RU2579900C2 - Очистка капсульных сахаридов staphylococcus aureus типа 5 и типа 8 - Google Patents
Очистка капсульных сахаридов staphylococcus aureus типа 5 и типа 8 Download PDFInfo
- Publication number
- RU2579900C2 RU2579900C2 RU2012122237/10A RU2012122237A RU2579900C2 RU 2579900 C2 RU2579900 C2 RU 2579900C2 RU 2012122237/10 A RU2012122237/10 A RU 2012122237/10A RU 2012122237 A RU2012122237 A RU 2012122237A RU 2579900 C2 RU2579900 C2 RU 2579900C2
- Authority
- RU
- Russia
- Prior art keywords
- antigen
- polysaccharide
- seq
- type
- aureus
- Prior art date
Links
- 238000000746 purification Methods 0.000 title abstract description 16
- 150000001720 carbohydrates Chemical class 0.000 title description 28
- 241000191967 Staphylococcus aureus Species 0.000 title description 4
- 150000004676 glycans Chemical class 0.000 claims abstract description 253
- 229920001282 polysaccharide Polymers 0.000 claims abstract description 253
- 239000005017 polysaccharide Substances 0.000 claims abstract description 253
- 238000000034 method Methods 0.000 claims abstract description 155
- 239000000203 mixture Substances 0.000 claims abstract description 70
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 63
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 61
- 239000012535 impurity Substances 0.000 claims abstract description 41
- 238000011282 treatment Methods 0.000 claims abstract description 35
- 238000005571 anion exchange chromatography Methods 0.000 claims abstract description 27
- 238000006640 acetylation reaction Methods 0.000 claims abstract description 26
- 238000002523 gelfiltration Methods 0.000 claims abstract description 24
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 claims abstract description 22
- 108010013639 Peptidoglycan Proteins 0.000 claims abstract description 22
- 238000011026 diafiltration Methods 0.000 claims abstract description 21
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 21
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 21
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 21
- 229960005486 vaccine Drugs 0.000 claims abstract description 19
- 108090000988 Lysostaphin Proteins 0.000 claims abstract description 16
- 238000010306 acid treatment Methods 0.000 claims abstract description 16
- 102000016911 Deoxyribonucleases Human genes 0.000 claims abstract description 14
- 108010053770 Deoxyribonucleases Proteins 0.000 claims abstract description 14
- 108010083644 Ribonucleases Proteins 0.000 claims abstract description 14
- 102000006382 Ribonucleases Human genes 0.000 claims abstract description 14
- 230000002378 acidificating effect Effects 0.000 claims abstract description 4
- 150000007524 organic acids Chemical class 0.000 claims abstract description 3
- 108091007433 antigens Proteins 0.000 claims description 304
- 102000036639 antigens Human genes 0.000 claims description 304
- 239000000427 antigen Substances 0.000 claims description 287
- 101150016690 esxA gene Proteins 0.000 claims description 35
- 101150079015 esxB gene Proteins 0.000 claims description 35
- 101150024289 hly gene Proteins 0.000 claims description 32
- 239000002253 acid Substances 0.000 claims description 19
- 238000012545 processing Methods 0.000 claims description 18
- 230000021615 conjugation Effects 0.000 claims description 16
- 101100455927 Mus musculus Maea gene Proteins 0.000 claims description 11
- 101150018857 emp gene Proteins 0.000 claims description 11
- 101100041727 Staphylococcus aureus (strain NCTC 8325 / PS 47) sasF gene Proteins 0.000 claims description 9
- 101150057984 isdB gene Proteins 0.000 claims description 9
- 101150026034 esxC gene Proteins 0.000 claims description 8
- 229920001542 oligosaccharide Polymers 0.000 claims description 8
- 150000002482 oligosaccharides Chemical class 0.000 claims description 8
- 101150064504 sdrC gene Proteins 0.000 claims description 8
- 101150009625 sdrD gene Proteins 0.000 claims description 8
- 101150085107 clfA gene Proteins 0.000 claims description 7
- 101150035844 clfB gene Proteins 0.000 claims description 7
- 238000001914 filtration Methods 0.000 claims description 7
- 101150116335 isdA gene Proteins 0.000 claims description 7
- 101150003115 isdC gene Proteins 0.000 claims description 7
- 108010009719 mutanolysin Proteins 0.000 claims description 7
- 239000006228 supernatant Substances 0.000 claims description 7
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 239000012736 aqueous medium Substances 0.000 claims description 2
- 238000011146 sterile filtration Methods 0.000 claims description 2
- 230000006037 cell lysis Effects 0.000 claims 1
- 238000006386 neutralization reaction Methods 0.000 claims 1
- 239000000126 substance Substances 0.000 abstract description 7
- 230000009089 cytolysis Effects 0.000 abstract description 3
- 230000000694 effects Effects 0.000 abstract description 3
- 238000000605 extraction Methods 0.000 abstract 1
- 150000001413 amino acids Chemical class 0.000 description 115
- 239000012634 fragment Substances 0.000 description 102
- 235000001014 amino acid Nutrition 0.000 description 76
- 229940024606 amino acid Drugs 0.000 description 74
- 235000018102 proteins Nutrition 0.000 description 60
- 210000004027 cell Anatomy 0.000 description 35
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 34
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 30
- 108090000765 processed proteins & peptides Proteins 0.000 description 29
- 102000004196 processed proteins & peptides Human genes 0.000 description 26
- 239000000872 buffer Substances 0.000 description 25
- 229920001184 polypeptide Polymers 0.000 description 24
- 241000282412 Homo Species 0.000 description 20
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 19
- 102000014914 Carrier Proteins Human genes 0.000 description 18
- 108020001580 protein domains Proteins 0.000 description 18
- 239000011780 sodium chloride Substances 0.000 description 18
- 239000002775 capsule Substances 0.000 description 17
- 108010078791 Carrier Proteins Proteins 0.000 description 16
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 15
- 230000001580 bacterial effect Effects 0.000 description 15
- 239000011347 resin Substances 0.000 description 15
- 229920005989 resin Polymers 0.000 description 15
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 14
- 239000012528 membrane Substances 0.000 description 13
- 239000000725 suspension Substances 0.000 description 13
- 238000005119 centrifugation Methods 0.000 description 12
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
- 238000006243 chemical reaction Methods 0.000 description 10
- 238000009295 crossflow filtration Methods 0.000 description 10
- 230000035772 mutation Effects 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 9
- 238000004587 chromatography analysis Methods 0.000 description 9
- 239000012153 distilled water Substances 0.000 description 9
- 238000003860 storage Methods 0.000 description 9
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 8
- 239000012141 concentrate Substances 0.000 description 8
- 230000002255 enzymatic effect Effects 0.000 description 8
- 239000000706 filtrate Substances 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 7
- 229920002271 DEAE-Sepharose Polymers 0.000 description 7
- 238000004108 freeze drying Methods 0.000 description 7
- 229940027941 immunoglobulin g Drugs 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 102000003839 Human Proteins Human genes 0.000 description 6
- 108090000144 Human Proteins Proteins 0.000 description 6
- 238000005481 NMR spectroscopy Methods 0.000 description 6
- 229960002885 histidine Drugs 0.000 description 6
- 230000007062 hydrolysis Effects 0.000 description 6
- 238000006460 hydrolysis reaction Methods 0.000 description 6
- 230000005847 immunogenicity Effects 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 5
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 5
- 241000872931 Myoporum sandwicense Species 0.000 description 5
- 241000588650 Neisseria meningitidis Species 0.000 description 5
- 201000005702 Pertussis Diseases 0.000 description 5
- 239000012506 Sephacryl® Substances 0.000 description 5
- 150000007513 acids Chemical class 0.000 description 5
- 238000000502 dialysis Methods 0.000 description 5
- 206010013023 diphtheria Diseases 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 239000008188 pellet Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 4
- 101710092462 Alpha-hemolysin Proteins 0.000 description 4
- 108010071134 CRM197 (non-toxic variant of diphtheria toxin) Proteins 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- GLUUGHFHXGJENI-UHFFFAOYSA-N Piperazine Chemical compound C1CNCCN1 GLUUGHFHXGJENI-UHFFFAOYSA-N 0.000 description 4
- 229920001218 Pullulan Polymers 0.000 description 4
- 239000004373 Pullulan Substances 0.000 description 4
- 206010043376 Tetanus Diseases 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 229940037003 alum Drugs 0.000 description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 239000000356 contaminant Substances 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
- 230000002163 immunogen Effects 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 235000019423 pullulan Nutrition 0.000 description 4
- 239000013049 sediment Substances 0.000 description 4
- 238000003756 stirring Methods 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- XFNJVJPLKCPIBV-UHFFFAOYSA-N trimethylenediamine Chemical compound NCCCN XFNJVJPLKCPIBV-UHFFFAOYSA-N 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- 241000606768 Haemophilus influenzae Species 0.000 description 3
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 3
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
- 229920005654 Sephadex Polymers 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 238000004140 cleaning Methods 0.000 description 3
- 230000006196 deacetylation Effects 0.000 description 3
- 238000003381 deacetylation reaction Methods 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 239000003480 eluent Substances 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 238000011068 loading method Methods 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 230000002572 peristaltic effect Effects 0.000 description 3
- 239000008194 pharmaceutical composition Substances 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000000425 proton nuclear magnetic resonance spectrum Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000012064 sodium phosphate buffer Substances 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 2
- PVOAHINGSUIXLS-UHFFFAOYSA-N 1-Methylpiperazine Chemical compound CN1CCNCC1 PVOAHINGSUIXLS-UHFFFAOYSA-N 0.000 description 2
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 2
- 101710197219 Alpha-toxin Proteins 0.000 description 2
- 239000007989 BIS-Tris Propane buffer Substances 0.000 description 2
- 241000588832 Bordetella pertussis Species 0.000 description 2
- 210000003771 C cell Anatomy 0.000 description 2
- 241000193163 Clostridioides difficile Species 0.000 description 2
- 108010060123 Conjugate Vaccines Proteins 0.000 description 2
- 108010016626 Dipeptides Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 229920002444 Exopolysaccharide Polymers 0.000 description 2
- 101710082714 Exotoxin A Proteins 0.000 description 2
- 101710154643 Filamentous hemagglutinin Proteins 0.000 description 2
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 125000003047 N-acetyl group Chemical group 0.000 description 2
- 108091005461 Nucleic proteins Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 101710124951 Phospholipase C Proteins 0.000 description 2
- NQRYJNQNLNOLGT-UHFFFAOYSA-N Piperidine Chemical compound C1CCNCC1 NQRYJNQNLNOLGT-UHFFFAOYSA-N 0.000 description 2
- 206010035664 Pneumonia Diseases 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 241000191963 Staphylococcus epidermidis Species 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 0.000 description 2
- 108010055044 Tetanus Toxin Proteins 0.000 description 2
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 230000004520 agglutination Effects 0.000 description 2
- 239000002776 alpha toxin Substances 0.000 description 2
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 2
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 2
- 238000005349 anion exchange Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 230000005540 biological transmission Effects 0.000 description 2
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 2
- HHKZCCWKTZRCCL-UHFFFAOYSA-N bis-tris propane Chemical compound OCC(CO)(CO)NCCCNC(CO)(CO)CO HHKZCCWKTZRCCL-UHFFFAOYSA-N 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 229940031670 conjugate vaccine Drugs 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- OOTFVKOQINZBBF-UHFFFAOYSA-N cystamine Chemical compound CCSSCCN OOTFVKOQINZBBF-UHFFFAOYSA-N 0.000 description 2
- 229940099500 cystamine Drugs 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 238000003795 desorption Methods 0.000 description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 230000029142 excretion Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 150000002243 furanoses Chemical group 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 235000011187 glycerol Nutrition 0.000 description 2
- 230000009931 harmful effect Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 239000007928 intraperitoneal injection Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- CRVGTESFCCXCTH-UHFFFAOYSA-N methyl diethanolamine Chemical compound OCCN(C)CCO CRVGTESFCCXCTH-UHFFFAOYSA-N 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 238000010397 one-hybrid screening Methods 0.000 description 2
- 230000003571 opsonizing effect Effects 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 108010094020 polyglycine Proteins 0.000 description 2
- 229920000232 polyglycine polymer Polymers 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 150000003214 pyranose derivatives Chemical class 0.000 description 2
- 238000010845 search algorithm Methods 0.000 description 2
- 238000004904 shortening Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N 2-Amino-2-Deoxy-Hexose Chemical compound NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 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 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 1
- 229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 1
- 102100030009 Azurocidin Human genes 0.000 description 1
- 101710154607 Azurocidin Proteins 0.000 description 1
- 108091008875 B cell receptors Proteins 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000222122 Candida albicans Species 0.000 description 1
- 241001647372 Chlamydia pneumoniae Species 0.000 description 1
- 241000606153 Chlamydia trachomatis Species 0.000 description 1
- 101000822677 Clostridium perfringens (strain 13 / Type A) Small, acid-soluble spore protein 1 Proteins 0.000 description 1
- 101000822695 Clostridium perfringens (strain 13 / Type A) Small, acid-soluble spore protein C1 Proteins 0.000 description 1
- 108090000056 Complement factor B Proteins 0.000 description 1
- 102000003712 Complement factor B Human genes 0.000 description 1
- 206010011409 Cross infection Diseases 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 102100037840 Dehydrogenase/reductase SDR family member 2, mitochondrial Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 241000194032 Enterococcus faecalis Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- BCCRXDTUTZHDEU-VKHMYHEASA-N Gly-Ser Chemical compound NCC(=O)N[C@@H](CO)C(O)=O BCCRXDTUTZHDEU-VKHMYHEASA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 1
- 108010004889 Heat-Shock Proteins Proteins 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 108010006464 Hemolysin Proteins Proteins 0.000 description 1
- 241000711549 Hepacivirus C Species 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 241000709721 Hepatovirus A Species 0.000 description 1
- 102000002268 Hexosaminidases Human genes 0.000 description 1
- 108010000540 Hexosaminidases Proteins 0.000 description 1
- NIKBMHGRNAPJFW-IUCAKERBSA-N His-Arg Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CN=CN1 NIKBMHGRNAPJFW-IUCAKERBSA-N 0.000 description 1
- 101100005713 Homo sapiens CD4 gene Proteins 0.000 description 1
- 108010028750 Integrin-Binding Sialoprotein Proteins 0.000 description 1
- 102000016921 Integrin-Binding Sialoprotein Human genes 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108010000851 Laminin Receptors Proteins 0.000 description 1
- 102000002297 Laminin Receptors Human genes 0.000 description 1
- 241000589242 Legionella pneumophila Species 0.000 description 1
- NFNVDJGXRFEYTK-YUMQZZPRSA-N Leu-Glu Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O NFNVDJGXRFEYTK-YUMQZZPRSA-N 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 241000186779 Listeria monocytogenes Species 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- CPLXHLVBOLITMK-UHFFFAOYSA-N Magnesium oxide Chemical compound [Mg]=O CPLXHLVBOLITMK-UHFFFAOYSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 201000005505 Measles Diseases 0.000 description 1
- WXHHTBVYQOSYSL-FXQIFTODSA-N Met-Ala-Ser Chemical compound CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O WXHHTBVYQOSYSL-FXQIFTODSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000588655 Moraxella catarrhalis Species 0.000 description 1
- 208000005647 Mumps Diseases 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 1
- 241000588652 Neisseria gonorrhoeae Species 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 102000008763 Neurofilament Proteins Human genes 0.000 description 1
- 108010088373 Neurofilament Proteins Proteins 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 101710116435 Outer membrane protein Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 208000002606 Paramyxoviridae Infections Diseases 0.000 description 1
- 108010081690 Pertussis Toxin Proteins 0.000 description 1
- 101710183389 Pneumolysin Proteins 0.000 description 1
- 208000000474 Poliomyelitis Diseases 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000605862 Porphyromonas gingivalis Species 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 101710188053 Protein D Proteins 0.000 description 1
- 101000576806 Protobothrops flavoviridis Small serum protein 1 Proteins 0.000 description 1
- 101000576807 Protobothrops flavoviridis Small serum protein 2 Proteins 0.000 description 1
- 101900161471 Pseudomonas aeruginosa Exotoxin A Proteins 0.000 description 1
- 108091030066 RNAIII Proteins 0.000 description 1
- 229940124875 RabAvert Drugs 0.000 description 1
- 206010037742 Rabies Diseases 0.000 description 1
- 101710132893 Resolvase Proteins 0.000 description 1
- 101100351057 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) PBP4 gene Proteins 0.000 description 1
- VBKBDLMWICBSCY-IMJSIDKUSA-N Ser-Asp Chemical compound OC[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O VBKBDLMWICBSCY-IMJSIDKUSA-N 0.000 description 1
- 102100027287 Serpin H1 Human genes 0.000 description 1
- 108050008290 Serpin H1 Proteins 0.000 description 1
- 101710084578 Short neurotoxin 1 Proteins 0.000 description 1
- 229910021607 Silver chloride Inorganic materials 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 241000295644 Staphylococcaceae Species 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 101100103322 Staphylococcus aureus (strain NCTC 8325 / PS 47) SAOUHSC_00052 gene Proteins 0.000 description 1
- 101100164230 Staphylococcus aureus (strain NCTC 8325 / PS 47) atl gene Proteins 0.000 description 1
- 101100439909 Staphylococcus aureus (strain NCTC 8325 / PS 47) clfA gene Proteins 0.000 description 1
- 101100439917 Staphylococcus aureus (strain NCTC 8325 / PS 47) clfB gene Proteins 0.000 description 1
- 101100501295 Staphylococcus aureus (strain NCTC 8325 / PS 47) emp gene Proteins 0.000 description 1
- 101100333827 Staphylococcus aureus (strain NCTC 8325 / PS 47) esxA gene Proteins 0.000 description 1
- 101100280092 Staphylococcus aureus (strain NCTC 8325 / PS 47) esxB gene Proteins 0.000 description 1
- 101100124415 Staphylococcus aureus (strain NCTC 8325 / PS 47) hly gene Proteins 0.000 description 1
- 101100233387 Staphylococcus aureus (strain NCTC 8325 / PS 47) isdA gene Proteins 0.000 description 1
- 101100019118 Staphylococcus aureus (strain NCTC 8325 / PS 47) isdB gene Proteins 0.000 description 1
- 101100019132 Staphylococcus aureus (strain NCTC 8325 / PS 47) isdC gene Proteins 0.000 description 1
- 101100532858 Staphylococcus aureus (strain NCTC 8325 / PS 47) sdrC gene Proteins 0.000 description 1
- 101100532867 Staphylococcus aureus (strain NCTC 8325 / PS 47) sdrD gene Proteins 0.000 description 1
- 101100096294 Staphylococcus aureus (strain NCTC 8325 / PS 47) spa gene Proteins 0.000 description 1
- 101100148962 Staphylococcus aureus (strain Newman) sdrE gene Proteins 0.000 description 1
- 241000193985 Streptococcus agalactiae Species 0.000 description 1
- 241000193998 Streptococcus pneumoniae Species 0.000 description 1
- 241000193996 Streptococcus pyogenes Species 0.000 description 1
- 241001505901 Streptococcus sp. 'group A' Species 0.000 description 1
- 241000193990 Streptococcus sp. 'group B' Species 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 101710182223 Toxin B Proteins 0.000 description 1
- 101710182532 Toxin a Proteins 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 108010031318 Vitronectin Proteins 0.000 description 1
- 102100035140 Vitronectin Human genes 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000001412 amines Chemical group 0.000 description 1
- 235000012538 ammonium bicarbonate Nutrition 0.000 description 1
- 239000001099 ammonium carbonate Substances 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 238000010913 antigen-directed enzyme pro-drug therapy Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 238000013528 artificial neural network Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 229940095731 candida albicans Drugs 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 150000007942 carboxylates Chemical group 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229940038705 chlamydia trachomatis Drugs 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- MGNCLNQXLYJVJD-UHFFFAOYSA-N cyanuric chloride Chemical compound ClC1=NC(Cl)=NC(Cl)=N1 MGNCLNQXLYJVJD-UHFFFAOYSA-N 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 238000005202 decontamination Methods 0.000 description 1
- 230000003588 decontaminative effect Effects 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000001784 detoxification Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 229960003983 diphtheria toxoid Drugs 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 229940032049 enterococcus faecalis Drugs 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 238000011010 flushing procedure Methods 0.000 description 1
- 235000021550 forms of sugar Nutrition 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-M glutaminate Chemical compound [O-]C(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-M 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 150000003278 haem Chemical class 0.000 description 1
- 229940047650 haemophilus influenzae Drugs 0.000 description 1
- 229940045808 haemophilus influenzae type b Drugs 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 239000003228 hemolysin Substances 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 229930186900 holotoxin Natural products 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000006054 immunological memory Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 229940115932 legionella pneumophila Drugs 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 108010016686 methionyl-alanyl-serine Proteins 0.000 description 1
- 244000000010 microbial pathogen Species 0.000 description 1
- 208000010805 mumps infectious disease Diseases 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 229960005030 other vaccine in atc Drugs 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000033116 oxidation-reduction process Effects 0.000 description 1
- 238000005949 ozonolysis reaction Methods 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 108010021711 pertactin Proteins 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 238000000575 proteomic method Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000006268 reductive amination reaction Methods 0.000 description 1
- 201000005404 rubella Diseases 0.000 description 1
- HKZLPVFGJNLROG-UHFFFAOYSA-M silver monochloride Chemical compound [Cl-].[Ag+] HKZLPVFGJNLROG-UHFFFAOYSA-M 0.000 description 1
- 239000010802 sludge Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 229940031000 streptococcus pneumoniae Drugs 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 238000006177 thiolation reaction Methods 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000001018 virulence Effects 0.000 description 1
- 239000000304 virulence factor Substances 0.000 description 1
- 230000007923 virulence factor Effects 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 102100036537 von Willebrand factor Human genes 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H1/00—Processes for the preparation of sugar derivatives
- C07H1/06—Separation; Purification
- C07H1/08—Separation; Purification from natural products
-
- 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
- A61K39/02—Bacterial antigens
- A61K39/085—Staphylococcus
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/04—Polysaccharides, i.e. compounds containing more than five saccharide radicals attached to each other by glycosidic bonds
-
- 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
- A61K2039/555—Medicinal preparations containing antigens or antibodies characterised by a specific combination antigen/adjuvant
- A61K2039/55505—Inorganic adjuvants
-
- 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
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6037—Bacterial toxins, e.g. diphteria toxoid [DT], tetanus toxoid [TT]
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Saccharide Compounds (AREA)
- Medicinal Preparation (AREA)
- External Artificial Organs (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US25690509P | 2009-10-30 | 2009-10-30 | |
| US61/256,905 | 2009-10-30 | ||
| PCT/IB2010/054934 WO2011051917A1 (en) | 2009-10-30 | 2010-11-01 | Purification of staphylococcus aureus type 5 and type 8 capsular saccharides |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| RU2012122237A RU2012122237A (ru) | 2013-12-10 |
| RU2579900C2 true RU2579900C2 (ru) | 2016-04-10 |
Family
ID=43513776
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2012122237/10A RU2579900C2 (ru) | 2009-10-30 | 2010-11-01 | Очистка капсульных сахаридов staphylococcus aureus типа 5 и типа 8 |
Country Status (23)
| Country | Link |
|---|---|
| US (5) | US9060965B2 (enExample) |
| EP (2) | EP2493498B1 (enExample) |
| JP (4) | JP5914344B2 (enExample) |
| CN (2) | CN109134677A (enExample) |
| AU (1) | AU2010310919B2 (enExample) |
| BR (2) | BR112012010223A2 (enExample) |
| CA (1) | CA2779578A1 (enExample) |
| CL (1) | CL2012001145A1 (enExample) |
| CY (1) | CY1118905T1 (enExample) |
| DK (1) | DK2493498T3 (enExample) |
| ES (1) | ES2626416T3 (enExample) |
| HR (1) | HRP20170674T1 (enExample) |
| HU (1) | HUE034251T2 (enExample) |
| LT (1) | LT2493498T (enExample) |
| MX (2) | MX345967B (enExample) |
| PL (1) | PL2493498T3 (enExample) |
| PT (1) | PT2493498T (enExample) |
| RS (1) | RS56000B1 (enExample) |
| RU (1) | RU2579900C2 (enExample) |
| SG (1) | SG10201407096RA (enExample) |
| SI (1) | SI2493498T1 (enExample) |
| SM (1) | SMT201700275T1 (enExample) |
| WO (1) | WO2011051917A1 (enExample) |
Families Citing this family (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20180221466A9 (en) * | 2006-06-12 | 2018-08-09 | Glaxosmithkline Biologicals S.A. | Use of alpha-toxin for treating and preventing staphylococcus infections |
| MX343111B (es) | 2009-06-22 | 2016-10-25 | Wyeth Llc | Composiciones inmunogenicas de antigenos de staphylococcus aureus. |
| BRPI1011753B8 (pt) | 2009-06-22 | 2021-05-25 | Wyeth Llc | conjugados imunogênicos de polissacarídeo capsular de staphylococcus aureus de sorotipos 5 e 8, seu uso e composições que os compreendem |
| AU2010352695B2 (en) | 2009-09-30 | 2014-08-21 | Glaxosmithkline Biologicals S.A. | Conjugation of Staphylococcus aureus type 5 and type 8 capsular polysaccharides |
| BR112012010223A2 (pt) * | 2009-10-30 | 2016-12-06 | Novartis Ag | purificação de staphylococcus aureus tipo 5 e tipo 8 sacarídeos capsulares |
| AU2012214677B2 (en) | 2011-02-08 | 2016-11-10 | Abvacc, Inc. | Immunogenic composition comprising alpha-hemolysin oligopeptides |
| CN102660602B (zh) * | 2012-04-17 | 2015-03-25 | 江苏康泰生物医学技术有限公司 | 快速纯化细菌荚膜多糖的方法 |
| PT2890394T (pt) * | 2012-08-31 | 2019-07-15 | Glaxosmithkline Biologicals Sa | Proteínas estabilizadas para imunização contra staphylococcus aureus |
| GB201310008D0 (en) | 2013-06-05 | 2013-07-17 | Glaxosmithkline Biolog Sa | Immunogenic composition for use in therapy |
| WO2015010185A1 (en) * | 2013-07-26 | 2015-01-29 | University Of Saskatchewan | Methods for producing salmonella o- antigen capsules, compositions and uses thereof |
| MX387007B (es) | 2014-12-10 | 2025-03-19 | Glaxosmithkline Biologicals Sa | Una composición inmunogénica para usarse en el tratamiento o prevención de la infección por staphylococcus aureus. |
| US11260119B2 (en) | 2018-08-24 | 2022-03-01 | Pfizer Inc. | Escherichia coli compositions and methods thereof |
| JP7239509B6 (ja) * | 2019-02-22 | 2023-03-28 | ファイザー・インク | 細菌多糖類を精製するための方法 |
| US12473379B2 (en) | 2019-09-06 | 2025-11-18 | Serum Institute Of India Private Limited | Method for obtaining purified bacterial polysaccharides |
| US10828360B1 (en) * | 2020-02-04 | 2020-11-10 | OneBioPharma, Inc. | Methods for inhibiting biofilm formation |
| BR112022015796A2 (pt) | 2020-02-21 | 2022-10-11 | Pfizer | Purificação de sacarídeos |
| EP4232593A1 (en) | 2020-10-22 | 2023-08-30 | Pfizer Inc. | Methods for purifying bacterial polysaccharides |
| US12138302B2 (en) | 2020-10-27 | 2024-11-12 | Pfizer Inc. | Escherichia coli compositions and methods thereof |
| US12357681B2 (en) | 2020-12-23 | 2025-07-15 | Pfizer Inc. | E. coli FimH mutants and uses thereof |
| CN112986457B (zh) * | 2021-02-25 | 2022-07-12 | 中国食品药品检定研究院 | HPSEC-MALS法检测多糖并与Sepharose CL-4B法关联的方法 |
| CN113234770B (zh) * | 2021-06-15 | 2024-06-14 | 广州知易生物科技有限公司 | 脆弱拟杆菌荚膜多糖a的制备方法 |
| WO2023161817A1 (en) | 2022-02-25 | 2023-08-31 | Pfizer Inc. | Methods for incorporating azido groups in bacterial capsular polysaccharides |
| CN114957509B (zh) * | 2022-08-01 | 2022-10-21 | 深圳柏垠生物科技有限公司 | 一种可放大的可拉酸纯化方法 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030180816A1 (en) * | 2001-06-11 | 2003-09-25 | Leenhouts Cornelis Johannes | Method to provide bacterial ghosts provided with antigens |
Family Cites Families (118)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2166963A (en) * | 1936-11-19 | 1939-07-25 | Sharp & Dohme Inc | Antigenic polysaccharide complex |
| CH417852A (fr) * | 1961-05-15 | 1966-07-31 | Parke Davis & Co | Procédé de préparation d'un antigène staphylococcique |
| US3269913A (en) * | 1962-05-11 | 1966-08-30 | Parke Davis & Co | Staphylococcal-immunizing products and methods for their production |
| GB995338A (en) | 1963-09-20 | 1965-06-16 | Parke Davis & Co | Polysaccharides and methods for their production |
| JPS5452794A (en) | 1977-09-30 | 1979-04-25 | Kousaku Yoshida | Extracting of polysacchride from capusle containing epidermis staphylococus |
| US4663160A (en) * | 1983-03-14 | 1987-05-05 | Miles Laboratories, Inc. | Vaccines for gram-negative bacteria |
| US4808700A (en) * | 1984-07-09 | 1989-02-28 | Praxis Biologics, Inc. | Immunogenic conjugates of non-toxic E. coli LT-B enterotoxin subunit and capsular polymers |
| US5055455A (en) * | 1988-09-28 | 1991-10-08 | Brigham And Women's Hospital | Capsular polysaccharide adhesin antigen, preparation, purification and use |
| DE3841091A1 (de) | 1988-12-07 | 1990-06-13 | Behringwerke Ag | Synthetische antigene, verfahren zu ihrer herstellung und ihre verwendung |
| CA2006700A1 (en) | 1989-01-17 | 1990-07-17 | Antonello Pessi | Synthetic peptides and their use as universal carriers for the preparation of immunogenic conjugates suitable for the development of synthetic vaccines |
| AU651949B2 (en) | 1989-07-14 | 1994-08-11 | American Cyanamid Company | Cytokine and hormone carriers for conjugate vaccines |
| IT1237764B (it) | 1989-11-10 | 1993-06-17 | Eniricerche Spa | Peptidi sintetici utili come carriers universali per la preparazione di coniugati immunogenici e loro impiego per lo sviluppo di vaccini sintetici. |
| SE466259B (sv) | 1990-05-31 | 1992-01-20 | Arne Forsgren | Protein d - ett igd-bindande protein fraan haemophilus influenzae, samt anvaendning av detta foer analys, vacciner och uppreningsaendamaal |
| DE69113564T2 (de) | 1990-08-13 | 1996-05-30 | American Cyanamid Co | Faser-Hemagglutinin von Bordetella pertussis als Träger für konjugierten Impfstoff. |
| US5153312A (en) | 1990-09-28 | 1992-10-06 | American Cyanamid Company | Oligosaccharide conjugate vaccines |
| FR2682388B1 (fr) | 1991-10-10 | 1995-06-09 | Pasteur Merieux Serums Vacc | Procede de preparation d'un oligoside par depolymerisation d'un polyoside issu d'un agent pathogene, oligoside ainsi obtenu et son utilisation notamment comme agent vaccinal. |
| ES2198405T3 (es) * | 1991-11-22 | 2004-02-01 | Nabi Biopharmaceuticals | Antigenos de superficie de tipo i asociados a staphylococcus epidermis. |
| IT1262896B (it) | 1992-03-06 | 1996-07-22 | Composti coniugati formati da proteine heat shock (hsp) e oligo-poli- saccaridi, loro uso per la produzione di vaccini. | |
| IL102687A (en) | 1992-07-30 | 1997-06-10 | Yeda Res & Dev | Conjugates of poorly immunogenic antigens and synthetic pepide carriers and vaccines comprising them |
| US5679654A (en) * | 1994-09-02 | 1997-10-21 | Brigham & Women's Hospital, Inc. | Capsular polysaccharide immunomodulator |
| IL117483A (en) | 1995-03-17 | 2008-03-20 | Bernard Brodeur | MENINGITIDIS NEISSERIA shell protein is resistant to proteinase K. |
| US6743430B1 (en) * | 1995-03-29 | 2004-06-01 | Richard E. Parizek | Multicomponent vaccine containing clostridial and non-clostridial organisms in a low dose |
| BR9608612A (pt) | 1995-06-07 | 1999-05-04 | Smithkline Beecham Biolog | Vacina compreendendo um conjugado de antígeno de polissacarídeo - proteína portadora e proteína portadora livre |
| US6294177B1 (en) * | 1996-09-11 | 2001-09-25 | Nabi | Staphylococcus aureus antigen-containing whole cell vaccine |
| US5770208A (en) | 1996-09-11 | 1998-06-23 | Nabi | Staphylococcus aureus B-linked hexosamine antigen |
| US6299881B1 (en) | 1997-03-24 | 2001-10-09 | Henry M. Jackson Foundation For The Advancement Of Military Medicine | Uronium salts for activating hydroxyls, carboxyls, and polysaccharides, and conjugate vaccines, immunogens, and other useful immunological reagents produced using uronium salts |
| JP2001519817A (ja) | 1997-03-26 | 2001-10-23 | ブリガム アンド ウイメンズ ホスピタル | 糖断片生成法 |
| GB9713156D0 (en) | 1997-06-20 | 1997-08-27 | Microbiological Res Authority | Vaccines |
| DE69841807D1 (de) | 1997-11-06 | 2010-09-16 | Novartis Vaccines & Diagnostic | Neisseriale antigene |
| ATE352624T1 (de) | 1997-11-21 | 2007-02-15 | Serono Genetics Inst Sa | Chlamydia pneumoniae genomische sequenzen und polypeptiden, fragmenten und anwendungen davon für nachweis, prevention und heilung |
| KR100760221B1 (ko) | 1997-11-28 | 2007-10-30 | 세로노 제네틱스 인스티튜트 에스.에이. | 클라미디아 트라코마티스 게놈 서열과 폴리펩티드, 이의단편 및 이의 용도, 특히, 감염의 진단, 예방 및 치료 용도 |
| DE69941567D1 (de) | 1998-01-14 | 2009-12-03 | Novartis Vaccines & Diagnostic | Antigene aus neisseria meningitidis |
| US7018637B2 (en) | 1998-02-23 | 2006-03-28 | Aventis Pasteur, Inc | Multi-oligosaccharide glycoconjugate bacterial meningitis vaccines |
| GB9808932D0 (en) * | 1998-04-27 | 1998-06-24 | Chiron Spa | Polyepitope carrier protein |
| DE69937419T2 (de) | 1998-05-01 | 2008-07-24 | Novartis Vaccines and Diagnostics, Inc., Emeryville | Neisseria Meningitidis Antigene und Zusammenstellungen |
| US7252828B2 (en) * | 1998-07-15 | 2007-08-07 | The Brigham And Women's Hospital, Inc. | Polysaccharide vaccine for staphylococcal infections |
| MXPA01003557A (es) | 1998-10-09 | 2004-04-05 | Chiron Corp | Secuencias genomicas de neisseria y metodos para su uso. |
| WO2000027994A2 (en) | 1998-11-12 | 2000-05-18 | The Regents Of The University Of California | Chlamydia pneumoniae genome sequence |
| GB9828000D0 (en) | 1998-12-18 | 1999-02-10 | Chiron Spa | Antigens |
| US6146902A (en) | 1998-12-29 | 2000-11-14 | Aventis Pasteur, Inc. | Purification of polysaccharide-protein conjugate vaccines by ultrafiltration with ammonium sulfate solutions |
| WO2000056359A2 (en) | 1999-03-19 | 2000-09-28 | Smithkline Beecham Biologicals S.A. | Vaccine against streptococcus pneumoniae |
| US6936258B1 (en) | 1999-03-19 | 2005-08-30 | Nabi Biopharmaceuticals | Staphylococcus antigen and vaccine |
| CA2365914A1 (en) | 1999-04-09 | 2000-10-19 | Techlab, Inc. | Recombinant clostridium toxin a protein carrier for polysaccharide conjugate vaccines |
| US7534866B2 (en) | 2005-10-19 | 2009-05-19 | Ibc Pharmaceuticals, Inc. | Methods and compositions for generating bioactive assemblies of increased complexity and uses |
| US6689567B1 (en) * | 1999-05-28 | 2004-02-10 | University Of Guelph | Method for assaying the function of FlaA1 and WbpM |
| EP2275129A3 (en) | 2000-01-17 | 2013-11-06 | Novartis Vaccines and Diagnostics S.r.l. | Outer membrane vesicle (OMV) vaccine comprising N. meningitidis serogroup B outer membrane proteins |
| GB0007432D0 (en) | 2000-03-27 | 2000-05-17 | Microbiological Res Authority | Proteins for use as carriers in conjugate vaccines |
| WO2002002606A2 (en) | 2000-07-03 | 2002-01-10 | Chiron S.P.A. | Immunisation against chlamydia pneumoniae |
| AU1412702A (en) | 2000-10-27 | 2002-05-06 | Chiron Spa | Nucleic acids and proteins from streptococcus groups a and b |
| WO2002091998A2 (en) | 2001-05-11 | 2002-11-21 | Aventis Pasteur, Inc. | Novel meningitis conjugate vaccine |
| US6537577B1 (en) * | 2001-06-04 | 2003-03-25 | Bio Medical Development Corporation | Method of prophylaxis for bovine mastitis |
| GB2379996B (en) * | 2001-06-05 | 2004-05-19 | Tayside Flow Technologies Ltd | Flow means |
| GB0115176D0 (en) | 2001-06-20 | 2001-08-15 | Chiron Spa | Capular polysaccharide solubilisation and combination vaccines |
| US20040161741A1 (en) | 2001-06-30 | 2004-08-19 | Elazar Rabani | Novel compositions and processes for analyte detection, quantification and amplification |
| US20030113350A1 (en) * | 2001-09-19 | 2003-06-19 | Fattom Ali I. | Glycoconjugate vaccines for use in immune-compromised populations |
| GB0210128D0 (en) | 2002-05-02 | 2002-06-12 | Chiron Spa | Nucleic acids and proteins from streptococcus groups A & B |
| US20040096461A1 (en) | 2002-07-30 | 2004-05-20 | Baxter Healthcare Corporation | Chimeric multivalent polysaccharide conjugate vaccines |
| US20060121058A1 (en) * | 2002-08-08 | 2006-06-08 | Children's Medical Center Corporation | Anti-pneumococcal preparations |
| AU2003260102A1 (en) | 2002-08-26 | 2004-03-11 | Chiron Corporation | Conserved and specific streptococcal genomes |
| GB0220198D0 (en) * | 2002-08-30 | 2002-10-09 | Chiron Spa | Modified saccharides,conjugates thereof and their manufacture |
| PT1551357E (pt) | 2002-09-13 | 2014-10-10 | Novartis Vaccines & Diagnostic | Vacina contra os estreptococos do grupo b |
| WO2004043407A2 (en) | 2002-11-12 | 2004-05-27 | The Brigham And Women's Hospital, Inc. | Methods and products for treating staphylococcal infections |
| AU2003295520B8 (en) | 2002-11-12 | 2011-05-19 | The Brigham And Women's Hospital, Inc. | Polysaccharide vaccine for Staphylococcal infections |
| GB0227346D0 (en) * | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
| EP1601381A2 (en) | 2003-03-07 | 2005-12-07 | Wyeth Holdings Corporation | Polysaccharide - staphylococcal surface adhesin carrier protein conjugates for immunization against nosocomial infections |
| US8084235B2 (en) | 2003-03-13 | 2011-12-27 | Glaxosmithkline Biologicals S.A. | Purification process for bacterial cytolysin |
| WO2005000346A1 (en) * | 2003-06-23 | 2005-01-06 | Baxter International Inc. | Carrier proteins for vaccines |
| HRP20100240T1 (hr) | 2003-07-24 | 2010-09-30 | Merck Sharp & Dohme Corp. | Polipeptidi za indukciju zaštitnog imunitetnog odgovora protiv staphylococcus aureus |
| WO2005009378A2 (en) | 2003-07-24 | 2005-02-03 | Merck & Co., Inc. | Polypeptides for inducing a protective immune response against staphylococcus aureus |
| US8048432B2 (en) * | 2003-08-06 | 2011-11-01 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Polysaccharide-protein conjugate vaccines |
| PL1664319T3 (pl) * | 2003-09-11 | 2010-07-30 | De Staat Der Nederlanden Vert Door De Mini Van Vws | Sposób wytwarzania polisacharydu otoczkowego do zastosowania w szczepionkach koniugatowych |
| GB0323103D0 (en) | 2003-10-02 | 2003-11-05 | Chiron Srl | De-acetylated saccharides |
| JP2007528217A (ja) | 2004-02-18 | 2007-10-11 | メルク エンド カムパニー インコーポレーテッド | スタヒロコッカス・アウレウスに対する防御免疫応答を誘導するためのポリペプチド |
| WO2005086663A2 (en) | 2004-02-27 | 2005-09-22 | Merck & Co., Inc. | Polypeptides for inducing a protective immune response against staphlococcus aureus |
| US20050250821A1 (en) * | 2004-04-16 | 2005-11-10 | Vincent Sewalt | Quaternary ammonium compounds in the treatment of water and as antimicrobial wash |
| US7842479B2 (en) * | 2004-05-21 | 2010-11-30 | The Board Of Regents Of The University Of Nebraska | Methods for altering acetic acid production and enhancing cell death in bacteria |
| CN1956727A (zh) | 2004-05-25 | 2007-05-02 | 默克公司 | 诱导抗金黄色葡萄球菌的保护性免疫应答的多肽 |
| GB0413868D0 (en) * | 2004-06-21 | 2004-07-21 | Chiron Srl | Dimensional anlaysis of saccharide conjugates |
| WO2006033918A2 (en) | 2004-09-17 | 2006-03-30 | Merck & Co., Inc. | Polypeptides for inducing a protective immune response against staphylococcus aureus |
| AU2005287505A1 (en) | 2004-09-22 | 2006-03-30 | Biosynexus Incorporated | Staphylococcal immunogenic compositions |
| US20060134141A1 (en) | 2004-12-14 | 2006-06-22 | Nabi Biopharmaceuticals | Glycoconjugate vaccines containing peptidoglycan |
| US7718182B2 (en) | 2005-01-21 | 2010-05-18 | Merck Sharp & Dohme Corp. | Polypeptides for inducing a protective immune response against Staphylococcus aureus |
| GB0502096D0 (en) * | 2005-02-01 | 2005-03-09 | Chiron Srl | Purification of streptococcal capsular polysaccharide |
| US20060228368A1 (en) | 2005-04-07 | 2006-10-12 | Nabi Biopharmaceuticals | Method of protecting against staphylococcal infection |
| FR2884830A1 (fr) | 2005-04-25 | 2006-10-27 | Sanofi Pasteur Sa | Procede de production de souches de staphylococcus aureus surproductrices |
| EP2201961B1 (en) * | 2005-06-27 | 2018-01-24 | GlaxoSmithKline Biologicals S.A. | Immunogenic composition |
| AU2006283302B2 (en) * | 2005-08-24 | 2012-11-15 | Novartis Vaccines And Diagnostics Srl | Zwitterionization of capsular saccharides |
| GB0526038D0 (en) | 2005-12-21 | 2006-02-01 | Glaxosmithkline Biolog Sa | Immunogenic composition |
| US8598337B2 (en) * | 2006-01-13 | 2013-12-03 | Baxter International Inc. | Method for purifying polysaccharides |
| AR060187A1 (es) | 2006-03-30 | 2008-05-28 | Glaxosmithkline Biolog Sa | Composicion inmunogenica |
| EA015833B1 (ru) | 2006-03-30 | 2011-12-30 | Глаксосмитклайн Байолоджикалс С.А. | Иммуногенная композиция |
| FR2899110A1 (fr) * | 2006-03-31 | 2007-10-05 | Sanofi Pasteur Sa | Polysaccharides capsulaires de type 5 et de type 8 des souches surproductrices de staphylococcus aureus |
| CN101466406B (zh) | 2006-06-12 | 2012-06-27 | 葛兰素史密斯克蓝生物品公司 | α-毒素在治疗和预防葡萄球菌感染上的用途 |
| GB0612854D0 (en) * | 2006-06-28 | 2006-08-09 | Novartis Ag | Saccharide analysis |
| WO2008152447A2 (en) | 2006-10-30 | 2008-12-18 | The University Of Western Ontario | Staphylococcus aureus specific anti-infectives |
| WO2008055501A1 (en) * | 2006-11-08 | 2008-05-15 | B-K Medical Aps | Method and apparatus for two-step sterilization |
| DE102006062398A1 (de) | 2006-12-20 | 2008-06-26 | Edi (Experimentelle & Diagnostische Immunologie) Gmbh | Verfahren zur Erkennung und/oder Charakterisierung zellulärer Aktivitätsmuster, Verwendung von Toll-like-Rezeptor-Liganden (TLR-Liganden) und ein Kit |
| GB0700136D0 (en) * | 2007-01-04 | 2007-02-14 | Glaxosmithkline Biolog Sa | Process for manufacturing vaccines |
| GB0700135D0 (en) * | 2007-01-04 | 2007-02-14 | Glaxosmithkline Biolog Sa | Vaccine |
| RU2009149294A (ru) | 2007-05-31 | 2011-07-10 | Мерк энд Ко., Инк. (US) | Антиген-связывающие белки, нацеленные на orf0657n s.aureus |
| GB0713880D0 (en) | 2007-07-17 | 2007-08-29 | Novartis Ag | Conjugate purification |
| CN101951948B (zh) | 2007-08-31 | 2015-12-09 | 芝加哥大学 | 与针对葡萄球菌性肺部疾病和病症进行免疫相关的方法和组合物 |
| EP2254592B1 (en) | 2008-02-28 | 2019-06-05 | Dako Denmark A/S | Mhc multimers in borrelia diagnostics and disease |
| PL2344523T3 (pl) * | 2008-09-17 | 2016-09-30 | Skojarzone szczepionki i środki terapeutyczne przeciw GAS | |
| WO2010042481A1 (en) * | 2008-10-06 | 2010-04-15 | University Of Chicago | Compositions and methods related to bacterial eap, emp, and/or adsa proteins |
| WO2010132833A1 (en) * | 2009-05-14 | 2010-11-18 | The Regents Of The University Of Michigan | Streptococcus vaccine compositions and methods of using the same |
| BRPI1011753B8 (pt) * | 2009-06-22 | 2021-05-25 | Wyeth Llc | conjugados imunogênicos de polissacarídeo capsular de staphylococcus aureus de sorotipos 5 e 8, seu uso e composições que os compreendem |
| MX343111B (es) * | 2009-06-22 | 2016-10-25 | Wyeth Llc | Composiciones inmunogenicas de antigenos de staphylococcus aureus. |
| GB0913681D0 (en) * | 2009-08-05 | 2009-09-16 | Glaxosmithkline Biolog Sa | Immunogenic composition |
| AU2010352695B2 (en) * | 2009-09-30 | 2014-08-21 | Glaxosmithkline Biologicals S.A. | Conjugation of Staphylococcus aureus type 5 and type 8 capsular polysaccharides |
| BR112012010223A2 (pt) * | 2009-10-30 | 2016-12-06 | Novartis Ag | purificação de staphylococcus aureus tipo 5 e tipo 8 sacarídeos capsulares |
| JPWO2011081075A1 (ja) * | 2009-12-28 | 2013-05-09 | キッコーマン株式会社 | 黄色ブドウ球菌抗原の抽出方法、黄色ブドウ球菌抗原の抽出用試薬および黄色ブドウ球菌の判定方法 |
| ES2707778T3 (es) | 2009-12-30 | 2019-04-05 | Glaxosmithkline Biologicals Sa | Inmunógenos polisacáridos conjugados con proteínas portadoras de E. coli |
| BR112013000097B1 (pt) * | 2010-07-02 | 2022-02-01 | The University Of Chicago | Polipeptídeo imunogênico isolado, composição imunogênica e seu uso |
| GB201310008D0 (en) * | 2013-06-05 | 2013-07-17 | Glaxosmithkline Biolog Sa | Immunogenic composition for use in therapy |
| EP3076998A1 (en) | 2013-12-04 | 2016-10-12 | Glycovaxyn AG | Prevention of staphylococcus aureus infections by glycoprotein vaccines synthesized in escherichia coli |
| US9775872B2 (en) | 2014-08-20 | 2017-10-03 | Professional Compounding Centers Of America | Topical pharmaceutical bases for preventing viral diseases |
| KR20200018787A (ko) * | 2017-05-22 | 2020-02-20 | 더 칠드런스 메디칼 센터 코포레이션 | 마이코박테리움 투버큘로시스에 대한 혼합 백신 |
-
2010
- 2010-11-01 BR BR112012010223A patent/BR112012010223A2/pt not_active Application Discontinuation
- 2010-11-01 RS RS20170528A patent/RS56000B1/sr unknown
- 2010-11-01 CA CA2779578A patent/CA2779578A1/en not_active Abandoned
- 2010-11-01 US US13/504,920 patent/US9060965B2/en active Active
- 2010-11-01 LT LTEP10782040.9T patent/LT2493498T/lt unknown
- 2010-11-01 JP JP2012536006A patent/JP5914344B2/ja not_active Expired - Fee Related
- 2010-11-01 CN CN201810862632.7A patent/CN109134677A/zh active Pending
- 2010-11-01 EP EP10782040.9A patent/EP2493498B1/en active Active
- 2010-11-01 PL PL10782040T patent/PL2493498T3/pl unknown
- 2010-11-01 CN CN2010800605540A patent/CN102971009A/zh active Pending
- 2010-11-01 MX MX2015017594A patent/MX345967B/es unknown
- 2010-11-01 WO PCT/IB2010/054934 patent/WO2011051917A1/en not_active Ceased
- 2010-11-01 DK DK10782040.9T patent/DK2493498T3/en active
- 2010-11-01 RU RU2012122237/10A patent/RU2579900C2/ru active
- 2010-11-01 PT PT107820409T patent/PT2493498T/pt unknown
- 2010-11-01 HU HUE10782040A patent/HUE034251T2/en unknown
- 2010-11-01 AU AU2010310919A patent/AU2010310919B2/en not_active Ceased
- 2010-11-01 SI SI201031449A patent/SI2493498T1/sl unknown
- 2010-11-01 HR HRP20170674TT patent/HRP20170674T1/hr unknown
- 2010-11-01 MX MX2012004851A patent/MX2012004851A/es unknown
- 2010-11-01 ES ES10782040.9T patent/ES2626416T3/es active Active
- 2010-11-01 BR BR122019005883A patent/BR122019005883A8/pt not_active Application Discontinuation
- 2010-11-01 EP EP17160320.2A patent/EP3199177A1/en not_active Withdrawn
- 2010-11-01 SG SG10201407096RA patent/SG10201407096RA/en unknown
- 2010-11-01 SM SM20170275T patent/SMT201700275T1/it unknown
-
2012
- 2012-04-30 CL CL2012001145A patent/CL2012001145A1/es unknown
-
2015
- 2015-05-15 US US14/714,097 patent/US9441004B2/en not_active Expired - Fee Related
- 2015-12-30 JP JP2015257722A patent/JP2016047852A/ja not_active Withdrawn
-
2016
- 2016-09-07 US US15/258,881 patent/US20160376301A1/en not_active Abandoned
-
2017
- 2017-04-26 CY CY20171100468T patent/CY1118905T1/el unknown
- 2017-09-01 JP JP2017168223A patent/JP2017206564A/ja not_active Withdrawn
-
2019
- 2019-02-13 US US16/274,822 patent/US11208424B2/en active Active
- 2019-04-05 JP JP2019072625A patent/JP2019104940A/ja not_active Withdrawn
-
2021
- 2021-11-17 US US17/528,426 patent/US20220089627A1/en not_active Abandoned
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030180816A1 (en) * | 2001-06-11 | 2003-09-25 | Leenhouts Cornelis Johannes | Method to provide bacterial ghosts provided with antigens |
Non-Patent Citations (2)
| Title |
|---|
| DENG L. et al. "Characterization of the linkage between the type III capcular polysaccharide and the bacterial cell wall of group 8 Streptococcus", J. Biol. Chem., 2000, v.275, p.7497-7504. GILBERT F. et al. "Purification of type 5 capsular polysaccharide from Straphylococcus aureus by a simple efficient method", J. Microbiol. Meth., 1994, v.20, p.39-46. LEFEBER D. et al. "Isolation of oligosaccharides from a partial-acid hydrolysate of pneumococcal type 3 polysaccharide for use in conjugate vaccines", Carbohydrate Research, 2002, v.337, p.819-825. * |
| FATTOM A. et al. "Synthesis and immunologic properties in mice of vaccines composed of Staphylococcus aureus type 5 and type 8 capsular polysaccharides conjugated to Pseudomonas aeruginosa Еxotoxin A", Infection and Immunity, 1990, v.58, p.2367-2374. * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2579900C2 (ru) | Очистка капсульных сахаридов staphylococcus aureus типа 5 и типа 8 | |
| AU2011303478B2 (en) | Immunogenic compositions | |
| JP6276227B2 (ja) | Ｓｔａｐｈｙｌｏｃｏｃｃｕｓ．ａｕｒｅｕｓ５型および８型莢膜多糖の結合体 | |
| US20100063270A1 (en) | Purification of Streptococcal Capsular Polysaccharide | |
| JPH10504717A (ja) | 肺炎双球菌感染症に対する免疫化のための肺炎双球菌多糖−組み換えニューモリシン結合体ワクチン類 | |
| WO2017011338A1 (en) | Sortase-mediated coupling of immunogenic polysaccharide-protein conjugates and their use | |
| US6722062B2 (en) | Capsular polysaccharides from enterococci |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PC41 | Official registration of the transfer of exclusive right |
Effective date: 20220127 |