AU2003203097C1 - Group B streptococcus antigen - Google Patents
Group B streptococcus antigen Download PDFInfo
- Publication number
- AU2003203097C1 AU2003203097C1 AU2003203097A AU2003203097A AU2003203097C1 AU 2003203097 C1 AU2003203097 C1 AU 2003203097C1 AU 2003203097 A AU2003203097 A AU 2003203097A AU 2003203097 A AU2003203097 A AU 2003203097A AU 2003203097 C1 AU2003203097 C1 AU 2003203097C1
- Authority
- AU
- Australia
- Prior art keywords
- polypeptide
- amino acid
- seq
- acid sequence
- polypeptides
- 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.)
- Ceased
Links
- 241000193990 Streptococcus sp. 'group B' Species 0.000 title claims abstract description 91
- 239000000427 antigen Substances 0.000 title claims description 24
- 108091007433 antigens Proteins 0.000 title claims description 24
- 102000036639 antigens Human genes 0.000 title claims description 24
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 304
- 229920001184 polypeptide Polymers 0.000 claims abstract description 303
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 302
- 239000012634 fragment Substances 0.000 claims description 59
- 108091033319 polynucleotide Proteins 0.000 claims description 56
- 102000040430 polynucleotide Human genes 0.000 claims description 56
- 239000002157 polynucleotide Substances 0.000 claims description 56
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 44
- 208000015181 infectious disease Diseases 0.000 claims description 40
- 238000000034 method Methods 0.000 claims description 32
- 239000000203 mixture Substances 0.000 claims description 18
- 239000008194 pharmaceutical composition Substances 0.000 claims description 18
- 239000013598 vector Substances 0.000 claims description 18
- 230000027455 binding Effects 0.000 claims description 17
- 241000282414 Homo sapiens Species 0.000 claims description 15
- 239000002671 adjuvant Substances 0.000 claims description 15
- 230000002163 immunogen Effects 0.000 claims description 14
- 238000011282 treatment Methods 0.000 claims description 14
- 239000012472 biological sample Substances 0.000 claims description 13
- 150000001413 amino acids Chemical class 0.000 claims description 12
- 230000014509 gene expression Effects 0.000 claims description 11
- 230000000069 prophylactic effect Effects 0.000 claims description 11
- 230000001225 therapeutic effect Effects 0.000 claims description 11
- 201000009906 Meningitis Diseases 0.000 claims description 10
- 230000000295 complement effect Effects 0.000 claims description 9
- 238000011321 prophylaxis Methods 0.000 claims description 9
- 206010007882 Cellulitis Diseases 0.000 claims description 7
- 241001465754 Metazoa Species 0.000 claims description 7
- 206010031252 Osteomyelitis Diseases 0.000 claims description 7
- 206010040047 Sepsis Diseases 0.000 claims description 7
- 206010014665 endocarditis Diseases 0.000 claims description 7
- 230000028993 immune response Effects 0.000 claims description 6
- 125000003729 nucleotide group Chemical group 0.000 claims description 6
- 206010053555 Arthritis bacterial Diseases 0.000 claims description 5
- 208000004575 Infectious Arthritis Diseases 0.000 claims description 5
- 206010035664 Pneumonia Diseases 0.000 claims description 5
- 238000001514 detection method Methods 0.000 claims description 5
- 239000003085 diluting agent Substances 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 239000002773 nucleotide Substances 0.000 claims description 5
- 201000001223 septic arthritis Diseases 0.000 claims description 5
- 230000001939 inductive effect Effects 0.000 claims description 3
- 108010078791 Carrier Proteins Proteins 0.000 claims description 2
- 102000014914 Carrier Proteins Human genes 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 239000003937 drug carrier Substances 0.000 claims 2
- 240000007594 Oryza sativa Species 0.000 claims 1
- 235000007164 Oryza sativa Nutrition 0.000 claims 1
- 208000001606 epiglottitis Diseases 0.000 claims 1
- 235000009566 rice Nutrition 0.000 claims 1
- 206010061372 Streptococcal infection Diseases 0.000 abstract description 10
- 241000193985 Streptococcus agalactiae Species 0.000 abstract description 4
- 241000194017 Streptococcus Species 0.000 description 38
- 210000004027 cell Anatomy 0.000 description 37
- 108090000623 proteins and genes Proteins 0.000 description 35
- 241000699670 Mus sp. Species 0.000 description 24
- 108091028043 Nucleic acid sequence Proteins 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 17
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 15
- 125000000539 amino acid group Chemical group 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 230000004048 modification Effects 0.000 description 13
- 238000012986 modification Methods 0.000 description 13
- 229960005486 vaccine Drugs 0.000 description 13
- 230000003053 immunization Effects 0.000 description 12
- 238000002649 immunization Methods 0.000 description 12
- 230000000890 antigenic effect Effects 0.000 description 11
- 235000001014 amino acid Nutrition 0.000 description 10
- 210000002966 serum Anatomy 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 238000003752 polymerase chain reaction Methods 0.000 description 9
- 238000006467 substitution reaction Methods 0.000 description 9
- 230000004927 fusion Effects 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 7
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 7
- 230000001580 bacterial effect Effects 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 239000002953 phosphate buffered saline Substances 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 230000004083 survival effect Effects 0.000 description 7
- 239000000872 buffer Substances 0.000 description 6
- 201000010099 disease Diseases 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 230000013595 glycosylation Effects 0.000 description 6
- 230000003248 secreting effect Effects 0.000 description 6
- 239000003298 DNA probe Substances 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- 241001644525 Nastus productus Species 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 210000004899 c-terminal region Anatomy 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 230000001681 protective effect Effects 0.000 description 5
- 230000009257 reactivity Effects 0.000 description 5
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 206010062255 Soft tissue infection Diseases 0.000 description 4
- 206010048038 Wound infection Diseases 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 238000002405 diagnostic procedure Methods 0.000 description 4
- 238000005755 formation reaction Methods 0.000 description 4
- 150000004676 glycans Chemical class 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 210000004408 hybridoma Anatomy 0.000 description 4
- 238000003119 immunoblot Methods 0.000 description 4
- 229930182817 methionine Natural products 0.000 description 4
- 238000010369 molecular cloning Methods 0.000 description 4
- 229920001282 polysaccharide Polymers 0.000 description 4
- 239000005017 polysaccharide Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 101710117545 C protein Proteins 0.000 description 3
- 208000004145 Endometritis Diseases 0.000 description 3
- 238000000729 Fisher's exact test Methods 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 239000002202 Polyethylene glycol Substances 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 230000009435 amidation Effects 0.000 description 3
- 238000007112 amidation reaction Methods 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 235000013365 dairy product Nutrition 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 231100000517 death Toxicity 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 244000144980 herd Species 0.000 description 3
- 230000036039 immunity Effects 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
- 238000002372 labelling Methods 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 238000010172 mouse model Methods 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 230000035935 pregnancy Effects 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000012552 review Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 230000005730 ADP ribosylation Effects 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 208000031729 Bacteremia Diseases 0.000 description 2
- 108020003215 DNA Probes Proteins 0.000 description 2
- 239000003155 DNA primer Substances 0.000 description 2
- 206010014568 Empyema Diseases 0.000 description 2
- 206010016228 Fasciitis Diseases 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 2
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 238000012181 QIAquick gel extraction kit Methods 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 208000025865 Ulcer Diseases 0.000 description 2
- 206010048709 Urosepsis Diseases 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000010933 acylation Effects 0.000 description 2
- 238000005917 acylation reaction Methods 0.000 description 2
- 238000010171 animal model Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 230000021615 conjugation Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 239000002552 dosage form Substances 0.000 description 2
- 210000002409 epiglottis Anatomy 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 230000006251 gamma-carboxylation Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000033444 hydroxylation Effects 0.000 description 2
- 238000005805 hydroxylation reaction Methods 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 231100000518 lethal Toxicity 0.000 description 2
- 230000001665 lethal effect Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 208000004396 mastitis Diseases 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 230000002093 peripheral effect Effects 0.000 description 2
- 206010034674 peritonitis Diseases 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 239000013615 primer Substances 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 230000019635 sulfation Effects 0.000 description 2
- 238000005670 sulfation reaction Methods 0.000 description 2
- -1 synthetic multimers) Polymers 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- 230000034512 ubiquitination Effects 0.000 description 2
- 238000010798 ubiquitination Methods 0.000 description 2
- 231100000397 ulcer Toxicity 0.000 description 2
- 208000019206 urinary tract infection Diseases 0.000 description 2
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- DEXFNLNNUZKHNO-UHFFFAOYSA-N 6-[3-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperidin-1-yl]-3-oxopropyl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C1CCN(CC1)C(CCC1=CC2=C(NC(O2)=O)C=C1)=O DEXFNLNNUZKHNO-UHFFFAOYSA-N 0.000 description 1
- HBAQYPYDRFILMT-UHFFFAOYSA-N 8-[3-(1-cyclopropylpyrazol-4-yl)-1H-pyrazolo[4,3-d]pyrimidin-5-yl]-3-methyl-3,8-diazabicyclo[3.2.1]octan-2-one Chemical class C1(CC1)N1N=CC(=C1)C1=NNC2=C1N=C(N=C2)N1C2C(N(CC1CC2)C)=O HBAQYPYDRFILMT-UHFFFAOYSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 229910018626 Al(OH) Inorganic materials 0.000 description 1
- 229910017119 AlPO Inorganic materials 0.000 description 1
- 239000005995 Aluminium silicate Substances 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- 101710197658 Capsid protein VP1 Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 208000017667 Chronic Disease Diseases 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 102000008130 Cyclic AMP-Dependent Protein Kinases Human genes 0.000 description 1
- 108010049894 Cyclic AMP-Dependent Protein Kinases Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 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 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 206010058780 Meningitis neonatal Diseases 0.000 description 1
- PYUSHNKNPOHWEZ-YFKPBYRVSA-N N-formyl-L-methionine Chemical compound CSCC[C@@H](C(O)=O)NC=O PYUSHNKNPOHWEZ-YFKPBYRVSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 241001460678 Napo <wasp> Species 0.000 description 1
- 208000006816 Neonatal Sepsis Diseases 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 241000187654 Nocardia Species 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 description 1
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 208000000474 Poliomyelitis Diseases 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 1
- 101710118046 RNA-directed RNA polymerase Proteins 0.000 description 1
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 101000874347 Streptococcus agalactiae IgA FC receptor Proteins 0.000 description 1
- 241000194042 Streptococcus dysgalactiae Species 0.000 description 1
- 241000193996 Streptococcus pyogenes Species 0.000 description 1
- 241001505901 Streptococcus sp. 'group A' Species 0.000 description 1
- 241000194054 Streptococcus uberis Species 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 101710137500 T7 RNA polymerase Proteins 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 108020004566 Transfer RNA Proteins 0.000 description 1
- 101710108545 Viral protein 1 Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 235000012211 aluminium silicate Nutrition 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 230000010516 arginylation Effects 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000006161 blood agar Substances 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 1
- 229960003669 carbenicillin Drugs 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 208000035850 clinical syndrome Diseases 0.000 description 1
- 230000000112 colonic effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000002716 delivery method Methods 0.000 description 1
- 230000017858 demethylation Effects 0.000 description 1
- 238000010520 demethylation reaction Methods 0.000 description 1
- 101150106284 deoR gene Proteins 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 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 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000022244 formylation Effects 0.000 description 1
- 238000006170 formylation reaction Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 230000001279 glycosylating effect Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 101150023479 hsdS gene Proteins 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- NLYAJNPCOHFWQQ-UHFFFAOYSA-N kaolin Chemical compound O.O.O=[Al]O[Si](=O)O[Si](=O)O[Al]=O NLYAJNPCOHFWQQ-UHFFFAOYSA-N 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 125000005647 linker group Chemical group 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 238000001325 log-rank test Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 239000002184 metal 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
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 230000007498 myristoylation Effects 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000007764 o/w emulsion Substances 0.000 description 1
- 101150093139 ompT gene Proteins 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 101150009573 phoA gene Proteins 0.000 description 1
- 101150022503 phoR gene Proteins 0.000 description 1
- 150000003905 phosphatidylinositols Chemical class 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 229940043131 pyroglutamate Drugs 0.000 description 1
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 1
- 238000011555 rabbit model Methods 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- ZZIZZTHXZRDOFM-XFULWGLBSA-N tamsulosin hydrochloride Chemical compound [H+].[Cl-].CCOC1=CC=CC=C1OCCN[C@H](C)CC1=CC=C(OC)C(S(N)(=O)=O)=C1 ZZIZZTHXZRDOFM-XFULWGLBSA-N 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 125000004149 thio group Chemical group *S* 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000001296 transplacental effect Effects 0.000 description 1
- 101150057627 trxB gene Proteins 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 229940124856 vaccine component Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000012138 yeast extract 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
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- 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)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (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)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Physical Education & Sports Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Rheumatology (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Pulmonology (AREA)
- Oncology (AREA)
- Pain & Pain Management (AREA)
- Communicable Diseases (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Dermatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (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 |
|---|---|---|---|
| US35494702P | 2002-02-11 | 2002-02-11 | |
| US60/354,947 | 2002-02-11 | ||
| PCT/CA2003/000186 WO2003068813A2 (en) | 2002-02-11 | 2003-02-11 | Group b streptococcus antigen |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| AU2003203097A1 AU2003203097A1 (en) | 2003-09-04 |
| AU2003203097B2 AU2003203097B2 (en) | 2009-10-01 |
| AU2003203097C1 true AU2003203097C1 (en) | 2010-02-04 |
Family
ID=27734441
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2003203097A Ceased AU2003203097C1 (en) | 2002-02-11 | 2003-02-11 | Group B streptococcus antigen |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US20070275004A1 (https=) |
| EP (1) | EP1472353B1 (https=) |
| JP (1) | JP2005535287A (https=) |
| AT (1) | ATE543906T1 (https=) |
| AU (1) | AU2003203097C1 (https=) |
| CA (1) | CA2475821C (https=) |
| ES (1) | ES2381967T3 (https=) |
| WO (1) | WO2003068813A2 (https=) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2540281T3 (es) | 1998-02-20 | 2015-07-09 | Id Biomedical Corporation Of Quebec | Antígenos de estreptococos del grupo B |
| DK1328543T3 (da) | 2000-10-27 | 2009-11-23 | Novartis Vaccines & Diagnostic | Nukleinsyrer og proteiner fra streptococcus-gruppe A & B |
| JP4875490B2 (ja) | 2003-07-31 | 2012-02-15 | ノバルティス バクシンズ アンド ダイアグノスティックス，インコーポレーテッド | ＳｔｒｅｐｔｏｃｏｃｃｕｓＰｙｏｇｅｎｅｓについての免疫原組成物 |
| US8945589B2 (en) | 2003-09-15 | 2015-02-03 | Novartis Vaccines And Diagnostics, Srl | Immunogenic compositions for Streptococcus agalactiae |
| EP1784211A4 (en) | 2004-07-29 | 2010-06-30 | Novartis Vaccines & Diagnostic | IMMUNOGENIC COMPOSITIONS FOR GRAMPOSITIVE BACTERIA SUCH AS STREPTOCOCCUS AGALACTIAE |
| WO2006086330A2 (en) * | 2005-02-08 | 2006-08-17 | Id Biomedical Corporation Of Quebec C.O.B. As Glaxosmithkline Biologicals North America | Pharmaceutical compositions |
| ES2310062B1 (es) * | 2005-07-15 | 2009-11-13 | Bionostra, S.L. | Particulas pseudovirales vacias quimericas derivadas del virus causante de la enfermedad de la bursitis infecciosa (ibdv), procedimiento de obtencion y aplicaciones. |
| CA2699513C (en) | 2007-09-12 | 2018-03-13 | Novartis Ag | Gas57 mutant antigens and gas57 antibodies |
| CN103834669B (zh) * | 2014-02-21 | 2016-06-29 | 通威股份有限公司 | 一种无乳链球菌的口服疫苗及其制备方法 |
| CN107502622A (zh) * | 2016-06-14 | 2017-12-22 | 广东省农业科学院动物卫生研究所 | Sip基因重组载体、壳聚糖‑PLGA包裹Sip基因DNA疫苗及其制备方法和应用 |
| CA3268712A1 (en) * | 2018-06-13 | 2025-10-14 | Gen-Probe Incorporated | Compositions and Methods for Detecting Group B Streptococcus Nucleic Acid |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999042588A2 (en) * | 1998-02-20 | 1999-08-26 | Biochem Pharma Inc. | Group b streptococcus antigens |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5302386A (en) * | 1986-04-16 | 1994-04-12 | Brigham And Women's Hospital, Inc. | Bacterial antigens, antibodies, vaccines and methods of manufacture |
| US5472696A (en) * | 1988-02-26 | 1995-12-05 | Univ. Of Florida Research Foundation, Inc. | Antigen of group B streptococci |
| US5648241A (en) * | 1989-09-15 | 1997-07-15 | The General Hospital Corporation | Conjugate vaccine against group B streptococcus |
| US5679768A (en) * | 1991-02-15 | 1997-10-21 | Uab Research Foundation | Epitopic regions of pneumococcal surface protein A |
| US5225331A (en) * | 1991-04-25 | 1993-07-06 | National Research Council Of Canada | Immunoassay for detecting group b streptococcus |
| DK0656014T3 (da) * | 1993-03-19 | 2003-08-11 | Gunnar Lindahl | Protein Rib, et celleoverfladeprotein der overfører immunitet mod mange gruppe B Streptococcus stammer, fremgangsmåde til oprensning af proteinet, reagenskit og farmaceutisk komposition |
| US5595740A (en) * | 1994-05-16 | 1997-01-21 | University Of Florida | Cloning of non-IgA FC binding forms of the group B streptococcal beta antigens |
| CN1142229A (zh) * | 1994-11-01 | 1997-02-05 | 麒麟麦酒株式会社 | 形成粘蛋白糖链的肽序列和修饰蛋白质使与粘蛋白糖链相连的方法 |
| GB9921125D0 (en) * | 1999-09-07 | 1999-11-10 | Microbial Technics Limited | Proteins |
-
2003
- 2003-02-11 AT AT03701402T patent/ATE543906T1/de active
- 2003-02-11 CA CA2475821A patent/CA2475821C/en not_active Expired - Fee Related
- 2003-02-11 JP JP2003567939A patent/JP2005535287A/ja active Pending
- 2003-02-11 EP EP03701402A patent/EP1472353B1/en not_active Expired - Lifetime
- 2003-02-11 US US10/504,191 patent/US20070275004A1/en not_active Abandoned
- 2003-02-11 ES ES03701402T patent/ES2381967T3/es not_active Expired - Lifetime
- 2003-02-11 WO PCT/CA2003/000186 patent/WO2003068813A2/en not_active Ceased
- 2003-02-11 AU AU2003203097A patent/AU2003203097C1/en not_active Ceased
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999042588A2 (en) * | 1998-02-20 | 1999-08-26 | Biochem Pharma Inc. | Group b streptococcus antigens |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2003068813A3 (en) | 2003-10-16 |
| EP1472353A2 (en) | 2004-11-03 |
| CA2475821C (en) | 2011-12-13 |
| EP1472353B1 (en) | 2012-02-01 |
| AU2003203097A1 (en) | 2003-09-04 |
| ATE543906T1 (de) | 2012-02-15 |
| CA2475821A1 (en) | 2003-08-21 |
| ES2381967T3 (es) | 2012-06-04 |
| AU2003203097B2 (en) | 2009-10-01 |
| JP2005535287A (ja) | 2005-11-24 |
| US20070275004A1 (en) | 2007-11-29 |
| WO2003068813A2 (en) | 2003-08-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7262024B2 (en) | Streptococcus antigens | |
| EP2281891A2 (en) | Streptococcus antigens | |
| AU2003203097C1 (en) | Group B streptococcus antigen | |
| US7740870B2 (en) | Group B Streptococcus antigens and corresponding DNA fragments | |
| US20060177465A1 (en) | Streptococcus antigens | |
| US20080227706A1 (en) | Bvh-a2 and bvh-a3 antigens of group b streptococcus | |
| AU2002317107A1 (en) | Group B streptococcus antigens and corresponding DNA fragments | |
| EP1660660B1 (en) | Pharmaceutical compositions for use in the treatment of Streptococcus Pyogenes infection | |
| US20040171113A1 (en) | Antigens of group b streptococcus and corresponding dna fragments |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PC1 | Assignment before grant (sect. 113) |
Owner name: ID BIOMEDICAL CORPORATION Free format text: FORMER APPLICANT(S): SHIRE BIOCHEM INC |
|
| DA2 | Applications for amendment section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT( S) FILED 01 SEP 2009. |
|
| DA3 | Amendments made section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT(S) FILED 01 SEP 2009 |
|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |