NO304546B1 - Preparat omfattende et immunogen i form av B. burgdorferi-pC-polypeptider, for immunisering av et pattedyr mot Lymeborreliose, samt anvendelse av preparat for fremstilling av et farmas°ytisk preparat for behandling av Lyme-borreliose - Google Patents
Preparat omfattende et immunogen i form av B. burgdorferi-pC-polypeptider, for immunisering av et pattedyr mot Lymeborreliose, samt anvendelse av preparat for fremstilling av et farmas°ytisk preparat for behandling av Lyme-borreliose Download PDFInfo
- Publication number
- NO304546B1 NO304546B1 NO922746A NO922746A NO304546B1 NO 304546 B1 NO304546 B1 NO 304546B1 NO 922746 A NO922746 A NO 922746A NO 922746 A NO922746 A NO 922746A NO 304546 B1 NO304546 B1 NO 304546B1
- Authority
- NO
- Norway
- Prior art keywords
- protein
- preparation
- immunogen
- preparation according
- polypeptide
- Prior art date
Links
- 241000124008 Mammalia Species 0.000 title claims abstract description 20
- 230000002163 immunogen Effects 0.000 title claims abstract description 20
- 241000589969 Borreliella burgdorferi Species 0.000 title claims abstract description 17
- 238000002360 preparation method Methods 0.000 title claims description 36
- 229920001184 polypeptide Polymers 0.000 title claims description 11
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 11
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 11
- 239000000825 pharmaceutical preparation Substances 0.000 title claims description 5
- 238000011282 treatment Methods 0.000 title claims description 5
- 230000003053 immunization Effects 0.000 title description 12
- 238000002649 immunization Methods 0.000 title description 10
- 208000016604 Lyme disease Diseases 0.000 claims abstract description 32
- 239000000546 pharmaceutical excipient Substances 0.000 claims abstract description 7
- 239000000427 antigen Substances 0.000 claims description 52
- 102000036639 antigens Human genes 0.000 claims description 52
- 108091007433 antigens Proteins 0.000 claims description 52
- 238000004519 manufacturing process Methods 0.000 claims description 12
- 230000028993 immune response Effects 0.000 claims description 10
- 230000000405 serological effect Effects 0.000 claims description 9
- 238000004255 ion exchange chromatography Methods 0.000 claims description 7
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 4
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical group [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 claims description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 2
- 108091034117 Oligonucleotide Proteins 0.000 claims description 2
- 238000003752 polymerase chain reaction Methods 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 83
- 102000004169 proteins and genes Human genes 0.000 abstract description 79
- 238000000034 method Methods 0.000 description 40
- 210000004027 cell Anatomy 0.000 description 37
- 208000015181 infectious disease Diseases 0.000 description 22
- 101150045801 ospA gene Proteins 0.000 description 21
- 239000000872 buffer Substances 0.000 description 18
- 238000000746 purification Methods 0.000 description 18
- 239000003599 detergent Substances 0.000 description 17
- 108020004414 DNA Proteins 0.000 description 15
- 241001465754 Metazoa Species 0.000 description 13
- 230000001681 protective effect Effects 0.000 description 13
- 241000699694 Gerbillinae Species 0.000 description 12
- 102000037865 fusion proteins Human genes 0.000 description 12
- 108020001507 fusion proteins Proteins 0.000 description 12
- 239000012528 membrane Substances 0.000 description 12
- 210000004379 membrane Anatomy 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 11
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical group [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 description 11
- 229960005486 vaccine Drugs 0.000 description 11
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 10
- 101150107960 ospB gene Proteins 0.000 description 10
- 239000013598 vector Substances 0.000 description 9
- 241001180982 Lappula squarrosa Species 0.000 description 8
- 102000004895 Lipoproteins Human genes 0.000 description 8
- 108090001030 Lipoproteins Proteins 0.000 description 8
- 101150005926 Pc gene Proteins 0.000 description 8
- 239000000523 sample Substances 0.000 description 8
- 241000589968 Borrelia Species 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 201000010099 disease Diseases 0.000 description 7
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 7
- 239000012634 fragment Substances 0.000 description 7
- 241000700626 Cowpox virus Species 0.000 description 6
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 6
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- 239000000306 component Substances 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 230000036039 immunity Effects 0.000 description 6
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 239000011521 glass Substances 0.000 description 5
- 210000002216 heart Anatomy 0.000 description 5
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 5
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 5
- 210000003734 kidney Anatomy 0.000 description 5
- 229910001629 magnesium chloride Inorganic materials 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 210000000952 spleen Anatomy 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- 108010067770 Endopeptidase K Proteins 0.000 description 4
- 108010052285 Membrane Proteins Proteins 0.000 description 4
- 102400000368 Surface protein Human genes 0.000 description 4
- 108090000631 Trypsin Proteins 0.000 description 4
- 102000004142 Trypsin Human genes 0.000 description 4
- 102000004139 alpha-Amylases Human genes 0.000 description 4
- 108090000637 alpha-Amylases Proteins 0.000 description 4
- 229940024171 alpha-amylase Drugs 0.000 description 4
- 230000027455 binding Effects 0.000 description 4
- 239000013599 cloning vector Substances 0.000 description 4
- 201000003740 cowpox Diseases 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000012588 trypsin Substances 0.000 description 4
- 210000003932 urinary bladder Anatomy 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- -1 aluminum compound Chemical class 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 229940088710 antibiotic agent Drugs 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 210000001124 body fluid Anatomy 0.000 description 3
- 239000010839 body fluid Substances 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 238000011835 investigation Methods 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 3
- 108091033319 polynucleotide Proteins 0.000 description 3
- 102000040430 polynucleotide Human genes 0.000 description 3
- 239000002157 polynucleotide Substances 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 229920000856 Amylose Polymers 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 210000000712 G cell Anatomy 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 241000589970 Spirochaetales Species 0.000 description 2
- 208000035056 Tick-Borne disease Diseases 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 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 2
- 238000010171 animal model Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 206010003246 arthritis Diseases 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000001684 chronic effect Effects 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 210000003495 flagella Anatomy 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- IPCSVZSSVZVIGE-UHFFFAOYSA-N hexadecanoic acid Chemical compound CCCCCCCCCCCCCCCC(O)=O IPCSVZSSVZVIGE-UHFFFAOYSA-N 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 239000002198 insoluble material Substances 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 239000003456 ion exchange resin Substances 0.000 description 2
- 229920003303 ion-exchange polymer Polymers 0.000 description 2
- 210000001503 joint Anatomy 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 210000000653 nervous system Anatomy 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-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 1
- 241000238876 Acari Species 0.000 description 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101100028791 Caenorhabditis elegans pbs-5 gene Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000483002 Euproctis similis Species 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 102000005720 Glutathione transferase Human genes 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 206010023232 Joint swelling Diseases 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 229920001491 Lentinan Polymers 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 241001082241 Lythrum hyssopifolia Species 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 101710160107 Outer membrane protein A Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 235000021314 Palmitic acid Nutrition 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 238000011579 SCID mouse model Methods 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 230000024932 T cell mediated immunity Effects 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000004523 agglutinating effect Effects 0.000 description 1
- 230000002009 allergenic effect Effects 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007434 bsk-medium Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 229940023913 cation exchange resins Drugs 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 238000001446 dark-field microscopy Methods 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 230000009567 fermentative growth Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000028996 humoral immune response Effects 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 230000004957 immunoregulator effect Effects 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 229940115286 lentinan Drugs 0.000 description 1
- 229920006008 lipopolysaccharide Polymers 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000011866 long-term treatment Methods 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000012533 medium component Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 235000010446 mineral oil Nutrition 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229940099789 ospa protein Drugs 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 239000003223 protective agent Substances 0.000 description 1
- 210000004777 protein coat Anatomy 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000003906 pulsed field gel electrophoresis Methods 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000284 resting effect Effects 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 239000013606 secretion vector Substances 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000000856 sucrose gradient centrifugation Methods 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 208000006379 syphilis Diseases 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000014621 translational initiation 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
- 210000002700 urine Anatomy 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 239000003643 water by type Substances 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
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/825—Bacteria
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (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)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicinal Preparation (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US72724591A | 1991-07-11 | 1991-07-11 | |
| US82416192A | 1992-01-22 | 1992-01-22 | |
| US07/903,580 US6221363B1 (en) | 1991-07-11 | 1992-06-25 | Vaccine for the prevention of lyme disease |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO922746D0 NO922746D0 (no) | 1992-07-10 |
| NO922746L NO922746L (no) | 1993-01-12 |
| NO304546B1 true NO304546B1 (no) | 1999-01-11 |
Family
ID=27419096
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO922746A NO304546B1 (no) | 1991-07-11 | 1992-07-10 | Preparat omfattende et immunogen i form av B. burgdorferi-pC-polypeptider, for immunisering av et pattedyr mot Lymeborreliose, samt anvendelse av preparat for fremstilling av et farmas°ytisk preparat for behandling av Lyme-borreliose |
Country Status (17)
| Country | Link |
|---|---|
| US (2) | US6221363B1 (fr) |
| EP (1) | EP0522560B2 (fr) |
| JP (1) | JP2611095B2 (fr) |
| AT (1) | ATE198489T1 (fr) |
| AU (1) | AU660178B2 (fr) |
| CA (1) | CA2073486C (fr) |
| CZ (1) | CZ280743B6 (fr) |
| DE (1) | DE69231619T3 (fr) |
| DK (1) | DK0522560T4 (fr) |
| ES (1) | ES2154633T3 (fr) |
| FI (1) | FI107334B (fr) |
| HR (1) | HRP950174B1 (fr) |
| HU (1) | HU219772B (fr) |
| MX (1) | MX9204078A (fr) |
| NO (1) | NO304546B1 (fr) |
| SI (1) | SI9200143B (fr) |
| SK (1) | SK217292A3 (fr) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6872550B1 (en) * | 1991-07-11 | 2005-03-29 | Baxter Vaccine Ag | Immunogenic formulation of OspC antigen vaccines for the prevention and treatment of lyme disease and recombinant methods for the preparation of such antigens |
| US6303129B1 (en) * | 1992-07-28 | 2001-10-16 | Rx Technologies | Production of borrelia burgdorferi vaccine, product produced thereby and method of use |
| DE69408135T2 (de) * | 1993-04-29 | 1998-06-10 | Immuno Ag | Ospc-antigen-impfstoffe immunogene zusammensetzung zur vorbeugung und behandlung von lyme-krankheit und rekombinante verfahren zur herstellung von derartige antigene |
| US6248562B1 (en) | 1993-11-01 | 2001-06-19 | Research Foundation State University Of New York | Chimeric proteins comprising borrelia polypeptides and uses therefor |
| US7008625B2 (en) | 1993-11-01 | 2006-03-07 | Research Foundation Of The State University Of New York | Recombinant constructs of Borrelia burgdorferi |
| ES2265643T3 (es) | 1994-04-11 | 2007-02-16 | Wyeth Holdings Corporation | Bacteria de borrelia burgdorferi. |
| US6087097A (en) * | 1994-05-12 | 2000-07-11 | Mayo Foundation For Medical Education And Research | PCR detection of Borrelia burgdorferi |
| ZA964896B (en) * | 1995-06-07 | 1997-01-08 | Connaught Lab | Expression of lipoproteins |
| AU712213B2 (en) * | 1995-09-22 | 1999-11-04 | Connaught Laboratories Limited | Parainfluenza virus glycoproteins and vaccines |
| EP0880543A4 (fr) * | 1995-10-26 | 2000-08-02 | Rhode Island Education | Antigenes servant de candidats vaccins et tires du spirochete (borrelia burgdorferi) de la maladie de lyme induit par la salive d'une tique vecteur (ixodes scapularis) |
| US6045804A (en) * | 1996-03-07 | 2000-04-04 | Mayo Foundation For Medical Educational Research | Method for detecting B. burgdorferi infection |
| US6716574B2 (en) | 1996-05-02 | 2004-04-06 | Dako A/S | Osp-C derived peptide fragments |
| US6969520B2 (en) | 1997-10-20 | 2005-11-29 | Acambis Inc. | Active immunization against clostridium difficile disease |
| GB9811219D0 (en) * | 1998-05-26 | 1998-07-22 | Smithkline Beecham Biolog | Novel process |
| WO2000063386A2 (fr) * | 1999-04-21 | 2000-10-26 | Boston Medical Center Corporation | Prevention, diagnostic et traitement de la maladie de lyme |
| ES2272296T3 (es) | 1999-06-18 | 2007-05-01 | Research Foundation Of State University Of New York | Grupos de borrelia burgdorferi que producen la enfermedad de lyme en humanos. |
| EP1311540B1 (fr) | 2000-08-18 | 2007-12-19 | Research Foundation Of State University Of New York | Ospa du borrelia burgdorferi modifie |
| US8277852B2 (en) * | 2002-01-25 | 2012-10-02 | Akzo Nobel Surface Chemistry Llc | Bioactive botanical cosmetic compositions and processes for their production |
| US7442391B2 (en) | 2002-01-25 | 2008-10-28 | Integrated Botanical Technologies, Llc | Bioactive botanical cosmetic compositions and processes for their production |
| ES2652603T3 (es) | 2004-01-12 | 2018-02-05 | Isp Investments Llc | Composiciones bioactivas de plantas de Theacea y procedimientos para su producción y uso |
| WO2007083834A1 (fr) | 2006-01-19 | 2007-07-26 | Toyo Seikan Kaisha, Ltd. | Coupleur et cartouche de combustible pour pile a combustible |
| BRPI0719360B1 (pt) * | 2006-11-03 | 2016-09-06 | Intervet Int Bv | vacina da doença de lyme canina, e, uso de organismos de uma genoespécie de borrelia |
| CA2677023C (fr) * | 2007-02-22 | 2016-08-30 | Baxter International Inc. | Procede de purification de proteines hydrophobes |
| WO2009131665A1 (fr) * | 2008-04-22 | 2009-10-29 | Research Foundation Of State University Of New York | Réseau de protéines d'enveloppes de cellules de borrelia burgdorferi |
| CA2781110C (fr) * | 2009-11-17 | 2018-07-31 | Abaxis, Inc. | Peptides et procedes pour la detection d'anticorps contre la maladie de lyme |
| BR112013027229B1 (pt) | 2011-04-22 | 2020-10-27 | Wyeth Llc | polipeptídeo imunogênico isolado e seu uso, composição imunogênica e seu uso, célula recombinante ou progênie da mesma, e método de produção de uma toxina de clostridium difficile mutante |
| US8758772B2 (en) | 2011-11-04 | 2014-06-24 | Abaxis, Inc. | Peptides and methods for the detection of lyme disease antibodies |
| BR122016023101B1 (pt) | 2012-10-21 | 2022-03-22 | Pfizer Inc | Polipeptídeo, composição imunogênica que o compreende, bem como célula recombinante derivada de clostridium difficile |
| KR102451333B1 (ko) * | 2018-10-22 | 2022-10-06 | 주식회사 엘지화학 | 마이크로비드 및 그 제조방법 |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK590288D0 (da) | 1988-10-24 | 1988-10-24 | Symbicom Ab | Kemiske forbindelser |
| US4603112A (en) * | 1981-12-24 | 1986-07-29 | Health Research, Incorporated | Modified vaccinia virus |
| US4767622A (en) * | 1983-08-19 | 1988-08-30 | University Of Illinois | Method and materials for development of immunological responses protective against malarial infection |
| US4601903A (en) * | 1985-05-01 | 1986-07-22 | The United States Of America As Represented By The Department Of Health And Human Services | Vaccine against Neisseria meningitidis Group B serotype 2 invasive disease |
| US4888276A (en) * | 1986-06-26 | 1989-12-19 | Minnesota Mining And Manufacturing Company | Method and composition for the diagnosis of Lyme disease |
| US4721617A (en) | 1986-08-14 | 1988-01-26 | Regents Of The University Of Minnesota | Vaccine against lyme disease |
| US5192540A (en) * | 1988-04-19 | 1993-03-09 | American Cyanamid Company | Haemophilus influenzae type b oxidized polysaccharide-outer membrane protein conjugate vaccine |
| DE3818013A1 (de) | 1988-05-27 | 1989-11-30 | Henkel Kgaa | Gewebeweichmachungsmittel |
| IT1223777B (it) * | 1988-08-18 | 1990-09-29 | Gevipi Ag | Rubinetto a due uscite con inversore a depressione |
| DE4015911A1 (de) * | 1989-09-19 | 1991-03-28 | Max Planck Gesellschaft | Impfstoff gegen die lyme-krankheit |
| DE3942728C1 (en) | 1989-12-22 | 1991-05-23 | Mikrogen Molekularbiologische Entwicklungs-Gmbh, 8000 Muenchen, De | New immunologically active proteins derived from Borelia burgdorferiensity polyethylene vessel and a high density polyethylene sealing cap - useful as vaccine and for quick accurate diagnosis of Borelia infections |
| AU7058691A (en) * | 1989-12-22 | 1991-07-24 | Mikrogen Molekularbiologische Entwicklungs-Gmbh | Immunologically active proteines from borrelia burgdorferi, related test kits and vaccine |
| ATE142888T1 (de) | 1990-03-05 | 1996-10-15 | Us Health | Antigen-wirkende proteine von borrelia burgdorferi |
| EP1016416A3 (fr) * | 1990-07-06 | 2002-10-23 | Wyeth | Vaccin contre la maladie de lyme et modèle pour l'évaluation de l'efficacité du vaccin |
-
1992
- 1992-06-25 US US07/903,580 patent/US6221363B1/en not_active Expired - Lifetime
- 1992-07-01 AU AU19349/92A patent/AU660178B2/en not_active Ceased
- 1992-07-08 CA CA002073486A patent/CA2073486C/fr not_active Expired - Fee Related
- 1992-07-09 DK DK92111713T patent/DK0522560T4/da active
- 1992-07-09 AT AT92111713T patent/ATE198489T1/de not_active IP Right Cessation
- 1992-07-09 ES ES92111713T patent/ES2154633T3/es not_active Expired - Lifetime
- 1992-07-09 FI FI923175A patent/FI107334B/fi not_active IP Right Cessation
- 1992-07-09 DE DE69231619T patent/DE69231619T3/de not_active Expired - Fee Related
- 1992-07-09 EP EP92111713A patent/EP0522560B2/fr not_active Expired - Lifetime
- 1992-07-10 HU HU9202289A patent/HU219772B/hu not_active IP Right Cessation
- 1992-07-10 SI SI9200143A patent/SI9200143B/sl not_active IP Right Cessation
- 1992-07-10 MX MX9204078A patent/MX9204078A/es unknown
- 1992-07-10 SK SK2172-92A patent/SK217292A3/sk unknown
- 1992-07-10 JP JP4207392A patent/JP2611095B2/ja not_active Expired - Fee Related
- 1992-07-10 CZ CS922172A patent/CZ280743B6/cs not_active IP Right Cessation
- 1992-07-10 NO NO922746A patent/NO304546B1/no not_active IP Right Cessation
-
1993
- 1993-03-12 US US08/031,295 patent/US5530103A/en not_active Expired - Lifetime
-
1995
- 1995-03-30 HR HR950174A patent/HRP950174B1/xx not_active IP Right Cessation
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO304546B1 (no) | Preparat omfattende et immunogen i form av B. burgdorferi-pC-polypeptider, for immunisering av et pattedyr mot Lymeborreliose, samt anvendelse av preparat for fremstilling av et farmas°ytisk preparat for behandling av Lyme-borreliose | |
| US7179448B2 (en) | Recombinant constructs of Borrelia burgdorferi | |
| Akins et al. | Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity | |
| Simon et al. | Recombinant outer surface protein A from Borrelia burgdorferi induces antibodies protective against spirochetal infection in mice | |
| Probert et al. | Identification and characterization of a surface-exposed, 66-kilodalton protein from Borrelia burgdorferi | |
| EP3609911B1 (fr) | Polypeptides ospa multivalents, procédés et utilisations associés | |
| AU2015205520B2 (en) | Mutant fragments of OspA and methods and uses relating thereto | |
| EP1311682B1 (fr) | Constructions recombinantes de borrelia burgdorferi | |
| US5807685A (en) | OspE, OspF, and S1 polypeptides in Borrelia burgdorferi | |
| AU644829B2 (en) | Recombinant vaccine for porcine pleuropneumonia | |
| Swancutt et al. | Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum | |
| Cullen et al. | Construction and evaluation of a plasmid vector for the expression of recombinant lipoproteins in Escherichia coli | |
| Moses et al. | A multiple site‐specific DNA‐inversion model for the control of Ompi phase and antigenic variation in Dichelobacter nodosus | |
| Champion et al. | Sequence analysis and recombinant expression of a 28-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp2) | |
| RU2102081C1 (ru) | Иммуногенная композиция против боррелиоза лайма, способ иммунизации млекопитающего против боррелиоза лайма, способ получения белка pc borrelia burgdorferi, диагностический агент для обнаружения b.burgdorferi и способ обнаружения антител к b.burgdorferi | |
| Redchuk et al. | Expression of Mycobacterium tuberculosis proteins MPT63 and MPT83 as a fusion: purification, refolding and immunological characterization | |
| EP1939294A1 (fr) | Structures recombinantes de borrelia burgdorferi | |
| WO2007081938A2 (fr) | Utilisation d'une proteine de membrane externe plpe de mannheimia haemolytica chimere et d'epitopes de la leucotoxine comme vaccin ou composant de vaccin contre la fievre des transports | |
| US6248583B1 (en) | Chromosomally-encoded membrane protein of borrelia burgdorferi | |
| against Infection | Active and Passive Immunity against | |
| MXPA97001224A (en) | Vaccines against borrelia burgdorferi o |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |