NO310417B1 - Fremstilling av rekombinante Borrelia-proteiner - Google Patents
Fremstilling av rekombinante Borrelia-proteiner Download PDFInfo
- Publication number
- NO310417B1 NO310417B1 NO19941376A NO941376A NO310417B1 NO 310417 B1 NO310417 B1 NO 310417B1 NO 19941376 A NO19941376 A NO 19941376A NO 941376 A NO941376 A NO 941376A NO 310417 B1 NO310417 B1 NO 310417B1
- Authority
- NO
- Norway
- Prior art keywords
- ospa
- lipoprotein
- phase
- borrelia
- proteins
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 77
- 102000004169 proteins and genes Human genes 0.000 title claims description 47
- 208000016604 Lyme disease Diseases 0.000 title claims description 31
- 241000589968 Borrelia Species 0.000 title claims description 24
- 238000002360 preparation method Methods 0.000 title description 2
- 108090001030 Lipoproteins Proteins 0.000 claims description 69
- 102000004895 Lipoproteins Human genes 0.000 claims description 67
- 239000003599 detergent Substances 0.000 claims description 46
- 239000013612 plasmid Substances 0.000 claims description 41
- 238000000034 method Methods 0.000 claims description 31
- 239000012071 phase Substances 0.000 claims description 30
- 241000588724 Escherichia coli Species 0.000 claims description 23
- 238000000746 purification Methods 0.000 claims description 18
- 238000004519 manufacturing process Methods 0.000 claims description 14
- 229920004929 Triton X-114 Polymers 0.000 claims description 12
- 239000000203 mixture Substances 0.000 claims description 12
- IDOQDZANRZQBTP-UHFFFAOYSA-N 2-[2-(2,4,4-trimethylpentan-2-yl)phenoxy]ethanol Chemical compound CC(C)(C)CC(C)(C)C1=CC=CC=C1OCCO IDOQDZANRZQBTP-UHFFFAOYSA-N 0.000 claims description 11
- 238000004587 chromatography analysis Methods 0.000 claims description 11
- 239000008346 aqueous phase Substances 0.000 claims description 10
- 230000006698 induction Effects 0.000 claims description 9
- 238000005191 phase separation Methods 0.000 claims description 8
- 238000000926 separation method Methods 0.000 claims description 6
- 230000001580 bacterial effect Effects 0.000 claims description 4
- 230000008014 freezing Effects 0.000 claims description 4
- 238000007710 freezing Methods 0.000 claims description 4
- 239000007790 solid phase Substances 0.000 claims description 4
- 238000005119 centrifugation Methods 0.000 claims description 3
- 230000009089 cytolysis Effects 0.000 claims description 3
- 238000010828 elution Methods 0.000 claims description 3
- 230000001965 increasing effect Effects 0.000 claims description 3
- 101150107995 ACA1 gene Proteins 0.000 claims description 2
- 101100135127 Borrelia burgdorferi ospA gene Proteins 0.000 claims description 2
- 239000000872 buffer Substances 0.000 claims description 2
- 239000002158 endotoxin Substances 0.000 claims description 2
- 239000007788 liquid Substances 0.000 claims description 2
- 239000004094 surface-active agent Substances 0.000 claims description 2
- 238000010257 thawing Methods 0.000 claims description 2
- 239000012466 permeate Substances 0.000 claims 4
- 239000003480 eluent Substances 0.000 claims 1
- 229920006008 lipopolysaccharide Polymers 0.000 claims 1
- 230000002934 lysing effect Effects 0.000 claims 1
- 230000000717 retained effect Effects 0.000 claims 1
- 239000002699 waste material Substances 0.000 claims 1
- 101710105714 Outer surface protein A Proteins 0.000 description 73
- 235000018102 proteins Nutrition 0.000 description 37
- 241000589969 Borreliella burgdorferi Species 0.000 description 25
- 241000699670 Mus sp. Species 0.000 description 25
- 101150045801 ospA gene Proteins 0.000 description 24
- 229940099789 ospa protein Drugs 0.000 description 15
- 108700006640 OspA Proteins 0.000 description 14
- 230000005847 immunogenicity Effects 0.000 description 13
- 210000004027 cell Anatomy 0.000 description 12
- 210000002966 serum Anatomy 0.000 description 12
- 102000036639 antigens Human genes 0.000 description 10
- 108091007433 antigens Proteins 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 150000002632 lipids Chemical group 0.000 description 10
- 238000003752 polymerase chain reaction Methods 0.000 description 10
- 229920002271 DEAE-Sepharose Polymers 0.000 description 9
- 239000000427 antigen Substances 0.000 description 9
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 9
- 239000008188 pellet Substances 0.000 description 9
- 108010077805 Bacterial Proteins Proteins 0.000 description 8
- 241000589970 Spirochaetales Species 0.000 description 8
- 238000010367 cloning Methods 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 231100000673 dose–response relationship Toxicity 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 230000012010 growth Effects 0.000 description 7
- 230000004044 response Effects 0.000 description 7
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 6
- 210000004899 c-terminal region Anatomy 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 5
- 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 5
- 229930027917 kanamycin Natural products 0.000 description 5
- 229960000318 kanamycin Drugs 0.000 description 5
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 5
- 229930182823 kanamycin A Natural products 0.000 description 5
- 239000006166 lysate Substances 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 229960005486 vaccine Drugs 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 239000013504 Triton X-100 Substances 0.000 description 4
- 229920004890 Triton X-100 Polymers 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 230000002163 immunogen Effects 0.000 description 4
- 208000015181 infectious disease Diseases 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 239000013615 primer Substances 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 239000012130 whole-cell lysate Substances 0.000 description 4
- QENJLXATANVWMR-UHFFFAOYSA-N 2-[(3-amino-3-imino-2-methylpropanethioyl)amino]acetic acid Chemical compound NC(=N)C(C)C(=S)NCC(O)=O QENJLXATANVWMR-UHFFFAOYSA-N 0.000 description 3
- 238000011725 BALB/c mouse Methods 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 3
- 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 3
- 238000012286 ELISA Assay Methods 0.000 description 3
- 108010052285 Membrane Proteins Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 150000001413 amino acids Chemical group 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 238000002255 vaccination Methods 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 239000003155 DNA primer Substances 0.000 description 2
- 241000701832 Enterobacteria phage T3 Species 0.000 description 2
- 239000012480 LAL reagent Substances 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 101710137500 T7 RNA polymerase Proteins 0.000 description 2
- 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 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- OOYGSFOGFJDDHP-KMCOLRRFSA-N kanamycin A sulfate Chemical compound OS(O)(=O)=O.O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N OOYGSFOGFJDDHP-KMCOLRRFSA-N 0.000 description 2
- 229960002064 kanamycin sulfate Drugs 0.000 description 2
- 210000004897 n-terminal region Anatomy 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010056891 Calnexin Proteins 0.000 description 1
- 102000034342 Calnexin Human genes 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 1
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 1
- 206010013700 Drug hypersensitivity Diseases 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 235000012601 Euterpe oleracea Nutrition 0.000 description 1
- 244000207620 Euterpe oleracea Species 0.000 description 1
- 102000005720 Glutathione transferase Human genes 0.000 description 1
- 108010070675 Glutathione transferase Proteins 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
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241001180982 Lappula squarrosa Species 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108010034634 Repressor Proteins Proteins 0.000 description 1
- 102000009661 Repressor Proteins Human genes 0.000 description 1
- 108090000233 Signal peptidase II Proteins 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 235000003650 acai Nutrition 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 229940126575 aminoglycoside Drugs 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
- 125000000926 ampicilloyl group Chemical group [H]N([H])[C@@]([H])(C(=O)N([H])[C@]1([H])C(=O)N2[C@]1([H])SC(C([H])([H])[H])(C([H])([H])[H])[C@]2([H])C(*)=O)C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
- 230000002917 arthritic effect Effects 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 101150049515 bla gene Proteins 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 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
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- -1 isopropyl- Chemical group 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 201000005354 penicillin allergy Diseases 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229940079862 sodium lauryl sarcosinate Drugs 0.000 description 1
- ADWNFGORSPBALY-UHFFFAOYSA-M sodium;2-[dodecyl(methyl)amino]acetate Chemical group [Na+].CCCCCCCCCCCCN(C)CC([O-])=O ADWNFGORSPBALY-UHFFFAOYSA-M 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 206010048282 zoonosis Diseases 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
- C07K14/20—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Spirochaetales (O), e.g. Treponema, Leptospira
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Communicable Diseases (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Genetics & Genomics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US77904891A | 1991-10-18 | 1991-10-18 | |
| US88876592A | 1992-05-27 | 1992-05-27 | |
| PCT/US1992/008697 WO1993008299A1 (en) | 1991-10-18 | 1992-10-16 | Preparation of recombinant borrelia proteins |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO941376D0 NO941376D0 (no) | 1994-04-15 |
| NO941376L NO941376L (no) | 1994-06-17 |
| NO310417B1 true NO310417B1 (no) | 2001-07-02 |
Family
ID=27119531
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19941376A NO310417B1 (no) | 1991-10-18 | 1994-04-15 | Fremstilling av rekombinante Borrelia-proteiner |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP0620860A4 (de) |
| JP (1) | JPH06511154A (de) |
| AU (1) | AU676140B2 (de) |
| CA (1) | CA2121121C (de) |
| FI (1) | FI941749A (de) |
| IL (1) | IL103462A0 (de) |
| NO (1) | NO310417B1 (de) |
| PT (1) | PT100980B (de) |
| WO (1) | WO1993008299A1 (de) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE4015911A1 (de) | 1989-09-19 | 1991-03-28 | Max Planck Gesellschaft | Impfstoff gegen die lyme-krankheit |
| EP0878545A3 (de) * | 1991-08-15 | 1998-12-16 | SMITHKLINE BEECHAM BIOLOGICALS s.a. | OspA Proteine von Borrelia Burgdorferi Untergruppen , dafür kodierende Gene sowie Impfstoffe |
| US6676942B1 (en) | 1991-08-15 | 2004-01-13 | Smithkline Beecham Biologicals (S.A.) | Osp a proteins of Borrelia burgdorferi subgroups, encoding genes and vaccines |
| CA2105629A1 (en) * | 1992-09-14 | 1994-03-15 | Robert S. Becker | Potentiation of immunogenic response |
| US7008625B2 (en) | 1993-11-01 | 2006-03-07 | Research Foundation Of The State University Of New York | Recombinant constructs of Borrelia burgdorferi |
| US6248562B1 (en) | 1993-11-01 | 2001-06-19 | Research Foundation State University Of New York | Chimeric proteins comprising borrelia polypeptides and uses therefor |
| US6610838B1 (en) | 1997-09-10 | 2003-08-26 | Symbicom Aktiebolag | P13 antigens from Borrelia |
| US6224882B1 (en) | 1997-11-07 | 2001-05-01 | Protein Science Corp. | Insect cells or fractions as adjuvant for antigens |
| GB9811219D0 (en) * | 1998-05-26 | 1998-07-22 | Smithkline Beecham Biolog | Novel process |
| US6667038B1 (en) * | 1999-04-21 | 2003-12-23 | Boston Medical Center Corp. | Prevention, diagnosis and treatment of lyme disease |
| WO2002016421A2 (en) | 2000-08-18 | 2002-02-28 | Research Foundation Of The State University Of New York | Altered ospa of borrelia burgdorferi |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK590288D0 (da) * | 1988-10-24 | 1988-10-24 | Symbicom Ab | Kemiske forbindelser |
| DE4015911A1 (de) * | 1989-09-19 | 1991-03-28 | Max Planck Gesellschaft | Impfstoff gegen die lyme-krankheit |
| DE59010422D1 (de) * | 1989-12-22 | 1996-08-22 | Mikrogen Molekularbiol Entw | Immunologisch aktive proteine von borrelia burgdorferi, zusammenhängende testkits und impfstoff |
| CA2057536C (en) * | 1990-12-21 | 1999-10-26 | John J. Dunn | Cloning and expression of borrelia lipoproteins |
| EP0878545A3 (de) * | 1991-08-15 | 1998-12-16 | SMITHKLINE BEECHAM BIOLOGICALS s.a. | OspA Proteine von Borrelia Burgdorferi Untergruppen , dafür kodierende Gene sowie Impfstoffe |
-
1992
- 1992-10-16 EP EP92922390A patent/EP0620860A4/en not_active Withdrawn
- 1992-10-16 JP JP5507751A patent/JPH06511154A/ja active Pending
- 1992-10-16 CA CA002121121A patent/CA2121121C/en not_active Expired - Fee Related
- 1992-10-16 AU AU28011/92A patent/AU676140B2/en not_active Ceased
- 1992-10-16 WO PCT/US1992/008697 patent/WO1993008299A1/en not_active Application Discontinuation
- 1992-10-16 PT PT100980A patent/PT100980B/pt not_active IP Right Cessation
- 1992-10-18 IL IL103462A patent/IL103462A0/xx unknown
-
1994
- 1994-04-15 NO NO19941376A patent/NO310417B1/no not_active IP Right Cessation
- 1994-04-15 FI FI941749A patent/FI941749A/fi unknown
Also Published As
| Publication number | Publication date |
|---|---|
| NO941376D0 (no) | 1994-04-15 |
| AU2801192A (en) | 1993-05-21 |
| AU676140B2 (en) | 1997-03-06 |
| IL103462A0 (en) | 1993-03-15 |
| PT100980B (pt) | 1999-07-30 |
| FI941749A (fi) | 1994-05-25 |
| FI941749A0 (fi) | 1994-04-15 |
| PT100980A (pt) | 1994-01-31 |
| WO1993008299A1 (en) | 1993-04-29 |
| CA2121121C (en) | 2003-06-10 |
| EP0620860A4 (en) | 1997-05-02 |
| NO941376L (no) | 1994-06-17 |
| JPH06511154A (ja) | 1994-12-15 |
| CA2121121A1 (en) | 1993-04-29 |
| EP0620860A1 (de) | 1994-10-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Fairweather et al. | Immunization of mice against tetanus with fragments of tetanus toxin synthesized in Escherichia coli | |
| Dunn et al. | Outer surface protein A (OspA) from the Lyme disease spirochete, Borrelia burgdorferi: high level expression and purification of a soluble recombinant form of OspA | |
| AU2007201553B8 (en) | Expression system | |
| JP5566684B2 (ja) | Ｃｌｏｓｔｒｉｄｉｕｍｄｉｆｆｉｃｉｌｅに対する、組換え毒素Ａ／毒素Ｂワクチン | |
| JP2981286B2 (ja) | 破傷風トキシンフラグメントｃの発現 | |
| EP0863211A1 (de) | Expression von rekombinanten Fusionsproteinen in abgeschwächten Bakterien | |
| US5571718A (en) | Cloning and expression of soluble truncated variants of Borrelia OspA, OspB and Vmp7 | |
| AU721954B2 (en) | Expression of lipoproteins | |
| NO310417B1 (no) | Fremstilling av rekombinante Borrelia-proteiner | |
| Knapp et al. | Protection of Aotus monkeys from malaria infection by immunization with recombinant hybrid proteins | |
| JP3236610B2 (ja) | 豚胸膜肺炎用ワクチン | |
| PL186847B1 (pl) | Konstrukcja DNA, wektor ekspresyjny, gospodarz, białko fuzyjne i sposób przygotowania bakterii | |
| EP1648501B1 (de) | Hybrid-toxine mit shiga-artigen toxin-untereinheiten, verbunden mit escherichia coli wärmeinstabilen enterotoxin-untereinheiten und vakzine daraus | |
| WO1991007979A1 (en) | Chimeric proteins | |
| AU7514494A (en) | Method for expression and purification of p2 protein from haemophilus influenzae type b | |
| CA2516661C (en) | M. haemolytica outer membrane protein plpe as a vaccine or vaccine component against shipping fever | |
| JPH11507827A (ja) | Ｆ型ボツリヌス毒素およびその用途 | |
| US7794734B2 (en) | Mannheimia haemolytica chimeric outer membrane protein PlpE and leukotoxin epitopes as a vaccine or vaccine component against shipping fever | |
| GB2232675A (en) | Stable forms of antigenic taenia ovis polypeptides | |
| US5366728A (en) | Stable forms of antigenic Taenia ovis polypeptides | |
| WO1990015132A2 (en) | Cloned treponema hyodysenteriae endoflagellar antigen | |
| WO2004000343A1 (en) | Recombinant polypeptide for immunocastration and vaccine comprising the same | |
| CA2281913A1 (en) | A vaccine against piscirickettsia salmonis based on a recombinant 17 kd protein |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |
Free format text: LAPSED IN APRIL 2003 |