AU2012311428A1 - Peptide or arrangement of peptides forming a Staphylococcus aureus epitope binding site - Google Patents
Peptide or arrangement of peptides forming a Staphylococcus aureus epitope binding site Download PDFInfo
- Publication number
- AU2012311428A1 AU2012311428A1 AU2012311428A AU2012311428A AU2012311428A1 AU 2012311428 A1 AU2012311428 A1 AU 2012311428A1 AU 2012311428 A AU2012311428 A AU 2012311428A AU 2012311428 A AU2012311428 A AU 2012311428A AU 2012311428 A1 AU2012311428 A1 AU 2012311428A1
- Authority
- AU
- Australia
- Prior art keywords
- peptide
- arrangement
- peptides
- infection
- antibody
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 108
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 54
- 230000027455 binding Effects 0.000 title claims abstract description 29
- 238000009739 binding Methods 0.000 title claims abstract description 29
- 241000191967 Staphylococcus aureus Species 0.000 title claims abstract description 15
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 27
- 208000015181 infectious disease Diseases 0.000 claims description 28
- 210000004027 cell Anatomy 0.000 claims description 22
- 210000004369 blood Anatomy 0.000 claims description 19
- 239000008280 blood Substances 0.000 claims description 19
- 241001465754 Metazoa Species 0.000 claims description 18
- 239000012634 fragment Substances 0.000 claims description 17
- 238000000034 method Methods 0.000 claims description 15
- 239000003814 drug Substances 0.000 claims description 13
- 238000011282 treatment Methods 0.000 claims description 11
- 206010040047 Sepsis Diseases 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 10
- RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 claims description 9
- 229960003085 meticillin Drugs 0.000 claims description 9
- 208000031729 Bacteremia Diseases 0.000 claims description 6
- 150000001413 amino acids Chemical class 0.000 claims description 6
- 208000037815 bloodstream infection Diseases 0.000 claims description 6
- 238000000502 dialysis Methods 0.000 claims description 6
- 208000004396 mastitis Diseases 0.000 claims description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 5
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 5
- 241000124008 Mammalia Species 0.000 claims description 5
- 230000003115 biocidal effect Effects 0.000 claims description 5
- 206010031252 Osteomyelitis Diseases 0.000 claims description 4
- 206010035664 Pneumonia Diseases 0.000 claims description 4
- 206010062255 Soft tissue infection Diseases 0.000 claims description 4
- 238000001514 detection method Methods 0.000 claims description 4
- 210000004962 mammalian cell Anatomy 0.000 claims description 4
- 238000001356 surgical procedure Methods 0.000 claims description 4
- 241000699802 Cricetulus griseus Species 0.000 claims description 3
- 206010056559 Graft infection Diseases 0.000 claims description 3
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 claims description 3
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 claims description 3
- 210000004408 hybridoma Anatomy 0.000 claims description 3
- 210000001672 ovary Anatomy 0.000 claims description 3
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 2
- 230000009885 systemic effect Effects 0.000 claims description 2
- 241001478240 Coccus Species 0.000 claims 1
- HWGBHCRJGXAGEU-UHFFFAOYSA-N Methylthiouracil Chemical compound CC1=CC(=O)NC(=S)N1 HWGBHCRJGXAGEU-UHFFFAOYSA-N 0.000 claims 1
- 241000191940 Staphylococcus Species 0.000 claims 1
- CSHFHJNMIMPJST-HOTGVXAUSA-N methyl (2s)-2-[[(2s)-2-[[2-[(2-aminoacetyl)amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoate Chemical compound NCC(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)OC)CC1=CC=CC=C1 CSHFHJNMIMPJST-HOTGVXAUSA-N 0.000 claims 1
- 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 abstract 1
- 241000894006 Bacteria Species 0.000 description 29
- 230000002147 killing effect Effects 0.000 description 18
- 206010057249 Phagocytosis Diseases 0.000 description 13
- 230000008782 phagocytosis Effects 0.000 description 13
- 238000002965 ELISA Methods 0.000 description 12
- 210000000601 blood cell Anatomy 0.000 description 12
- 239000000243 solution Substances 0.000 description 9
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 8
- 241000283690 Bos taurus Species 0.000 description 6
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- 235000020183 skimmed milk Nutrition 0.000 description 6
- 238000005415 bioluminescence Methods 0.000 description 5
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- 230000003287 optical effect Effects 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 238000010494 dissociation reaction Methods 0.000 description 3
- 230000005593 dissociations Effects 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
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- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 239000000523 sample Substances 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 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 239000012124 Opti-MEM Substances 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
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- 230000000903 blocking effect Effects 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
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- 239000013642 negative control Substances 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 2
- 229930182490 saponin Natural products 0.000 description 2
- 150000007949 saponins Chemical class 0.000 description 2
- 238000013207 serial dilution Methods 0.000 description 2
- 238000011895 specific detection Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- 208000031462 Bovine Mastitis Diseases 0.000 description 1
- 240000001546 Byrsonima crassifolia Species 0.000 description 1
- 235000003197 Byrsonima crassifolia Nutrition 0.000 description 1
- 241000543381 Cliftonia monophylla Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101100114416 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) con-10 gene Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 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
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 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 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 230000000625 opsonophagocytic effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000000242 pagocytic effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 230000019254 respiratory burst Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1271—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Micrococcaceae (F), e.g. Staphylococcus
-
- 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
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
- A61P15/14—Drugs for genital or sexual disorders; Contraceptives for lactation disorders, e.g. galactorrhoea
-
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56911—Bacteria
- G01N33/56938—Staphylococcus
-
- 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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1214—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Pseudomonadaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/77—Internalization into the cell
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Virology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Tropical Medicine & Parasitology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Gynecology & Obstetrics (AREA)
- Pregnancy & Childbirth (AREA)
- Endocrinology (AREA)
- Reproductive Health (AREA)
- Pulmonology (AREA)
- Oncology (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP11182598.0 | 2011-09-23 | ||
| EP11182598 | 2011-09-23 | ||
| US201161545763P | 2011-10-11 | 2011-10-11 | |
| US61/545,763 | 2011-10-11 | ||
| PCT/EP2012/068703 WO2013041707A1 (en) | 2011-09-23 | 2012-09-21 | Peptide or arrangement of peptides forming a staphylococcus aureus epitope binding site |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2012311428A1 true AU2012311428A1 (en) | 2014-04-24 |
| AU2012311428A2 AU2012311428A2 (en) | 2014-06-26 |
Family
ID=47913924
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2012311428A Abandoned AU2012311428A1 (en) | 2011-09-23 | 2012-09-21 | Peptide or arrangement of peptides forming a Staphylococcus aureus epitope binding site |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US9422365B2 (enExample) |
| EP (1) | EP2758431A1 (enExample) |
| JP (1) | JP2014534169A (enExample) |
| CN (1) | CN103857697A (enExample) |
| AU (1) | AU2012311428A1 (enExample) |
| WO (1) | WO2013041707A1 (enExample) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2616728T3 (es) | 2008-05-23 | 2017-06-14 | Siwa Corporation | Procedimientos y composiciones para facilitar la regeneración |
| US8721571B2 (en) | 2010-11-22 | 2014-05-13 | Siwa Corporation | Selective removal of cells having accumulated agents |
| US9944694B2 (en) * | 2013-12-13 | 2018-04-17 | Rijksuniversiteit Groningen | Antibodies against Staphylococcus aureus and uses therof |
| IL251210B2 (en) | 2014-09-19 | 2023-12-01 | Siwa Corp | Anti-aging antibodies for the treatment of inflammation and autoimmune disorders |
| US9993535B2 (en) | 2014-12-18 | 2018-06-12 | Siwa Corporation | Method and composition for treating sarcopenia |
| US10358502B2 (en) | 2014-12-18 | 2019-07-23 | Siwa Corporation | Product and method for treating sarcopenia |
| CN109071675A (zh) | 2016-02-19 | 2018-12-21 | Siwa有限公司 | 使用高级糖化终产物(age)的抗体治疗癌症、杀死转移性癌细胞和预防癌症转移的方法和组合物 |
| CA3057829A1 (en) | 2016-04-15 | 2017-10-19 | Siwa Corporation | Anti-age antibodies for treating neurodegenerative disorders |
| EP3475306A1 (en) | 2016-06-23 | 2019-05-01 | Siwa Corporation | Vaccines for use in treating various diseases and disorders |
| US10858449B1 (en) * | 2017-01-06 | 2020-12-08 | Siwa Corporation | Methods and compositions for treating osteoarthritis |
| US10961321B1 (en) | 2017-01-06 | 2021-03-30 | Siwa Corporation | Methods and compositions for treating pain associated with inflammation |
| US10925937B1 (en) | 2017-01-06 | 2021-02-23 | Siwa Corporation | Vaccines for use in treating juvenile disorders associated with inflammation |
| US10995151B1 (en) * | 2017-01-06 | 2021-05-04 | Siwa Corporation | Methods and compositions for treating disease-related cachexia |
| US10919957B2 (en) | 2017-04-13 | 2021-02-16 | Siwa Corporation | Humanized monoclonal advanced glycation end-product antibody |
| US11518801B1 (en) | 2017-12-22 | 2022-12-06 | Siwa Corporation | Methods and compositions for treating diabetes and diabetic complications |
| CN109021109A (zh) * | 2018-07-20 | 2018-12-18 | 上海交通大学 | 一种牛源性抗金黄色葡萄球菌融合抗体scFv-Fc及其制备方法 |
| CN119431528B (zh) * | 2024-10-28 | 2025-10-14 | 中国人民解放军陆军军医大学 | 一种金黄色葡萄球菌毒素LukG抗原表位肽及其应用 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR0207068A (pt) | 2001-01-26 | 2004-12-21 | Inhibitex Inc | Anticorpo monoclonal para a protéina clfa, anti-soro isolado, anticorpo isolado e anticorpo humanizado contendo o referido anticorpo, kit diagnóstico compreendendo o referido anticorpo, método para diagnóstico de uma infecção por s.aureus, composição farmacêutica para o tratamento ou prevenção da referida infecção, método para indução de de uma resposta imunológica, método para identificação de anticorpos monoclonais para a protéina clfa e fragmento ativo isolado a partir do domìnio a da protéina clfa do s.aureus |
| JP2009031009A (ja) * | 2007-07-24 | 2009-02-12 | St Marianna Univ School Of Medicine | 黄色ブドウ球菌の検出または同定方法および検出キット |
| JP5882892B2 (ja) * | 2009-05-18 | 2016-03-09 | ユリウス・マクシミリアンス−ウニヴェルジテート・ヴュルツブルクＪｕｌｉｕｓ Ｍａｘｉｍｉｌｉａｎｓ−Ｕｎｉｖｅｒｓｉｔａｅｔ Ｗｕｅｒｚｂｕｒｇ | 黄色ブドウ球菌エピトープＩｓａＡまたはＩｓａＢに対する抗体またはそれらのフラグメント |
-
2012
- 2012-09-21 WO PCT/EP2012/068703 patent/WO2013041707A1/en not_active Ceased
- 2012-09-21 AU AU2012311428A patent/AU2012311428A1/en not_active Abandoned
- 2012-09-21 EP EP12759781.3A patent/EP2758431A1/en not_active Withdrawn
- 2012-09-21 CN CN201280046452.2A patent/CN103857697A/zh active Pending
- 2012-09-21 US US14/346,435 patent/US9422365B2/en not_active Expired - Fee Related
- 2012-09-21 JP JP2014531256A patent/JP2014534169A/ja not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| CN103857697A (zh) | 2014-06-11 |
| WO2013041707A1 (en) | 2013-03-28 |
| EP2758431A1 (en) | 2014-07-30 |
| US9422365B2 (en) | 2016-08-23 |
| US20140234339A1 (en) | 2014-08-21 |
| JP2014534169A (ja) | 2014-12-18 |
| AU2012311428A2 (en) | 2014-06-26 |
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