N DLBFLQKQABVKGT-UHFFFAOYSA-L 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000011278 mitosis Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000037230 mobility Effects 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 201000006938 muscular dystrophy Diseases 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- JPXMTWWFLBLUCD-UHFFFAOYSA-N nitro blue tetrazolium(2+) Chemical compound COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 JPXMTWWFLBLUCD-UHFFFAOYSA-N 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 229920002866 paraformaldehyde Polymers 0.000 description 1
- 208000017058 pharyngeal squamous cell carcinoma Diseases 0.000 description 1
- 108010055837 phosphocarrier protein HPr Proteins 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 230000007505 plaque formation Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 108091006091 regulatory enzymes Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 230000037432 silent mutation Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229940054269 sodium pyruvate Drugs 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
- 229960000553 somatostatin Drugs 0.000 description 1
- 210000002325 somatostatin-secreting cell Anatomy 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 239000010959 steel Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000011191 terminal modification Methods 0.000 description 1
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 1
- 230000005100 tissue tropism Effects 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000017105 transposition Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 210000003954 umbilical cord Anatomy 0.000 description 1
- 210000003606 umbilical vein Anatomy 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 230000017613 viral reproduction Effects 0.000 description 1
- 230000010464 virion assembly Effects 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 102100036537 von Willebrand factor Human genes 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- 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
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/10011—Adenoviridae
- C12N2710/10311—Mastadenovirus, e.g. human or simian adenoviruses
- C12N2710/10322—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/14011—Baculoviridae
- C12N2710/14111—Nucleopolyhedrovirus, e.g. autographa californica nucleopolyhedrovirus
- C12N2710/14141—Use of virus, viral particle or viral elements as a vector
- C12N2710/14143—Use of virus, viral particle or viral elements as a vector viral genome or elements thereof as genetic vector
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Pharmacology & Pharmacy (AREA)
- Molecular Biology (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Virology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Biotechnology (AREA)
- Epidemiology (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US7394798P | 1998-02-06 | 1998-02-06 | |
| US60/073,947 | 1998-02-06 | ||
| US9980198P | 1998-09-10 | 1998-09-10 | |
| US60/099,801 | 1998-09-10 | ||
| PCT/US1999/002549 WO1999039734A1 (en) | 1998-02-06 | 1999-02-05 | Adenovirus vector containing a heterologous peptide epitope in the hi loop of the fiber knob |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2002507391A true JP2002507391A (ja) | 2002-03-12 |
| JP2002507391A5 JP2002507391A5 (https=) | 2006-03-30 |
Family
ID=26755086
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000530231A Pending JP2002507391A (ja) | 1998-02-06 | 1999-02-05 | 繊維ノブのｈｉループに異種ペプチドエピトープを含有するアデノウイルスベクター |
Country Status (11)
| Country | Link |
|---|---|
| US (1) | US7297542B2 (https=) |
| EP (1) | EP1053013A4 (https=) |
| JP (1) | JP2002507391A (https=) |
| KR (1) | KR20010034487A (https=) |
| CN (1) | CN1304316A (https=) |
| AU (1) | AU744252B2 (https=) |
| BR (1) | BR9908613A (https=) |
| CA (1) | CA2327545A1 (https=) |
| IL (1) | IL137681A0 (https=) |
| NO (1) | NO20003956L (https=) |
| WO (1) | WO1999039734A1 (https=) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2006514538A (ja) * | 2002-07-10 | 2006-05-11 | トランスジーン ソシエテ アノニム | 細胞受容体への結合が除去された改変アデノウイルス繊維 |
| JP2015511822A (ja) * | 2012-03-13 | 2015-04-23 | ソーク インスティテュート フォー バイオロジカル スタディーズ | アデノウイルスおよび化学二量体を用いる選択細胞の標的化 |
Families Citing this family (46)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6395875B1 (en) * | 1999-01-25 | 2002-05-28 | Brookhaven Science Associates Llc | Recombinant soluble adenovirus receptor |
| US7157266B2 (en) * | 1999-01-25 | 2007-01-02 | Brookhaven Science Associates Llc | Structure of adenovirus bound to cellular receptor car |
| US7560527B1 (en) | 1999-11-25 | 2009-07-14 | Transgene S.A. | Modified adenovirus fibre and uses |
| CN1230441C (zh) | 2000-04-12 | 2005-12-07 | 安盛药业有限公司 | 结合整联蛋白的肽衍生物 |
| JP3635462B2 (ja) | 2000-05-31 | 2005-04-06 | 国立医薬品食品衛生研究所長 | アデノウイルスベクター |
| JP2003534805A (ja) | 2000-05-31 | 2003-11-25 | ユニバーシティ オブ サスカチュワン | 変化した親和性を有する改変ウシアデノウイルス |
| NO20004795D0 (no) | 2000-09-26 | 2000-09-26 | Nycomed Imaging As | Peptidbaserte forbindelser |
| WO2003006491A2 (en) | 2001-07-10 | 2003-01-23 | Amersham Health As | Peptide-based compounds for targeting intergin receptors |
| EP1446479B1 (en) | 2001-09-29 | 2012-08-15 | Chae-Ok Yun | Recombinant adenovirus with enhanced therapeutic effect and pharmaceutical composition comprising said recombinant adenovirus |
| US20060281090A1 (en) * | 2003-05-01 | 2006-12-14 | University Of Washington Uw Tech Transfer- Invention Licensing | Capsid-modified adenovirus vectors and methods of using the same |
| US7611868B2 (en) | 2003-05-14 | 2009-11-03 | Instituto Di Ricerche Di Biologia Molecolare P. Angeletti S.P.A. | Recombinant modified adenovirus fiber protein |
| US20070104732A1 (en) * | 2003-10-24 | 2007-05-10 | Bernard Massie | Ligand-pseudoreceptor system for generation of adenoviral vectors with altered tropism |
| CA2552262C (en) | 2004-02-02 | 2016-04-19 | The University Of British Columbia | Scodaphoresis and methods and apparatus for moving and concentrating particles |
| US8529744B2 (en) | 2004-02-02 | 2013-09-10 | Boreal Genomics Corp. | Enrichment of nucleic acid targets |
| US10337054B2 (en) | 2004-02-02 | 2019-07-02 | Quantum-Si Incorporated | Enrichment of nucleic acid targets |
| US7473418B2 (en) | 2004-03-25 | 2009-01-06 | Cell Genesys, Inc. | Pan cancer oncolytic vectors and methods of use thereof |
| DE102004021584A1 (de) * | 2004-05-03 | 2005-12-01 | Stefan Kochanek | Modifizierte virale Vektorpartikel |
| US7776322B2 (en) | 2004-08-16 | 2010-08-17 | Stefan Kochanek | Modified viral vector particles |
| CA2496294A1 (en) * | 2005-02-07 | 2006-08-07 | The University Of British Columbia | Apparatus and methods for concentrating and separating particles such as molecules |
| JP6092497B2 (ja) | 2006-03-30 | 2017-03-08 | ユニバーシティー オブ カリフォルニア | 抗ｃｔｌａ−４抗体の限局性分泌のための方法および組成物 |
| US7919079B2 (en) | 2006-03-31 | 2011-04-05 | Biosante Pharmaceuticals, Inc. | Cancer immunotherapy compositions and methods of use |
| WO2008140474A1 (en) * | 2006-10-26 | 2008-11-20 | Johns Hopkins University | Recombinant adenovirus vaccines |
| EP2238434A4 (en) | 2008-02-01 | 2011-06-22 | Univ British Columbia | METHOD AND DEVICE FOR PARTICLE INTRODUCTION AND RECOVERY |
| WO2009137211A2 (en) * | 2008-05-04 | 2009-11-12 | University Of Maryland Biotechnology Institute Off. Of Research Admin./ Tech. Dev. | Fibrous assemblies for antibody presentation, and multiplexed antigenic analysis using same |
| US20110256055A1 (en) | 2008-12-23 | 2011-10-20 | Ge Healthcare Limited | Application of 99mtc peptide-based compound as a bone marrow imaging agent |
| US8877028B2 (en) | 2009-04-21 | 2014-11-04 | The University Of British Columbia | System and methods for detection of particles |
| ES2385251B1 (es) | 2009-05-06 | 2013-05-06 | Fundació Privada Institut D'investigació Biomèdica De Bellvitge | Adenovirus oncolíticos para el tratamiento del cáncer. |
| US9458473B2 (en) * | 2010-06-29 | 2016-10-04 | The Johns Hopkins University | Compositions and methods for retargeting virus constructs |
| CA2742327A1 (en) | 2011-05-20 | 2012-11-20 | The University Of British Columiba | Systems and methods for enhanced scoda |
| WO2013090806A2 (en) * | 2011-12-15 | 2013-06-20 | Washington University | Porcine knob xenotype chimeric adenoviral vector for dendritic cell infection |
| WO2013104994A2 (en) | 2012-01-13 | 2013-07-18 | The University Of British Columbia | Multiple arm apparatus and methods for separation of particles |
| WO2013166444A2 (en) | 2012-05-04 | 2013-11-07 | Boreal Genomics Corp. | Biomarker analysis using scodaphoresis |
| AU2014236207B2 (en) | 2013-03-14 | 2019-05-23 | Salk Institute For Biological Studies | Oncolytic adenovirus compositions |
| US9340835B2 (en) | 2013-03-15 | 2016-05-17 | Boreal Genomics Corp. | Method for separating homoduplexed and heteroduplexed nucleic acids |
| CN104634978A (zh) * | 2013-11-13 | 2015-05-20 | 长春百克生物科技股份公司 | 一种分型检测腺病毒中和抗体的方法以及用于分型检测腺病毒中和抗体的试剂盒 |
| WO2016025469A1 (en) * | 2014-08-11 | 2016-02-18 | The Board Of Regents Of The University Of Texas System | Prevention of muscular dystrophy by crispr/cas9-mediated gene editing |
| KR20250081944A (ko) | 2014-09-24 | 2025-06-05 | 솔크 인스티튜트 포 바이올로지칼 스터디즈 | 종양 살상 바이러스 및 이의 사용방법 |
| US11130986B2 (en) | 2015-05-20 | 2021-09-28 | Quantum-Si Incorporated | Method for isolating target nucleic acid using heteroduplex binding proteins |
| EP4155411A1 (en) | 2016-02-23 | 2023-03-29 | Salk Institute for Biological Studies | Exogenous gene expression in therapeutic adenovirus for minimal impact on viral kinetics |
| WO2017147265A1 (en) | 2016-02-23 | 2017-08-31 | Salk Institute For Biological Studies | High throughput assay for measuring adenovirus replication kinetics |
| EP3532082A4 (en) | 2016-12-12 | 2020-08-26 | Salk Institute for Biological Studies | SYNTHETIC ADENOVIRUS TUMOR TARGETING AND THEIR USES |
| EP3565578A1 (en) | 2016-12-21 | 2019-11-13 | Memgen LLC | Armed replication-competent oncolytic adenoviruses |
| MX2020000244A (es) | 2017-06-27 | 2020-09-28 | Regeneron Pharma | Vectores virales recombinantes con tropismo modificado y usos de estos para la introduccion dirigida de material genetico a celulas humanas. |
| MX2020010499A (es) | 2018-04-09 | 2020-10-28 | Salk Inst For Biological Studi | Composiciones de adenovirus oncoliticas con propiedades aumentadas de replicacion. |
| EP3927833A4 (en) | 2019-02-21 | 2022-11-30 | Unleash Immuno Oncolytics, Inc. | ONCOLYTIC ADENOVIRAL VECTOR AND METHODS OF USE |
| AU2020372908A1 (en) | 2019-10-29 | 2022-06-02 | Quantum-Si Incorporated | Peristaltic pumping of fluids and associated methods, systems, and devices |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9223084D0 (en) * | 1992-11-04 | 1992-12-16 | Imp Cancer Res Tech | Compounds to target cells |
| US5846782A (en) | 1995-11-28 | 1998-12-08 | Genvec, Inc. | Targeting adenovirus with use of constrained peptide motifs |
| US5770442A (en) * | 1995-02-21 | 1998-06-23 | Cornell Research Foundation, Inc. | Chimeric adenoviral fiber protein and methods of using same |
| EP0866721A4 (en) * | 1995-12-08 | 2003-06-04 | Univ Alabama Birmingham Res Fo | TARGET ADENOVIRAL VECTORS |
| AU767904B2 (en) * | 1999-05-12 | 2003-11-27 | Uab Research Foundation, The | Infectivity-enhanced conditionally-replicative adenovirus and uses thereof |
-
1999
- 1999-02-05 IL IL13768199A patent/IL137681A0/xx unknown
- 1999-02-05 EP EP99906761A patent/EP1053013A4/en not_active Withdrawn
- 1999-02-05 CN CN99804659A patent/CN1304316A/zh active Pending
- 1999-02-05 KR KR1020007008593A patent/KR20010034487A/ko not_active Withdrawn
- 1999-02-05 WO PCT/US1999/002549 patent/WO1999039734A1/en not_active Ceased
- 1999-02-05 US US09/245,603 patent/US7297542B2/en not_active Expired - Fee Related
- 1999-02-05 JP JP2000530231A patent/JP2002507391A/ja active Pending
- 1999-02-05 AU AU26595/99A patent/AU744252B2/en not_active Ceased
- 1999-02-05 BR BR9908613-1A patent/BR9908613A/pt not_active IP Right Cessation
- 1999-02-05 CA CA002327545A patent/CA2327545A1/en not_active Abandoned
-
2000
- 2000-08-04 NO NO20003956A patent/NO20003956L/no not_active Application Discontinuation
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2006514538A (ja) * | 2002-07-10 | 2006-05-11 | トランスジーン ソシエテ アノニム | 細胞受容体への結合が除去された改変アデノウイルス繊維 |
| JP2015511822A (ja) * | 2012-03-13 | 2015-04-23 | ソーク インスティテュート フォー バイオロジカル スタディーズ | アデノウイルスおよび化学二量体を用いる選択細胞の標的化 |
Also Published As
| Publication number | Publication date |
|---|---|
| CN1304316A (zh) | 2001-07-18 |
| IL137681A0 (en) | 2001-10-31 |
| KR20010034487A (ko) | 2001-04-25 |
| US7297542B2 (en) | 2007-11-20 |
| NO20003956L (no) | 2000-10-05 |
| AU744252B2 (en) | 2002-02-21 |
| EP1053013A1 (en) | 2000-11-22 |
| NO20003956D0 (no) | 2000-08-04 |
| AU2659599A (en) | 1999-08-23 |
| BR9908613A (pt) | 2000-10-31 |
| WO1999039734A1 (en) | 1999-08-12 |
| EP1053013A4 (en) | 2004-12-22 |
| CA2327545A1 (en) | 1999-08-12 |
| US20020081280A1 (en) | 2002-06-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2002507391A (ja) | 繊維ノブのｈｉループに異種ペプチドエピトープを含有するアデノウイルスベクター | |
| JP2002507391A5 (https=) | ||
| AU684220B2 (en) | Recombinant adenovirus comprising a chimeric penton base protein | |
| Wickham et al. | Increased in vitro and in vivo gene transfer by adenovirus vectors containing chimeric fiber proteins | |
| AU698254B2 (en) | Chimeric adenoviral fiber protein and methods of using same | |
| EP1181382B1 (en) | Recombinant adenoviral vectors expressing chimeric fiber proteins for cell specific infection and genome integration | |
| WO1994017832A1 (en) | Targeting and delivery of genes and antiviral agents into cells by the adenovirus penton | |
| JP2002523105A (ja) | 異種遺伝子の運搬用の標的化アデノウイルスベクター | |
| JPH11501219A (ja) | 細胞への遣伝子導入のためのベクターおよび方法 | |
| EP1002119A1 (en) | Targeted hsv vectors | |
| JP2003514526A (ja) | 永久羊膜細胞株、その生成、および遺伝子移入ベクターの生成のための使用 | |
| JP2003531609A (ja) | 目に関する形質導入用ベクターおよび遺伝子治療を目的とするその用途 | |
| JP2001503250A (ja) | 束縛ペプチドモチーフを用いたターゲッティングアデノウイルス | |
| Sharma et al. | Comparative analysis of vector biodistribution, persistence and gene expression following intravenous delivery of bovine, porcine and human adenoviral vectors in a mouse model | |
| CA2317941A1 (en) | Adenoviral vectors with modified capsid proteins | |
| JP2003534805A (ja) | 変化した親和性を有する改変ウシアデノウイルス | |
| JP2007503843A (ja) | アデノウイルス親和性の拡大 | |
| EP1593742A2 (en) | Recombinant adenoviral vectors expressing chimeric fiber proteins for cell specific infection | |
| US6815200B1 (en) | Modified adenovirus containing a fiber replacement protein | |
| MXPA00007721A (en) | Adenovirus vector containing a heterologous peptide epitope in the hi loop of the fiber knob | |
| NZ505950A (en) | Adenovirus vector containing a heterologous peptide epitope in the hi loop of the fiber knob | |
| Denby et al. | 127. Adenovirus type 5 vectors pseudotyped with fibers from subgroup D (19p and 37) show detargeting from hepatocytes in vitro and in vivo | |
| Roy et al. | 128. Use of chimeric adenoviral vectors to assess capsid neutralization determinants | |
| MXPA98004203A (en) | Vectors and methods for gene transfer acelu |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20060206 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20060206 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20081104 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20090421 |