CA2616698C - Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie - Google Patents

Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie Download PDF

Info

Publication number: CA2616698C
Authority: CA; Canada
Prior art keywords: dna; virus; gene; plasmid; site
Prior art date: 1991-08-26
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 - Fee Related

Application number

CA002616698A

Other languages

English (en)

Other versions

CA2616698A1 (fr

Inventor

Friedrich Dorner

Friedrich Scheiflinger

Falko Gunter Falkner

Michael Pfleiderer

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Baxter Healthcare SA

Original Assignee

Baxter Healthcare SA

Priority date (The priority date 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 date listed.)

1991-08-26

Filing date

1992-08-25

Publication date

2009-03-17

1991-08-26 Priority claimed from US07/750,080 external-priority patent/US5445953A/en

1992-08-25 Application filed by Baxter Healthcare SA filed Critical Baxter Healthcare SA

1992-08-25 Priority claimed from CA002558864A external-priority patent/CA2558864C/fr

1993-02-27 Publication of CA2616698A1 publication Critical patent/CA2616698A1/fr

2009-03-17 Application granted granted Critical

2009-03-17 Publication of CA2616698C publication Critical patent/CA2616698C/fr

2012-08-25 Anticipated expiration legal-status Critical

Status Expired - Fee Related legal-status Critical Current

Links

238000010369 molecular cloning Methods 0.000 title claims description 39
241000700605 Viruses Species 0.000 title description 385
230000001086 cytosolic effect Effects 0.000 title description 67
239000013612 plasmid Substances 0.000 claims abstract description 320
241000700618 Vaccinia virus Species 0.000 claims abstract description 263
239000013598 vector Substances 0.000 claims abstract description 147
238000010367 cloning Methods 0.000 claims abstract description 146
108091028043 Nucleic acid sequence Proteins 0.000 claims description 84
108091081024 Start codon Proteins 0.000 claims description 63
238000013519 translation Methods 0.000 claims description 16
101000651439 Homo sapiens Prothrombin Proteins 0.000 claims description 11
229940039715 human prothrombin Drugs 0.000 claims description 9
108020004414 DNA Proteins 0.000 description 458
210000004027 cell Anatomy 0.000 description 231
239000012634 fragment Substances 0.000 description 197
108090000623 proteins and genes Proteins 0.000 description 194
230000003612 virological effect Effects 0.000 description 167
238000003776 cleavage reaction Methods 0.000 description 119
230000007017 scission Effects 0.000 description 119
238000000034 method Methods 0.000 description 113
238000003780 insertion Methods 0.000 description 111
230000037431 insertion Effects 0.000 description 111
230000014509 gene expression Effects 0.000 description 108
101150106093 gpt gene Proteins 0.000 description 102
239000003550 marker Substances 0.000 description 89
206010046865 Vaccinia virus infection Diseases 0.000 description 87
208000007089 vaccinia Diseases 0.000 description 87
238000010276 construction Methods 0.000 description 86
241000700662 Fowlpox virus Species 0.000 description 85
238000004806 packaging method and process Methods 0.000 description 72
102000053602 DNA Human genes 0.000 description 58
108020005202 Viral DNA Proteins 0.000 description 48
108700026244 Open Reading Frames Proteins 0.000 description 45
108091034117 Oligonucleotide Proteins 0.000 description 44
239000002299 complementary DNA Substances 0.000 description 41
241000588724 Escherichia coli Species 0.000 description 39
239000000523 sample Substances 0.000 description 39
208000015181 infectious disease Diseases 0.000 description 38
101150003725 TK gene Proteins 0.000 description 35
108010042407 Endonucleases Proteins 0.000 description 34
102000004533 Endonucleases Human genes 0.000 description 34
238000002474 experimental method Methods 0.000 description 33
238000013518 transcription Methods 0.000 description 32
230000035897 transcription Effects 0.000 description 32
238000002105 Southern blotting Methods 0.000 description 31
108010051456 Plasminogen Proteins 0.000 description 30
208000000666 Fowlpox Diseases 0.000 description 29
108091008146 restriction endonucleases Proteins 0.000 description 29
102000013566 Plasminogen Human genes 0.000 description 28
230000006798 recombination Effects 0.000 description 28
238000005215 recombination Methods 0.000 description 28
210000002845 virion Anatomy 0.000 description 28
102100022641 Coagulation factor IX Human genes 0.000 description 27
108020004705 Codon Proteins 0.000 description 27
108010076282 Factor IX Proteins 0.000 description 27
241000287828 Gallus gallus Species 0.000 description 27
238000012216 screening Methods 0.000 description 27
238000012217 deletion Methods 0.000 description 26
229960004222 factor ix Drugs 0.000 description 26
229940096437 Protein S Drugs 0.000 description 25
108010066124 Protein S Proteins 0.000 description 25
101150066555 lacZ gene Proteins 0.000 description 25
210000001161 mammalian embryo Anatomy 0.000 description 25
238000003752 polymerase chain reaction Methods 0.000 description 25
230000037430 deletion Effects 0.000 description 24
210000002950 fibroblast Anatomy 0.000 description 24
230000004048 modification Effects 0.000 description 22
238000012986 modification Methods 0.000 description 22
238000004113 cell culture Methods 0.000 description 21
230000002458 infectious effect Effects 0.000 description 21
102000029301 Protein S Human genes 0.000 description 20
238000004458 analytical method Methods 0.000 description 20
238000013459 approach Methods 0.000 description 20
230000003834 intracellular effect Effects 0.000 description 20
230000010076 replication Effects 0.000 description 20
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 19
102000004169 proteins and genes Human genes 0.000 description 18
108091026890 Coding region Proteins 0.000 description 17
102000004190 Enzymes Human genes 0.000 description 17
108090000790 Enzymes Proteins 0.000 description 17
241000725303 Human immunodeficiency virus Species 0.000 description 17
238000006243 chemical reaction Methods 0.000 description 17
235000018102 proteins Nutrition 0.000 description 17
210000004962 mammalian cell Anatomy 0.000 description 16
238000012546 transfer Methods 0.000 description 16
238000009396 hybridization Methods 0.000 description 15
101710163270 Nuclease Proteins 0.000 description 13
108020004440 Thymidine kinase Proteins 0.000 description 13
239000011543 agarose gel Substances 0.000 description 13
230000002441 reversible effect Effects 0.000 description 13
235000001014 amino acid Nutrition 0.000 description 12
150000001413 amino acids Chemical class 0.000 description 12
238000003556 assay Methods 0.000 description 12
238000011534 incubation Methods 0.000 description 12
239000000463 material Substances 0.000 description 12
108010047303 von Willebrand Factor Proteins 0.000 description 12
102100036537 von Willebrand factor Human genes 0.000 description 12
229960001134 von willebrand factor Drugs 0.000 description 12
108020005065 3' Flanking Region Proteins 0.000 description 11
108020005029 5' Flanking Region Proteins 0.000 description 11
239000000543 intermediate Substances 0.000 description 11
238000002703 mutagenesis Methods 0.000 description 11
231100000350 mutagenesis Toxicity 0.000 description 11
HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 11
108090000765 processed proteins & peptides Proteins 0.000 description 11
238000000746 purification Methods 0.000 description 11
241000700629 Orthopoxvirus Species 0.000 description 10
108010094028 Prothrombin Proteins 0.000 description 10
102100027378 Prothrombin Human genes 0.000 description 10
102000006601 Thymidine Kinase Human genes 0.000 description 10
230000003321 amplification Effects 0.000 description 10
230000001580 bacterial effect Effects 0.000 description 10
238000001727 in vivo Methods 0.000 description 10
HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 10
230000035772 mutation Effects 0.000 description 10
229960000951 mycophenolic acid Drugs 0.000 description 10
238000003199 nucleic acid amplification method Methods 0.000 description 10
229940039716 prothrombin Drugs 0.000 description 10
238000001890 transfection Methods 0.000 description 10
238000011144 upstream manufacturing Methods 0.000 description 10
238000001262 western blot Methods 0.000 description 10
241000700663 Avipoxvirus Species 0.000 description 9
241000450599 DNA viruses Species 0.000 description 9
101000577630 Homo sapiens Vitamin K-dependent protein S Proteins 0.000 description 9
230000008901 benefit Effects 0.000 description 9
230000000295 complement effect Effects 0.000 description 9
239000012228 culture supernatant Substances 0.000 description 9
230000000694 effects Effects 0.000 description 9
230000012010 growth Effects 0.000 description 9
108010087750 lysyl-plasminogen Proteins 0.000 description 9
238000004519 manufacturing process Methods 0.000 description 9
229920001184 polypeptide Polymers 0.000 description 9
102000004196 processed proteins & peptides Human genes 0.000 description 9
210000003501 vero cell Anatomy 0.000 description 9
241000702208 Shigella phage SfX Species 0.000 description 8
239000000499 gel Substances 0.000 description 8
102000052932 human PROS1 Human genes 0.000 description 8
210000005260 human cell Anatomy 0.000 description 8
229940099815 human protein s Drugs 0.000 description 8
239000002609 medium Substances 0.000 description 8
238000010561 standard procedure Methods 0.000 description 8
101000605403 Homo sapiens Plasminogen Proteins 0.000 description 7
108091029795 Intergenic region Proteins 0.000 description 7
102000003960 Ligases Human genes 0.000 description 7
108090000364 Ligases Proteins 0.000 description 7
108010076504 Protein Sorting Signals Proteins 0.000 description 7
229960001714 calcium phosphate Drugs 0.000 description 7
239000001506 calcium phosphate Substances 0.000 description 7
229910000389 calcium phosphate Inorganic materials 0.000 description 7
235000011010 calcium phosphates Nutrition 0.000 description 7
230000029087 digestion Effects 0.000 description 7
238000010790 dilution Methods 0.000 description 7
239000012895 dilution Substances 0.000 description 7
229960000027 human factor ix Drugs 0.000 description 7
238000002955 isolation Methods 0.000 description 7
238000005304 joining Methods 0.000 description 7
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 7
229960005486 vaccine Drugs 0.000 description 7
241000271566 Aves Species 0.000 description 6
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
239000000427 antigen Substances 0.000 description 6
108091007433 antigens Proteins 0.000 description 6
102000036639 antigens Human genes 0.000 description 6
230000001276 controlling effect Effects 0.000 description 6
238000005520 cutting process Methods 0.000 description 6
238000010353 genetic engineering Methods 0.000 description 6
238000002844 melting Methods 0.000 description 6
230000008018 melting Effects 0.000 description 6
239000002244 precipitate Substances 0.000 description 6
239000000047 product Substances 0.000 description 6
230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 6
230000003362 replicative effect Effects 0.000 description 6
WYWHKKSPHMUBEB-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 description 6
102000004163 DNA-directed RNA polymerases Human genes 0.000 description 5
108090000626 DNA-directed RNA polymerases Proteins 0.000 description 5
102000003886 Glycoproteins Human genes 0.000 description 5
108090000288 Glycoproteins Proteins 0.000 description 5
108091026898 Leader sequence (mRNA) Proteins 0.000 description 5
108020004511 Recombinant DNA Proteins 0.000 description 5
IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical class O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 5
238000001514 detection method Methods 0.000 description 5
229940079593 drug Drugs 0.000 description 5
239000003814 drug Substances 0.000 description 5
108700004025 env Genes Proteins 0.000 description 5
101150030339 env gene Proteins 0.000 description 5
239000013604 expression vector Substances 0.000 description 5
230000010354 integration Effects 0.000 description 5
239000006228 supernatant Substances 0.000 description 5
230000029812 viral genome replication Effects 0.000 description 5
QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 4
LRFVTYWOQMYALW-UHFFFAOYSA-N 9H-xanthine Chemical compound O=C1NC(=O)NC2=C1NC=N2 LRFVTYWOQMYALW-UHFFFAOYSA-N 0.000 description 4
102000002260 Alkaline Phosphatase Human genes 0.000 description 4
108020004774 Alkaline Phosphatase Proteins 0.000 description 4
108091003079 Bovine Serum Albumin Proteins 0.000 description 4
241000282552 Chlorocebus aethiops Species 0.000 description 4
108020003215 DNA Probes Proteins 0.000 description 4
239000003298 DNA probe Substances 0.000 description 4
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 4
102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 4
241000701832 Enterobacteria phage T3 Species 0.000 description 4
208000034454 F12-related hereditary angioedema with normal C1Inh Diseases 0.000 description 4
241000713772 Human immunodeficiency virus 1 Species 0.000 description 4
241000701372 Iridovirus Species 0.000 description 4
239000000020 Nitrocellulose Substances 0.000 description 4
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
108020004682 Single-Stranded DNA Proteins 0.000 description 4
229930006000 Sucrose Natural products 0.000 description 4
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 4
230000001413 cellular effect Effects 0.000 description 4
239000003153 chemical reaction reagent Substances 0.000 description 4
238000007796 conventional method Methods 0.000 description 4
238000000605 extraction Methods 0.000 description 4
239000012894 fetal calf serum Substances 0.000 description 4
230000002068 genetic effect Effects 0.000 description 4
208000016861 hereditary angioedema type 3 Diseases 0.000 description 4
239000012528 membrane Substances 0.000 description 4
239000000203 mixture Substances 0.000 description 4
229920001220 nitrocellulos Polymers 0.000 description 4
239000002773 nucleotide Substances 0.000 description 4
125000003729 nucleotide group Chemical group 0.000 description 4
239000002243 precursor Substances 0.000 description 4
210000002966 serum Anatomy 0.000 description 4
238000002741 site-directed mutagenesis Methods 0.000 description 4
238000006467 substitution reaction Methods 0.000 description 4
239000000758 substrate Substances 0.000 description 4
239000005720 sucrose Substances 0.000 description 4
238000012360 testing method Methods 0.000 description 4
230000014621 translational initiation Effects 0.000 description 4
241001430294 unidentified retrovirus Species 0.000 description 4
WOVKYSAHUYNSMH-RRKCRQDMSA-N 5-bromodeoxyuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-RRKCRQDMSA-N 0.000 description 3
208000030507 AIDS Diseases 0.000 description 3
108010039209 Blood Coagulation Factors Proteins 0.000 description 3
102000015081 Blood Coagulation Factors Human genes 0.000 description 3
108091028026 C-DNA Proteins 0.000 description 3
241000282693 Cercopithecidae Species 0.000 description 3
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
108010042546 GCGGCCGC-specific type II deoxyribonucleases Proteins 0.000 description 3
241000238631 Hexapoda Species 0.000 description 3
102100036860 Troponin T, slow skeletal muscle Human genes 0.000 description 3
241000251539 Vertebrata <Metazoa> Species 0.000 description 3
229930003448 Vitamin K Natural products 0.000 description 3
239000003242 anti bacterial agent Substances 0.000 description 3
229940088710 antibiotic agent Drugs 0.000 description 3
239000003114 blood coagulation factor Substances 0.000 description 3
239000000872 buffer Substances 0.000 description 3
230000002950 deficient Effects 0.000 description 3
238000001962 electrophoresis Methods 0.000 description 3
238000012869 ethanol precipitation Methods 0.000 description 3
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 3
229960005542 ethidium bromide Drugs 0.000 description 3
238000001502 gel electrophoresis Methods 0.000 description 3
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
238000000338 in vitro Methods 0.000 description 3
238000013383 initial experiment Methods 0.000 description 3
210000004185 liver Anatomy 0.000 description 3
239000013642 negative control Substances 0.000 description 3
SHUZOJHMOBOZST-UHFFFAOYSA-N phylloquinone Natural products CC(C)CCCCC(C)CCC(C)CCCC(=CCC1=C(C)C(=O)c2ccccc2C1=O)C SHUZOJHMOBOZST-UHFFFAOYSA-N 0.000 description 3
230000004481 post-translational protein modification Effects 0.000 description 3
238000001556 precipitation Methods 0.000 description 3
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
230000007420 reactivation Effects 0.000 description 3
238000011084 recovery Methods 0.000 description 3
230000002829 reductive effect Effects 0.000 description 3
230000001105 regulatory effect Effects 0.000 description 3
238000011160 research Methods 0.000 description 3
230000028327 secretion Effects 0.000 description 3
238000000926 separation method Methods 0.000 description 3
241000894007 species Species 0.000 description 3
238000010186 staining Methods 0.000 description 3
229960003087 tioguanine Drugs 0.000 description 3
230000035899 viability Effects 0.000 description 3
239000013603 viral vector Substances 0.000 description 3
235000019168 vitamin K Nutrition 0.000 description 3
239000011712 vitamin K Substances 0.000 description 3
150000003721 vitamin K derivatives Chemical class 0.000 description 3
229940046010 vitamin k Drugs 0.000 description 3
SNBCLPGEMZEWLU-QXFUBDJGSA-N 2-chloro-n-[[(2r,3s,5r)-3-hydroxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methyl]acetamide Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CNC(=O)CCl)[C@@H](O)C1 SNBCLPGEMZEWLU-QXFUBDJGSA-N 0.000 description 2
OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 2
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
101800001401 Activation peptide Proteins 0.000 description 2
102400000069 Activation peptide Human genes 0.000 description 2
229920000936 Agarose Polymers 0.000 description 2
WOVKYSAHUYNSMH-UHFFFAOYSA-N BROMODEOXYURIDINE Natural products C1C(O)C(CO)OC1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-UHFFFAOYSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
108010077805 Bacterial Proteins Proteins 0.000 description 2
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 2
102000004506 Blood Proteins Human genes 0.000 description 2
108010017384 Blood Proteins Proteins 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
206010053567 Coagulopathies Diseases 0.000 description 2
108020004635 Complementary DNA Proteins 0.000 description 2
102000012410 DNA Ligases Human genes 0.000 description 2
108010061982 DNA Ligases Proteins 0.000 description 2
230000003682 DNA packaging effect Effects 0.000 description 2
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 2
238000002965 ELISA Methods 0.000 description 2
241000710188 Encephalomyocarditis virus Species 0.000 description 2
101710121417 Envelope glycoprotein Proteins 0.000 description 2
101710091045 Envelope protein Proteins 0.000 description 2
241001524679 Escherichia virus M13 Species 0.000 description 2
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
101000636168 Grapevine leafroll-associated virus 3 (isolate United States/NY1) Movement protein p5 Proteins 0.000 description 2
101000782195 Homo sapiens von Willebrand factor Proteins 0.000 description 2
108090000144 Human Proteins Proteins 0.000 description 2
102000003839 Human Proteins Human genes 0.000 description 2
241000124008 Mammalia Species 0.000 description 2
102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 2
108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 2
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
101710188315 Protein X Proteins 0.000 description 2
240000004808 Saccharomyces cerevisiae Species 0.000 description 2
108091027544 Subgenomic mRNA Proteins 0.000 description 2
206010042566 Superinfection Diseases 0.000 description 2
101900209501 Vaccinia virus Thymidine kinase Proteins 0.000 description 2
241000700646 Vaccinia virus WR Species 0.000 description 2
108010027570 Xanthine phosphoribosyltransferase Proteins 0.000 description 2
230000002238 attenuated effect Effects 0.000 description 2
IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
229960000182 blood factors Drugs 0.000 description 2
229950004398 broxuridine Drugs 0.000 description 2
244000309466 calf Species 0.000 description 2
230000010261 cell growth Effects 0.000 description 2
108091092356 cellular DNA Proteins 0.000 description 2
230000008859 change Effects 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
230000035602 clotting Effects 0.000 description 2
230000000120 cytopathologic effect Effects 0.000 description 2
229940127089 cytotoxic agent Drugs 0.000 description 2
239000002254 cytotoxic agent Substances 0.000 description 2
230000030609 dephosphorylation Effects 0.000 description 2
238000006209 dephosphorylation reaction Methods 0.000 description 2
230000008030 elimination Effects 0.000 description 2
238000003379 elimination reaction Methods 0.000 description 2
230000004927 fusion Effects 0.000 description 2
238000012224 gene deletion Methods 0.000 description 2
238000010362 genome editing Methods 0.000 description 2
125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 2
230000013595 glycosylation Effects 0.000 description 2
238000006206 glycosylation reaction Methods 0.000 description 2
210000002443 helper t lymphocyte Anatomy 0.000 description 2
239000003112 inhibitor Substances 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
210000000936 intestine Anatomy 0.000 description 2
210000003292 kidney cell Anatomy 0.000 description 2
238000011031 large-scale manufacturing process Methods 0.000 description 2
230000003505 mutagenic effect Effects 0.000 description 2
239000002245 particle Substances 0.000 description 2
239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
229920002401 polyacrylamide Polymers 0.000 description 2
238000002360 preparation method Methods 0.000 description 2
230000008569 process Effects 0.000 description 2
230000020964 regulation of blood coagulation Effects 0.000 description 2
238000010187 selection method Methods 0.000 description 2
239000006152 selective media Substances 0.000 description 2
238000012163 sequencing technique Methods 0.000 description 2
239000012679 serum free medium Substances 0.000 description 2
230000037432 silent mutation Effects 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
229940104230 thymidine Drugs 0.000 description 2
238000004448 titration Methods 0.000 description 2
230000002103 transcriptional effect Effects 0.000 description 2
229940075420 xanthine Drugs 0.000 description 2
RNAMYOYQYRYFQY-UHFFFAOYSA-N 2-(4,4-difluoropiperidin-1-yl)-6-methoxy-n-(1-propan-2-ylpiperidin-4-yl)-7-(3-pyrrolidin-1-ylpropoxy)quinazolin-4-amine Chemical compound N1=C(N2CCC(F)(F)CC2)N=C2C=C(OCCCN3CCCC3)C(OC)=CC2=C1NC1CCN(C(C)C)CC1 RNAMYOYQYRYFQY-UHFFFAOYSA-N 0.000 description 1
108020003589 5' Untranslated Regions Proteins 0.000 description 1
101710191936 70 kDa protein Proteins 0.000 description 1
101150056788 A51R gene Proteins 0.000 description 1
108010088237 ATCGAT-specific type II deoxyribonucleases Proteins 0.000 description 1
RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
241000701386 African swine fever virus Species 0.000 description 1
108010039627 Aprotinin Proteins 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
241001473877 Biserrula isolate Species 0.000 description 1
101000583086 Bunodosoma granuliferum Delta-actitoxin-Bgr2b Proteins 0.000 description 1
102100023702 C-C motif chemokine 13 Human genes 0.000 description 1
108010037936 CCCGGG-specific type II deoxyribonucleases Proteins 0.000 description 1
101100275473 Caenorhabditis elegans ctc-3 gene Proteins 0.000 description 1
241000283707 Capra Species 0.000 description 1
241000700664 Capripoxvirus Species 0.000 description 1
208000003322 Coinfection Diseases 0.000 description 1
241000557626 Corvus corax Species 0.000 description 1
241000699800 Cricetinae Species 0.000 description 1
230000008836 DNA modification Effects 0.000 description 1
230000007018 DNA scission Effects 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
101001092183 Drosophila melanogaster Regulator of gene activity Proteins 0.000 description 1
206010059866 Drug resistance Diseases 0.000 description 1
208000006586 Ectromelia Diseases 0.000 description 1
241000725630 Ectromelia virus Species 0.000 description 1
108010067770 Endopeptidase K Proteins 0.000 description 1
108060002716 Exonuclease Proteins 0.000 description 1
102000009123 Fibrin Human genes 0.000 description 1
108010073385 Fibrin Proteins 0.000 description 1
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
101150111020 GLUL gene Proteins 0.000 description 1
108700039691 Genetic Promoter Regions Proteins 0.000 description 1
108700007698 Genetic Terminator Regions Proteins 0.000 description 1
101150106864 HR gene Proteins 0.000 description 1
208000031220 Hemophilia Diseases 0.000 description 1
208000009292 Hemophilia A Diseases 0.000 description 1
101000978379 Homo sapiens C-C motif chemokine 13 Proteins 0.000 description 1
101100321817 Human parvovirus B19 (strain HV) 7.5K gene Proteins 0.000 description 1
108091092195 Intron Proteins 0.000 description 1
241000701377 Iridoviridae Species 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
101710192606 Latent membrane protein 2 Proteins 0.000 description 1
241000700563 Leporipoxvirus Species 0.000 description 1
206010024503 Limb reduction defect Diseases 0.000 description 1
UGTZHPSKYRIGRJ-YUMQZZPRSA-N Lys-Glu Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O UGTZHPSKYRIGRJ-YUMQZZPRSA-N 0.000 description 1
241001465754 Metazoa Species 0.000 description 1
101000713102 Mus musculus C-C motif chemokine 1 Proteins 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
238000009004 PCR Kit Methods 0.000 description 1
238000012408 PCR amplification Methods 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
241001631646 Papillomaviridae Species 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
241000700625 Poxviridae Species 0.000 description 1
101710192141 Protein Nef Proteins 0.000 description 1
241001455645 Rabbitpox virus Species 0.000 description 1
241000220317 Rosa Species 0.000 description 1
101150010882 S gene Proteins 0.000 description 1
101150082969 SELP gene Proteins 0.000 description 1
101150036293 Selenop gene Proteins 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
101000626626 Serratia marcescens Type II restriction enzyme SmaI Proteins 0.000 description 1
BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
241000700568 Suipoxvirus Species 0.000 description 1
101710137500 T7 RNA polymerase Proteins 0.000 description 1
101710109576 Terminal protein Proteins 0.000 description 1
208000007536 Thrombosis Diseases 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
108091023045 Untranslated Region Proteins 0.000 description 1
101150045640 VWF gene Proteins 0.000 description 1
108010067390 Viral Proteins Proteins 0.000 description 1
210000001766 X chromosome Anatomy 0.000 description 1
230000001594 aberrant effect Effects 0.000 description 1
229960000583 acetic acid Drugs 0.000 description 1
239000002253 acid Substances 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
210000000677 aggregate cell Anatomy 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
238000000137 annealing Methods 0.000 description 1
229960004405 aprotinin Drugs 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
101150047533 artP gene Proteins 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
229940019700 blood coagulation factors Drugs 0.000 description 1
238000010804 cDNA synthesis Methods 0.000 description 1
230000021523 carboxylation Effects 0.000 description 1
238000006473 carboxylation reaction Methods 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
239000002962 chemical mutagen Substances 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
239000003593 chromogenic compound Substances 0.000 description 1
239000013599 cloning vector Substances 0.000 description 1
238000012790 confirmation Methods 0.000 description 1
201000005332 contagious pustular dermatitis Diseases 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
238000011109 contamination Methods 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
230000006378 damage Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000013461 design Methods 0.000 description 1
230000000368 destabilizing effect Effects 0.000 description 1
238000011161 development Methods 0.000 description 1
238000010586 diagram Methods 0.000 description 1
230000008034 disappearance Effects 0.000 description 1
238000010828 elution Methods 0.000 description 1
108010067298 endodeoxyribonuclease RsrII Proteins 0.000 description 1
210000002889 endothelial cell Anatomy 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
108010078428 env Gene Products Proteins 0.000 description 1
102000013165 exonuclease Human genes 0.000 description 1
238000010195 expression analysis Methods 0.000 description 1
229950003499 fibrin Drugs 0.000 description 1
206010016629 fibroma Diseases 0.000 description 1
238000012248 genetic selection Methods 0.000 description 1
239000012362 glacial acetic acid Substances 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
208000009429 hemophilia B Diseases 0.000 description 1
208000031169 hemorrhagic disease Diseases 0.000 description 1
230000023597 hemostasis Effects 0.000 description 1
238000002744 homologous recombination Methods 0.000 description 1
230000006801 homologous recombination Effects 0.000 description 1
238000005805 hydroxylation reaction Methods 0.000 description 1
230000036039 immunity Effects 0.000 description 1
230000003053 immunization Effects 0.000 description 1
238000011065 in-situ storage Methods 0.000 description 1
230000000415 inactivating effect Effects 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
208000007203 infectious ectromelia Diseases 0.000 description 1
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
238000007689 inspection Methods 0.000 description 1
238000011835 investigation Methods 0.000 description 1
210000003734 kidney Anatomy 0.000 description 1
231100000518 lethal Toxicity 0.000 description 1
230000001665 lethal effect Effects 0.000 description 1
210000005229 liver cell Anatomy 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
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 1
108010009298 lysylglutamic acid Proteins 0.000 description 1
230000001404 mediated effect Effects 0.000 description 1
230000002503 metabolic effect Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013206 minimal dilution Methods 0.000 description 1
150000004712 monophosphates Chemical class 0.000 description 1
231100000219 mutagenic Toxicity 0.000 description 1
239000003471 mutagenic agent Substances 0.000 description 1
231100000707 mutagenic chemical Toxicity 0.000 description 1
208000009091 myxoma Diseases 0.000 description 1
PGSADBUBUOPOJS-UHFFFAOYSA-N neutral red Chemical compound Cl.C1=C(C)C(N)=CC2=NC3=CC(N(C)C)=CC=C3N=C21 PGSADBUBUOPOJS-UHFFFAOYSA-N 0.000 description 1
238000007899 nucleic acid hybridization Methods 0.000 description 1
150000007523 nucleic acids Chemical group 0.000 description 1
210000004940 nucleus Anatomy 0.000 description 1
UOJMTSCORVQOHS-UHFFFAOYSA-N pachypodol Natural products COc1cc(ccc1O)C2=C(C)C(=O)c3c(O)cc(C)cc3O2 UOJMTSCORVQOHS-UHFFFAOYSA-N 0.000 description 1
238000012856 packing Methods 0.000 description 1
230000036961 partial effect Effects 0.000 description 1
238000009471 passive packaging Methods 0.000 description 1
230000001717 pathogenic effect Effects 0.000 description 1
230000007030 peptide scission Effects 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
125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
230000007505 plaque formation Effects 0.000 description 1
239000013641 positive control Substances 0.000 description 1
230000008092 positive effect Effects 0.000 description 1
230000000644 propagated effect Effects 0.000 description 1
235000019833 protease Nutrition 0.000 description 1
230000001681 protective effect Effects 0.000 description 1
239000012474 protein marker Substances 0.000 description 1
230000020978 protein processing Effects 0.000 description 1
238000012552 review Methods 0.000 description 1
238000010008 shearing Methods 0.000 description 1
229910052709 silver Inorganic materials 0.000 description 1
239000004332 silver Substances 0.000 description 1
239000000243 solution Substances 0.000 description 1
238000012916 structural analysis Methods 0.000 description 1
239000003104 tissue culture media Substances 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
PIEPQKCYPFFYMG-UHFFFAOYSA-N tris acetate Chemical compound CC(O)=O.OCC(N)(CO)CO PIEPQKCYPFFYMG-UHFFFAOYSA-N 0.000 description 1
241000701161 unidentified adenovirus Species 0.000 description 1
241000700570 unidentified entomopoxvirus Species 0.000 description 1
241001515965 unidentified phage Species 0.000 description 1
230000017613 viral reproduction Effects 0.000 description 1

Landscapes

Micro-Organisms Or Cultivation Processes Thereof (AREA)
Peptides Or Proteins (AREA)

CA002616698A 1991-08-26 1992-08-25 Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie Expired - Fee Related CA2616698C (fr)

Applications Claiming Priority (5)

Application Number	Priority Date	Filing Date	Title
US07/750,080 US5445953A (en)	1991-08-26	1991-08-26	Direct molecular cloning of a modified poxvirus genome
US07/750,080		1991-08-26
US91473892A	1992-07-20	1992-07-20
US07/914,738		1992-07-20
CA002558864A CA2558864C (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie

Related Parent Applications (1)

Application Number	Title	Priority Date	Filing Date
CA002558864A Division CA2558864C (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie

Publications (2)

Publication Number	Publication Date
CA2616698A1 CA2616698A1 (fr)	1993-02-27
CA2616698C true CA2616698C (fr)	2009-03-17

Family

ID=39103181

Family Applications (3)

Application Number	Title	Priority Date	Filing Date
CA2617830A Expired - Fee Related CA2617830C (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucar otique modifie
CA002616698A Expired - Fee Related CA2616698C (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie
CA002616717A Abandoned CA2616717A1 (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie

Family Applications Before (1)

Application Number	Title	Priority Date	Filing Date
CA2617830A Expired - Fee Related CA2617830C (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucar otique modifie

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
CA002616717A Abandoned CA2616717A1 (fr)	1991-08-26	1992-08-25	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie

Country Status (1)

Country	Link
CA (3)	CA2617830C (fr)

1992
- 1992-08-25 CA CA2617830A patent/CA2617830C/fr not_active Expired - Fee Related
- 1992-08-25 CA CA002616698A patent/CA2616698C/fr not_active Expired - Fee Related
- 1992-08-25 CA CA002616717A patent/CA2616717A1/fr not_active Abandoned

Also Published As

Publication number	Publication date
CA2617830A1 (fr)	1993-02-27
CA2616717A1 (fr)	1993-02-27
CA2617830C (fr)	2010-04-06
CA2616698A1 (fr)	1993-02-27

Legal Events

Date	Code	Title	Description
2008-01-31	EEER	Examination request
2011-08-25	MKLA	Lapsed

Publication	Publication Date	Title
EP0561034B1 (fr)	1999-06-09	Clonage moléculaire direct d'un génome modifié d'un virus chordopox
US5445953A (en)	1995-08-29	Direct molecular cloning of a modified poxvirus genome
AU694519B2 (en)	1998-07-23	Recombinant poxviruses with foreign polynucleotides in essential regions
JP3044062B2 (ja)	2000-05-22	組換えポックスウイルス宿主選択系
US5670367A (en)	1997-09-23	Recombinant fowlpox virus
KR101005630B1 (ko)	2011-01-05	수두 바이러스 게놈내로 삽입된 상동 유전자를 발현하는재조합 수두 바이러스
Staib et al.	2000	Transient host range selection for genetic engineering of modified vaccinia virus Ankara
US20030013076A1 (en)	2003-01-16	Parapoxvirus vectors
Scheiflinger et al.	1992	Construction of chimeric vaccinia viruses by molecular cloning and packaging.
JP2549224B2 (ja)	1996-10-30	組換えにより産生される血液因子及びその血液因子の発現方法並びにその方法に使用されるワクシニアウイルス組換え体
EP0753581A1 (fr)	1997-01-15	Virus recombinantes eucaryotes cytoplasmiques améliorés, un procédé pour leur préparation et leur utilisation comme vaccins
EP0338807B1 (fr)	1995-11-02	Production de matériaux protéiniques isolés en utilisant des vecteurs de virus avipox recombinés
JPH0365191A (ja)	1991-03-20	スフェロイジン単離ｄｎａおよび組み換え昆虫ポックスウィルス発現ベクター
Scheiflinger et al.	1998	Transient marker stabilisation: a general procedure to construct marker-free recombinant vaccinia virus
CA2616698C (fr)	2009-03-17	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie
US20040014034A1 (en)	2004-01-22	Method of producing a recombinant virus
EP0422072B1 (fr)	1993-05-19	Procede de selection de virus de la variole recombinants
Mazzara et al.	1993	[39] Generation and analysis of vaccinia virus recombinants
US5691170A (en)	1997-11-25	Generation of hybrid genes and proteins by virus-mediated recombination
EP0469089B1 (fr)	1997-11-19	Generation de genes hybrides et de proteines par recombinaison a mediation virale
CA2558864C (fr)	2009-12-08	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie
CA2515166C (fr)	2007-05-15	Clonage moleculaire direct d'un genome du virus adn cytoplasmique eucaryotique modifie
Hall et al.	1996	TheAmsacta mooreiEntomopoxvirus Spheroidin Gene Is Improperly Transcribed in Vertebrate Poxviruses
SK277781B6 (en)	1995-01-12	Peptides and polypeptides, vaccines and nucleous acid
Pfleiderer et al.	1996	Deletion of the myristylation signal allows high-level production of the hepatitis B virus large surface glycoprotein preS1 with vaccinia virus recombinants