CA2658217A1 - Expression system - Google Patents
Expression system Download PDFInfo
- Publication number
- CA2658217A1 CA2658217A1 CA002658217A CA2658217A CA2658217A1 CA 2658217 A1 CA2658217 A1 CA 2658217A1 CA 002658217 A CA002658217 A CA 002658217A CA 2658217 A CA2658217 A CA 2658217A CA 2658217 A1 CA2658217 A1 CA 2658217A1
- Authority
- CA
- Canada
- Prior art keywords
- domain
- protective
- anthracis
- immunogenic
- immune response
- 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.)
- Abandoned
Links
- 101710194807 Protective antigen Proteins 0.000 claims abstract description 92
- 241000193738 Bacillus anthracis Species 0.000 claims abstract description 51
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 41
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 39
- 229920001184 polypeptide Polymers 0.000 claims abstract description 37
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 35
- 230000028993 immune response Effects 0.000 claims abstract description 34
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 34
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 34
- 241000588724 Escherichia coli Species 0.000 claims abstract description 31
- 230000002163 immunogen Effects 0.000 claims abstract description 29
- 238000000034 method Methods 0.000 claims abstract description 26
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 24
- 229940065181 bacillus anthracis Drugs 0.000 claims abstract description 21
- 239000013598 vector Substances 0.000 claims abstract description 10
- 230000001681 protective effect Effects 0.000 claims description 52
- 108010070675 Glutathione transferase Proteins 0.000 claims description 33
- 102000005720 Glutathione transferase Human genes 0.000 claims description 33
- 208000015181 infectious disease Diseases 0.000 claims description 8
- 230000004927 fusion Effects 0.000 claims description 7
- 238000012258 culturing Methods 0.000 claims description 6
- 230000009466 transformation Effects 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 239000013604 expression vector Substances 0.000 claims description 3
- 239000000203 mixture Substances 0.000 claims description 3
- 238000002360 preparation method Methods 0.000 claims description 3
- 238000011321 prophylaxis Methods 0.000 claims description 3
- 230000001131 transforming effect Effects 0.000 claims description 3
- 238000011282 treatment Methods 0.000 claims description 3
- 241000124008 Mammalia Species 0.000 claims description 2
- 239000003814 drug Substances 0.000 claims description 2
- 108090000623 proteins and genes Proteins 0.000 description 36
- 102000004169 proteins and genes Human genes 0.000 description 33
- 235000018102 proteins Nutrition 0.000 description 30
- 150000001413 amino acids Chemical class 0.000 description 25
- 108020001507 fusion proteins Proteins 0.000 description 25
- 102000037865 fusion proteins Human genes 0.000 description 25
- 235000001014 amino acid Nutrition 0.000 description 24
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 22
- 210000004027 cell Anatomy 0.000 description 20
- 241000699670 Mus sp. Species 0.000 description 16
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical group NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 13
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 11
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 11
- 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 11
- 239000002953 phosphate buffered saline Substances 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 108020004705 Codon Proteins 0.000 description 9
- 101100449763 Anopheles gambiae GstD2 gene Proteins 0.000 description 8
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 8
- 238000013296 A/J mouse Methods 0.000 description 7
- 235000014469 Bacillus subtilis Nutrition 0.000 description 7
- 238000002649 immunization Methods 0.000 description 7
- 101000906005 Fasciola hepatica Glutathione S-transferase class-mu 26 kDa isozyme 1 Proteins 0.000 description 6
- 102100036534 Glutathione S-transferase Mu 1 Human genes 0.000 description 6
- 101000851788 Homo sapiens Eukaryotic peptide chain release factor GTP-binding subunit ERF3A Proteins 0.000 description 6
- 101001071694 Homo sapiens Glutathione S-transferase Mu 1 Proteins 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 238000000855 fermentation Methods 0.000 description 6
- 230000004151 fermentation Effects 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 238000001262 western blot Methods 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 5
- 108010024636 Glutathione Proteins 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 5
- 239000004202 carbamide Substances 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 230000017854 proteolysis Effects 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 101100069663 Caenorhabditis elegans gst-1 gene Proteins 0.000 description 4
- 101100393846 Caenorhabditis elegans gst-4 gene Proteins 0.000 description 4
- 101100449761 Musca domestica Gst1 gene Proteins 0.000 description 4
- 101100449774 Musca domestica Gst4 gene Proteins 0.000 description 4
- 239000004365 Protease Substances 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 230000006698 induction Effects 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 3
- 102100038782 Carbohydrate sulfotransferase 1 Human genes 0.000 description 3
- 101710158459 Carbohydrate sulfotransferase 1 Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 238000009825 accumulation Methods 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 230000007541 cellular toxicity Effects 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 229960003180 glutathione Drugs 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 210000003000 inclusion body Anatomy 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 229960005486 vaccine Drugs 0.000 description 3
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 108700010070 Codon Usage Proteins 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
- 102100036533 Glutathione S-transferase Mu 2 Human genes 0.000 description 2
- 101001071691 Homo sapiens Glutathione S-transferase Mu 2 Proteins 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 101000882995 Mus musculus Carbohydrate sulfotransferase 5 Proteins 0.000 description 2
- 102000016248 PA domains Human genes 0.000 description 2
- 108050004751 PA domains Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108700005078 Synthetic Genes Proteins 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 208000022338 anthrax infection Diseases 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 229940104302 cytosine Drugs 0.000 description 2
- 210000000172 cytosol Anatomy 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- XMTQQYYKAHVGBJ-UHFFFAOYSA-N 3-(3,4-DICHLOROPHENYL)-1,1-DIMETHYLUREA Chemical compound CN(C)C(=O)NC1=CC=C(Cl)C(Cl)=C1 XMTQQYYKAHVGBJ-UHFFFAOYSA-N 0.000 description 1
- PCDWFBFHIIKIPM-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole-2-sulfonic acid Chemical compound C1=CC=C2N(CC)C(S(O)(=O)=O)SC2=C1 PCDWFBFHIIKIPM-UHFFFAOYSA-N 0.000 description 1
- 241000034280 Bacillus anthracis str. Sterne Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 241001646716 Escherichia coli K-12 Species 0.000 description 1
- -1 GSTlb-2 Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930064664 L-arginine Natural products 0.000 description 1
- 235000014852 L-arginine Nutrition 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- HRNLUBSXIHFDHP-UHFFFAOYSA-N N-(2-aminophenyl)-4-[[[4-(3-pyridinyl)-2-pyrimidinyl]amino]methyl]benzamide Chemical compound NC1=CC=CC=C1NC(=O)C(C=C1)=CC=C1CNC1=NC=CC(C=2C=NC=CC=2)=N1 HRNLUBSXIHFDHP-UHFFFAOYSA-N 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 108010023294 Protease La Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 108700042075 T-Cell Receptor Genes Proteins 0.000 description 1
- 102100036407 Thioredoxin Human genes 0.000 description 1
- 241000710959 Venezuelan equine encephalitis virus Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000000240 adjuvant effect Effects 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 238000003556 assay Methods 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
- 230000004071 biological effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
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- 230000003028 elevating effect Effects 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
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- 239000008103 glucose Substances 0.000 description 1
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- 239000012642 immune effector Substances 0.000 description 1
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- 229940121354 immunomodulator Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
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- 239000003999 initiator Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000035987 intoxication Effects 0.000 description 1
- 231100000566 intoxication Toxicity 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000001906 matrix-assisted laser desorption--ionisation mass spectrometry Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 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
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000027086 plasmid maintenance Effects 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 108010006230 protelin Proteins 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000012807 shake-flask culturing Methods 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- AIDBEARHLBRLMO-UHFFFAOYSA-M sodium;dodecyl sulfate;2-morpholin-4-ylethanesulfonic acid Chemical compound [Na+].OS(=O)(=O)CCN1CCOCC1.CCCCCCCCCCCCOS([O-])(=O)=O AIDBEARHLBRLMO-UHFFFAOYSA-M 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
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- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0016702.3 | 2000-07-08 | ||
| GBGB0016702.3A GB0016702D0 (en) | 2000-07-08 | 2000-07-08 | Expression system |
| CA2413045A CA2413045C (en) | 2000-07-08 | 2001-07-06 | Expression system |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2413045A Division CA2413045C (en) | 2000-07-08 | 2001-07-06 | Expression system |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2658217A1 true CA2658217A1 (en) | 2002-01-17 |
Family
ID=9895205
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002658217A Abandoned CA2658217A1 (en) | 2000-07-08 | 2001-07-06 | Expression system |
| CA2413045A Expired - Lifetime CA2413045C (en) | 2000-07-08 | 2001-07-06 | Expression system |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2413045A Expired - Lifetime CA2413045C (en) | 2000-07-08 | 2001-07-06 | Expression system |
Country Status (10)
| Country | Link |
|---|---|
| US (3) | US7537771B2 (enExample) |
| EP (2) | EP1301606A1 (enExample) |
| JP (2) | JP2004502460A (enExample) |
| CN (2) | CN1322134C (enExample) |
| AU (1) | AU2007201553B8 (enExample) |
| CA (2) | CA2658217A1 (enExample) |
| GB (1) | GB0016702D0 (enExample) |
| RU (2) | RU2385348C2 (enExample) |
| WO (1) | WO2002004646A1 (enExample) |
| ZA (1) | ZA200210206B (enExample) |
Families Citing this family (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB0016702D0 (en) | 2000-07-08 | 2000-08-23 | Secr Defence Brit | Expression system |
| US7601351B1 (en) | 2002-06-26 | 2009-10-13 | Human Genome Sciences, Inc. | Antibodies against protective antigen |
| AU2003278776A1 (en) * | 2002-09-10 | 2004-04-30 | Vical Incorporated | Codon-optimized polynucleotide-based vaccines against bacillus anthracis infection |
| US9453251B2 (en) | 2002-10-08 | 2016-09-27 | Pfenex Inc. | Expression of mammalian proteins in Pseudomonas fluorescens |
| AU2003303307B2 (en) | 2002-11-15 | 2006-12-07 | Gen-Probe Incorporated | Assay and compositions for detection of bacillus anthracis nucleic acid |
| EP1670505B1 (en) | 2003-09-18 | 2012-11-14 | GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Dna promoters and anthrax vaccines |
| FR2860005A1 (fr) * | 2003-09-23 | 2005-03-25 | Univ Aix Marseille Ii | Methode de detection d'agents bacteriens ou viraux de bioterrorisme |
| WO2005030991A1 (fr) * | 2003-09-23 | 2005-04-07 | Universite De La Mediterranee (Aix-Marseille Ii) | Methode de detection d’agents bacteriens ou viraux de bioterrorisme |
| GB0401036D0 (en) * | 2004-01-17 | 2004-02-18 | Royal Holloway University Of L | Improvements in or relating to vaccination |
| US8101735B2 (en) | 2004-06-16 | 2012-01-24 | Health Protection Agency | Preparation of protective antigen |
| US7355027B2 (en) | 2004-06-16 | 2008-04-08 | Dynport Vaccine Company Llc | Bacillus anthracis protective antigen |
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| RU2115433C1 (ru) * | 1992-08-28 | 1998-07-20 | Научно-исследовательский институт микробиологии МО РФ | Вакцина сибиреязвенная комбинированная |
| US5677274A (en) | 1993-02-12 | 1997-10-14 | The Government Of The United States As Represented By The Secretary Of The Department Of Health And Human Services | Anthrax toxin fusion proteins and related methods |
| RU2110575C1 (ru) * | 1995-07-19 | 1998-05-10 | Государственное Федеральное предприятие Государственный научный центр прикладной микробиологии | Рекомбинантная плазмидная днк pro pf 5, определяющая синтез капсульного антигена fi возбудителя чумы и протективного антигена возбудителя сибирской язвы, и способ конструирования рекомбинантной плазмидной днк pro pf5 |
| WO2000002522A2 (en) | 1998-07-10 | 2000-01-20 | U.S. Medical Research Institute Of Infectious Diseases | Anthrax vaccine |
| GB0016702D0 (en) | 2000-07-08 | 2000-08-23 | Secr Defence Brit | Expression system |
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2000
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- 2001-07-06 EP EP01947659A patent/EP1301606A1/en not_active Withdrawn
- 2001-07-06 CN CNA2006101290967A patent/CN101012458A/zh active Pending
- 2001-07-06 CA CA002658217A patent/CA2658217A1/en not_active Abandoned
- 2001-07-06 RU RU2004134341/13A patent/RU2385348C2/ru not_active IP Right Cessation
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- 2001-07-06 EP EP07005671.8A patent/EP1808489B1/en not_active Expired - Lifetime
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| EP1301606A1 (en) | 2003-04-16 |
| US20130164823A1 (en) | 2013-06-27 |
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| ZA200210206B (en) | 2004-03-17 |
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| AU2007201553B8 (en) | 2010-06-03 |
| CN101012458A (zh) | 2007-08-08 |
| US7537771B2 (en) | 2009-05-26 |
| EP1808489B1 (en) | 2016-03-23 |
| US9346860B2 (en) | 2016-05-24 |
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| AU2007201553A1 (en) | 2007-05-03 |
| RU2270865C2 (ru) | 2006-02-27 |
| AU2007201553B2 (en) | 2010-04-22 |
| WO2002004646A1 (en) | 2002-01-17 |
| US8313928B2 (en) | 2012-11-20 |
| JP2012010706A (ja) | 2012-01-19 |
| JP2004502460A (ja) | 2004-01-29 |
| AU6930501A (en) | 2002-01-21 |
| CN1440459A (zh) | 2003-09-03 |
| GB0016702D0 (en) | 2000-08-23 |
| CN1322134C (zh) | 2007-06-20 |
| CA2413045A1 (en) | 2002-01-17 |
| US20030170263A1 (en) | 2003-09-11 |
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