NO305463B1 - FremgangsmÕte for fremstilling av en vaksine mot Neisseria meningitidis, klasse 2/3 minusmutant av Neisseria Neisseria meningitidis stamme, samt mikroorganisme som uttrykker et fusjonsprotein - Google Patents
FremgangsmÕte for fremstilling av en vaksine mot Neisseria meningitidis, klasse 2/3 minusmutant av Neisseria Neisseria meningitidis stamme, samt mikroorganisme som uttrykker et fusjonsprotein Download PDFInfo
- Publication number
- NO305463B1 NO305463B1 NO912369A NO912369A NO305463B1 NO 305463 B1 NO305463 B1 NO 305463B1 NO 912369 A NO912369 A NO 912369A NO 912369 A NO912369 A NO 912369A NO 305463 B1 NO305463 B1 NO 305463B1
- Authority
- NO
- Norway
- Prior art keywords
- class
- outer membrane
- protein
- membrane protein
- meningococcal
- Prior art date
Links
- 241000588650 Neisseria meningitidis Species 0.000 title claims abstract description 43
- 229960005486 vaccine Drugs 0.000 title claims description 79
- 238000000034 method Methods 0.000 title claims description 66
- 108020001507 fusion proteins Proteins 0.000 title claims description 21
- 102000037865 fusion proteins Human genes 0.000 title claims description 21
- 244000005700 microbiome Species 0.000 title claims description 10
- 101710116435 Outer membrane protein Proteins 0.000 claims abstract description 197
- 239000012634 fragment Substances 0.000 claims abstract description 59
- 108010038807 Oligopeptides Proteins 0.000 claims abstract description 36
- 102000015636 Oligopeptides Human genes 0.000 claims abstract description 36
- 239000012528 membrane Substances 0.000 claims abstract description 18
- 108090000623 proteins and genes Proteins 0.000 claims description 120
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 82
- 102000004169 proteins and genes Human genes 0.000 claims description 72
- 108010040721 Flagellin Proteins 0.000 claims description 50
- 150000001413 amino acids Chemical class 0.000 claims description 42
- 241000700605 Viruses Species 0.000 claims description 27
- 239000000427 antigen Substances 0.000 claims description 23
- 108091007433 antigens Proteins 0.000 claims description 23
- 102000036639 antigens Human genes 0.000 claims description 23
- 230000001580 bacterial effect Effects 0.000 claims description 23
- 229920001282 polysaccharide Polymers 0.000 claims description 21
- 108010071134 CRM197 (non-toxic variant of diphtheria toxin) Proteins 0.000 claims description 20
- 239000005017 polysaccharide Substances 0.000 claims description 20
- 238000004519 manufacturing process Methods 0.000 claims description 19
- 241000588653 Neisseria Species 0.000 claims description 18
- 150000004676 glycans Chemical class 0.000 claims description 18
- 230000021615 conjugation Effects 0.000 claims description 17
- 230000014509 gene expression Effects 0.000 claims description 16
- 230000002163 immunogen Effects 0.000 claims description 16
- 238000000746 purification Methods 0.000 claims description 15
- 239000003937 drug carrier Substances 0.000 claims description 14
- 102000014914 Carrier Proteins Human genes 0.000 claims description 13
- 108010078791 Carrier Proteins Proteins 0.000 claims description 13
- 239000000126 substance Substances 0.000 claims description 13
- 239000013604 expression vector Substances 0.000 claims description 12
- 229960000814 tetanus toxoid Drugs 0.000 claims description 11
- 230000000890 antigenic effect Effects 0.000 claims description 10
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 claims description 10
- 241000607142 Salmonella Species 0.000 claims description 9
- 150000002632 lipids Chemical class 0.000 claims description 9
- 108010013381 Porins Proteins 0.000 claims description 8
- 102000007739 porin activity proteins Human genes 0.000 claims description 8
- 230000002238 attenuated effect Effects 0.000 claims description 6
- 150000002482 oligosaccharides Polymers 0.000 claims description 6
- 238000003786 synthesis reaction Methods 0.000 claims description 6
- 238000012258 culturing Methods 0.000 claims description 5
- 230000002068 genetic effect Effects 0.000 claims description 5
- 108010051815 Glutamyl endopeptidase Proteins 0.000 claims description 4
- 108091005804 Peptidases Proteins 0.000 claims description 4
- 231100000699 Bacterial toxin Toxicity 0.000 claims description 3
- 239000004365 Protease Substances 0.000 claims description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 3
- 239000000688 bacterial toxin Substances 0.000 claims description 3
- 239000002502 liposome Substances 0.000 claims description 3
- 102000016607 Diphtheria Toxin Human genes 0.000 claims description 2
- 108010053187 Diphtheria Toxin Proteins 0.000 claims description 2
- 230000000415 inactivating effect Effects 0.000 claims description 2
- 230000008569 process Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 102000005936 beta-Galactosidase Human genes 0.000 claims 2
- 108010005774 beta-Galactosidase Proteins 0.000 claims 2
- 108010030544 Peptidyl-Lys metalloendopeptidase Proteins 0.000 claims 1
- 108010059339 submandibular proteinase A Proteins 0.000 claims 1
- 208000037941 meningococcal disease Diseases 0.000 abstract description 5
- 235000018102 proteins Nutrition 0.000 description 66
- 102000004196 processed proteins & peptides Human genes 0.000 description 38
- 108020004414 DNA Proteins 0.000 description 36
- 210000004027 cell Anatomy 0.000 description 29
- 239000000562 conjugate Substances 0.000 description 28
- 239000013598 vector Substances 0.000 description 26
- 238000002360 preparation method Methods 0.000 description 25
- 210000001744 T-lymphocyte Anatomy 0.000 description 24
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 23
- 239000000203 mixture Substances 0.000 description 19
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 18
- 229940024606 amino acid Drugs 0.000 description 17
- 235000001014 amino acid Nutrition 0.000 description 17
- 230000000844 anti-bacterial effect Effects 0.000 description 17
- 238000006243 chemical reaction Methods 0.000 description 17
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 16
- 238000007792 addition Methods 0.000 description 14
- 101710169972 Menin Proteins 0.000 description 13
- 102100030550 Menin Human genes 0.000 description 13
- 108091034117 Oligonucleotide Proteins 0.000 description 13
- 238000013518 transcription Methods 0.000 description 13
- 241000588724 Escherichia coli Species 0.000 description 12
- 238000001262 western blot Methods 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 11
- 230000001681 protective effect Effects 0.000 description 11
- 239000011780 sodium chloride Substances 0.000 description 11
- 230000035897 transcription Effects 0.000 description 11
- 108020004511 Recombinant DNA Proteins 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 239000013612 plasmid Substances 0.000 description 10
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 230000005875 antibody response Effects 0.000 description 9
- 239000004202 carbamide Substances 0.000 description 9
- 210000003495 flagella Anatomy 0.000 description 9
- 230000028993 immune response Effects 0.000 description 9
- 238000003780 insertion Methods 0.000 description 9
- 230000037431 insertion Effects 0.000 description 9
- 230000004044 response Effects 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- -1 tert-butyloxycarbonylamino acids Chemical class 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 108091006905 Human Serum Albumin Proteins 0.000 description 8
- 102000008100 Human Serum Albumin Human genes 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 8
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 8
- 239000000499 gel Substances 0.000 description 8
- 230000005847 immunogenicity Effects 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 7
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 7
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 7
- 238000005119 centrifugation Methods 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 238000010367 cloning Methods 0.000 description 7
- 238000010276 construction Methods 0.000 description 7
- 238000002523 gelfiltration Methods 0.000 description 7
- 239000002953 phosphate buffered saline Substances 0.000 description 7
- 239000004094 surface-active agent Substances 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 6
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- 125000005647 linker group Chemical group 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 238000012163 sequencing technique Methods 0.000 description 6
- 108700005089 MHC Class I Genes Proteins 0.000 description 5
- 210000004899 c-terminal region Anatomy 0.000 description 5
- 239000000969 carrier Substances 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 238000005227 gel permeation chromatography Methods 0.000 description 5
- 230000001900 immune effect Effects 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 230000004807 localization Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 230000001717 pathogenic effect Effects 0.000 description 5
- 238000010647 peptide synthesis reaction Methods 0.000 description 5
- 238000003752 polymerase chain reaction Methods 0.000 description 5
- 230000009257 reactivity Effects 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 238000003756 stirring Methods 0.000 description 5
- 229940125575 vaccine candidate Drugs 0.000 description 5
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 4
- 108700018753 Neisseria porin Proteins 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 210000000612 antigen-presenting cell Anatomy 0.000 description 4
- 210000003719 b-lymphocyte Anatomy 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 239000003480 eluent Substances 0.000 description 4
- 239000002158 endotoxin Substances 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 210000004698 lymphocyte Anatomy 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
- 229920001542 oligosaccharide Polymers 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- SQGYOTSLMSWVJD-UHFFFAOYSA-N silver(1+) nitrate Chemical compound [Ag+].[O-]N(=O)=O SQGYOTSLMSWVJD-UHFFFAOYSA-N 0.000 description 4
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 4
- 229940033663 thimerosal Drugs 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
- 241000700626 Cowpox virus Species 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
- 244000182691 Echinochloa frumentacea Species 0.000 description 3
- 235000008247 Echinochloa frumentacea Nutrition 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- 201000009906 Meningitis Diseases 0.000 description 3
- 229940122605 Short-acting muscarinic antagonist Drugs 0.000 description 3
- 230000005867 T cell response Effects 0.000 description 3
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 3
- 235000011130 ammonium sulphate Nutrition 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 150000001720 carbohydrates Chemical group 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 238000004440 column chromatography Methods 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 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
- 238000000338 in vitro Methods 0.000 description 3
- 229940031551 inactivated vaccine Drugs 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 229920006008 lipopolysaccharide Polymers 0.000 description 3
- 229960005037 meningococcal vaccines Drugs 0.000 description 3
- 230000004899 motility Effects 0.000 description 3
- 229940031348 multivalent vaccine Drugs 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 238000007254 oxidation reaction Methods 0.000 description 3
- 244000045947 parasite Species 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000012064 sodium phosphate buffer Substances 0.000 description 3
- 230000000638 stimulation Effects 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 231100000765 toxin Toxicity 0.000 description 3
- 108700012359 toxins Proteins 0.000 description 3
- 241000701161 unidentified adenovirus Species 0.000 description 3
- NKUZQMZWTZAPSN-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 2-bromoacetate Chemical compound BrCC(=O)ON1C(=O)CCC1=O NKUZQMZWTZAPSN-UHFFFAOYSA-N 0.000 description 2
- BQWBEDSJTMWJAE-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 4-[(2-iodoacetyl)amino]benzoate Chemical compound C1=CC(NC(=O)CI)=CC=C1C(=O)ON1C(=O)CCC1=O BQWBEDSJTMWJAE-UHFFFAOYSA-N 0.000 description 2
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 2
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 2
- FJLUATLTXUNBOT-UHFFFAOYSA-N 1-Hexadecylamine Chemical compound CCCCCCCCCCCCCCCCN FJLUATLTXUNBOT-UHFFFAOYSA-N 0.000 description 2
- PYAFUXYGTYWWBP-UHFFFAOYSA-N 19-methoxynonadecane-1,2,3-triol Chemical compound COCCCCCCCCCCCCCCCCC(O)C(O)CO PYAFUXYGTYWWBP-UHFFFAOYSA-N 0.000 description 2
- MGADZUXDNSDTHW-UHFFFAOYSA-N 2H-pyran Chemical compound C1OC=CC=C1 MGADZUXDNSDTHW-UHFFFAOYSA-N 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 2
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 101710132601 Capsid protein Proteins 0.000 description 2
- 239000004971 Cross linker Substances 0.000 description 2
- 229920002271 DEAE-Sepharose Polymers 0.000 description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 2
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- 230000005526 G1 to G0 transition Effects 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- IFQSXNOEEPCSLW-DKWTVANSSA-N L-cysteine hydrochloride Chemical compound Cl.SC[C@H](N)C(O)=O IFQSXNOEEPCSLW-DKWTVANSSA-N 0.000 description 2
- 108010074338 Lymphokines Proteins 0.000 description 2
- 102000008072 Lymphokines Human genes 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 101710081079 Minor spike protein H Proteins 0.000 description 2
- FFDGPVCHZBVARC-UHFFFAOYSA-N N,N-dimethylglycine Chemical compound CN(C)CC(O)=O FFDGPVCHZBVARC-UHFFFAOYSA-N 0.000 description 2
- 241000588652 Neisseria gonorrhoeae Species 0.000 description 2
- REYJJPSVUYRZGE-UHFFFAOYSA-N Octadecylamine Chemical compound CCCCCCCCCCCCCCCCCCN REYJJPSVUYRZGE-UHFFFAOYSA-N 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 102100029251 Phagocytosis-stimulating peptide Human genes 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- NQRYJNQNLNOLGT-UHFFFAOYSA-N Piperidine Chemical compound C1CCNCC1 NQRYJNQNLNOLGT-UHFFFAOYSA-N 0.000 description 2
- 241000125945 Protoparvovirus Species 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 108700031314 Rotavirus VP6 Proteins 0.000 description 2
- 241000392514 Salmonella enterica subsp. enterica serovar Dublin Species 0.000 description 2
- 241000607124 Salmonella enterica subsp. enterica serovar Muenchen Species 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 229920002125 Sokalan® Polymers 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 2
- 108010006785 Taq Polymerase Proteins 0.000 description 2
- 102000006601 Thymidine Kinase Human genes 0.000 description 2
- 108020004440 Thymidine kinase Proteins 0.000 description 2
- 108010084754 Tuftsin Proteins 0.000 description 2
- BHATUINFZWUDIX-UHFFFAOYSA-N Zwittergent 3-14 Chemical compound CCCCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O BHATUINFZWUDIX-UHFFFAOYSA-N 0.000 description 2
- CWGJBBRZFIPXNZ-UHFFFAOYSA-N [C-]#N.Br Chemical compound [C-]#N.Br CWGJBBRZFIPXNZ-UHFFFAOYSA-N 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 229940037003 alum Drugs 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 244000052616 bacterial pathogen Species 0.000 description 2
- 230000000721 bacterilogical effect Effects 0.000 description 2
- 230000001588 bifunctional effect Effects 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 201000003740 cowpox Diseases 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
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 229960000633 dextran sulfate Drugs 0.000 description 2
- 238000011026 diafiltration Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 239000005546 dideoxynucleotide Substances 0.000 description 2
- PSLWZOIUBRXAQW-UHFFFAOYSA-M dimethyl(dioctadecyl)azanium;bromide Chemical compound [Br-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CCCCCCCCCCCCCCCCCC PSLWZOIUBRXAQW-UHFFFAOYSA-M 0.000 description 2
- 108700003601 dimethylglycine Proteins 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 235000019253 formic acid Nutrition 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 229960002989 glutamic acid Drugs 0.000 description 2
- 208000002672 hepatitis B Diseases 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000003308 immunostimulating effect Effects 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 229910052500 inorganic mineral Inorganic materials 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 244000000010 microbial pathogen Species 0.000 description 2
- 239000004005 microsphere Substances 0.000 description 2
- 239000011707 mineral Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 238000012261 overproduction Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 229920001983 poloxamer Polymers 0.000 description 2
- 229920000768 polyamine Polymers 0.000 description 2
- 229920005862 polyol Polymers 0.000 description 2
- 150000003077 polyols Chemical class 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000002062 proliferating effect Effects 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000004007 reversed phase HPLC Methods 0.000 description 2
- 230000000405 serological effect Effects 0.000 description 2
- 229910001961 silver nitrate Inorganic materials 0.000 description 2
- 239000002002 slurry Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 229940031626 subunit vaccine Drugs 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- DLYUQMMRRRQYAE-UHFFFAOYSA-N tetraphosphorus decaoxide Chemical compound O1P(O2)(=O)OP3(=O)OP1(=O)OP2(=O)O3 DLYUQMMRRRQYAE-UHFFFAOYSA-N 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- 230000005026 transcription initiation Effects 0.000 description 2
- 230000014621 translational initiation Effects 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
- IESDGNYHXIOKRW-LEOABGAYSA-N tuftsin Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@H](CCCNC(N)=N)C(O)=O IESDGNYHXIOKRW-LEOABGAYSA-N 0.000 description 2
- 229940035670 tuftsin Drugs 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 101150084750 1 gene Proteins 0.000 description 1
- ASOKPJOREAFHNY-UHFFFAOYSA-N 1-Hydroxybenzotriazole Chemical compound C1=CC=C2N(O)N=NC2=C1 ASOKPJOREAFHNY-UHFFFAOYSA-N 0.000 description 1
- 101150028074 2 gene Proteins 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- OGMADIBCHLQMIP-UHFFFAOYSA-N 2-aminoethanethiol;hydron;chloride Chemical compound Cl.NCCS OGMADIBCHLQMIP-UHFFFAOYSA-N 0.000 description 1
- LYFYWXLKKQIOKO-UHFFFAOYSA-N 3,3-diaminopentan-1-ol Chemical compound CCC(N)(N)CCO LYFYWXLKKQIOKO-UHFFFAOYSA-N 0.000 description 1
- WKALLSVICJPZTM-UHFFFAOYSA-N 3-[decyl(dimethyl)azaniumyl]propane-1-sulfonate Chemical compound CCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O WKALLSVICJPZTM-UHFFFAOYSA-N 0.000 description 1
- 101150096316 5 gene Proteins 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
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241001167018 Aroa Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000031504 Asymptomatic Infections Diseases 0.000 description 1
- 108020000946 Bacterial DNA Proteins 0.000 description 1
- 101100346198 Caenorhabditis elegans mpc-2 gene Proteins 0.000 description 1
- 101710197658 Capsid protein VP1 Proteins 0.000 description 1
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical compound [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108091033380 Coding strand Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 108010060123 Conjugate Vaccines Proteins 0.000 description 1
- 201000007336 Cryptococcosis Diseases 0.000 description 1
- 241000221204 Cryptococcus neoformans Species 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- 238000007900 DNA-DNA hybridization Methods 0.000 description 1
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 description 1
- 101100491986 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) aromA gene Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 241000606768 Haemophilus influenzae Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 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
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-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
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 108010054278 Lac Repressors Proteins 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
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 206010027202 Meningitis bacterial Diseases 0.000 description 1
- 208000010495 Meningocele Diseases 0.000 description 1
- 241000588655 Moraxella catarrhalis Species 0.000 description 1
- 241000872931 Myoporum sandwicense Species 0.000 description 1
- 229940124912 Neisseria meningitidis vaccine Drugs 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 101150063378 OMP gene Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 201000005702 Pertussis Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 101710118046 RNA-directed RNA polymerase Proteins 0.000 description 1
- 241000725643 Respiratory syncytial virus Species 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 241000702670 Rotavirus Species 0.000 description 1
- 239000012506 Sephacryl® Substances 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 206010043376 Tetanus Diseases 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 241000700647 Variola virus Species 0.000 description 1
- 101710108545 Viral protein 1 Proteins 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- PMZXXNPJQYDFJX-UHFFFAOYSA-N acetonitrile;2,2,2-trifluoroacetic acid Chemical compound CC#N.OC(=O)C(F)(F)F PMZXXNPJQYDFJX-UHFFFAOYSA-N 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 101150037081 aroA gene Proteins 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 150000001510 aspartic acids Chemical class 0.000 description 1
- 238000007846 asymmetric PCR Methods 0.000 description 1
- 108010042854 bacteria histone-like protein HU Proteins 0.000 description 1
- 201000009904 bacterial meningitis Diseases 0.000 description 1
- 239000013602 bacteriophage vector Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000006161 blood agar Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000000337 buffer salt Substances 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- 210000004900 c-terminal fragment Anatomy 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 239000003093 cationic surfactant Substances 0.000 description 1
- 238000001516 cell proliferation assay Methods 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 229940031670 conjugate vaccine Drugs 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000011969 continuous reassessment method Methods 0.000 description 1
- 101150044687 crm gene Proteins 0.000 description 1
- 101150054175 cro gene Proteins 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000003381 deacetylation reaction Methods 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- 206010013023 diphtheria Diseases 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
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 150000002307 glutamic acids Chemical class 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 235000004554 glutamine Nutrition 0.000 description 1
- 244000000058 gram-negative pathogen Species 0.000 description 1
- 239000001307 helium Substances 0.000 description 1
- 229910052734 helium Inorganic materials 0.000 description 1
- SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 1
- 238000000703 high-speed centrifugation Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 210000005104 human peripheral blood lymphocyte Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 238000002169 hydrotherapy Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000006054 immunological memory Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 201000004792 malaria Diseases 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000010436 membrane biogenesis Effects 0.000 description 1
- 210000002418 meninge Anatomy 0.000 description 1
- 229940124731 meningococcal vaccine Drugs 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- HEGSGKPQLMEBJL-RKQHYHRCSA-N octyl beta-D-glucopyranoside Chemical compound CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RKQHYHRCSA-N 0.000 description 1
- 101150073640 ompF gene Proteins 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 239000000863 peptide conjugate Substances 0.000 description 1
- 238000012510 peptide mapping method Methods 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 108010083127 phage repressor proteins Proteins 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229940031937 polysaccharide vaccine Drugs 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000003156 radioimmunoprecipitation Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 235000004400 serine Nutrition 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000004513 sizing Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- NRHMKIHPTBHXPF-TUJRSCDTSA-M sodium cholate Chemical compound [Na+].C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 NRHMKIHPTBHXPF-TUJRSCDTSA-M 0.000 description 1
- BEOOHQFXGBMRKU-UHFFFAOYSA-N sodium cyanoborohydride Chemical compound [Na+].[B-]C#N BEOOHQFXGBMRKU-UHFFFAOYSA-N 0.000 description 1
- FHHPUSMSKHSNKW-SMOYURAASA-M sodium deoxycholate Chemical compound [Na+].C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 FHHPUSMSKHSNKW-SMOYURAASA-M 0.000 description 1
- HHSGWIABCIVPJT-UHFFFAOYSA-M sodium;1-[4-[(2-iodoacetyl)amino]benzoyl]oxy-2,5-dioxopyrrolidine-3-sulfonate Chemical compound [Na+].O=C1C(S(=O)(=O)[O-])CC(=O)N1OC(=O)C1=CC=C(NC(=O)CI)C=C1 HHSGWIABCIVPJT-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 238000010399 three-hybrid screening Methods 0.000 description 1
- 235000008521 threonine Nutrition 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 235000002374 tyrosine Nutrition 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 239000012646 vaccine adjuvant Substances 0.000 description 1
- 229940124931 vaccine adjuvant Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 244000052613 viral pathogen Species 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 239000002888 zwitterionic surfactant Substances 0.000 description 1
Classifications
-
- 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
- A61K39/095—Neisseria
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/22—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Neisseriaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K14/255—Salmonella (G)
-
- 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
- C07K16/1217—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Neisseriaceae (F)
-
- 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]
-
- 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
- A61K2039/6068—Other bacterial proteins, e.g. OMP
-
- 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
- A61K2039/6081—Albumin; Keyhole limpet haemocyanin [KLH]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Pharmacology & Pharmacy (AREA)
- Oncology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Communicable Diseases (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8803111A NL8803111A (nl) | 1988-12-19 | 1988-12-19 | Multivalent meningococcen klasse i buitenmembraaneiwit vaccin. |
| NL8900036A NL8900036A (nl) | 1988-12-19 | 1989-01-06 | Multivalent meningococcen klasse 1 buitenmembraaneiwit vaccin. |
| NL8901612A NL8901612A (nl) | 1988-12-19 | 1989-06-26 | Multivalent meningococcen klasse i buitenmembraaneiwit vaccin. |
| PCT/US1989/005678 WO1990006696A2 (en) | 1988-12-19 | 1989-12-19 | Meningococcal class 1 outer-membrane protein vaccine |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO912369D0 NO912369D0 (no) | 1991-06-18 |
| NO912369L NO912369L (no) | 1991-08-06 |
| NO305463B1 true NO305463B1 (no) | 1999-06-07 |
Family
ID=27352237
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO912369A NO305463B1 (no) | 1988-12-19 | 1991-06-18 | FremgangsmÕte for fremstilling av en vaksine mot Neisseria meningitidis, klasse 2/3 minusmutant av Neisseria Neisseria meningitidis stamme, samt mikroorganisme som uttrykker et fusjonsprotein |
Country Status (10)
| Country | Link |
|---|---|
| EP (1) | EP0449958B9 (de) |
| JP (1) | JP3436756B2 (de) |
| AT (1) | ATE120093T1 (de) |
| AU (1) | AU640118B2 (de) |
| DE (1) | DE68921895T3 (de) |
| DK (1) | DK175788B1 (de) |
| ES (1) | ES2070312T5 (de) |
| FI (1) | FI113009B (de) |
| NO (1) | NO305463B1 (de) |
| WO (1) | WO1990006696A2 (de) |
Families Citing this family (82)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7118757B1 (en) * | 1988-12-19 | 2006-10-10 | Wyeth Holdings Corporation | Meningococcal class 1 outer-membrane protein vaccine |
| NZ239643A (en) * | 1990-09-17 | 1996-05-28 | North American Vaccine Inc | Vaccine containing bacterial polysaccharide protein conjugate and adjuvant (c-nd-che-a-co-b-r) with a long chain alkyl group. |
| WO1993018150A1 (en) | 1992-03-02 | 1993-09-16 | Biocine S.P.A. | Helicobacter pylori proteins useful for vaccines and diagnostics |
| NL9201716A (nl) * | 1992-10-02 | 1994-05-02 | Nederlanden Staat | Buitenmembraanvesikel dat voorzien is van een groep polypeptiden welke ten minste de immuunwerking van aan membraan gebonden buitenmembraaneiwitten (OMP's) hebben, werkwijze ter bereiding ervan alsmede een vaccin dat een dergelijk buitenmembraanvesikel omvat. |
| CA2147877A1 (en) * | 1992-10-26 | 1994-05-11 | Robert J. Arko | Immunization against neisseria gonorrhoeae and neisseria meningitidis |
| EP0624376B1 (de) | 1993-05-13 | 2000-03-15 | American Cyanamid Company | Herstellung und Verwendungen von LOS-verminderten Aussenmembran-Proteinen von Gram-negativen Kokken |
| US5439808A (en) * | 1993-07-23 | 1995-08-08 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane group B porin proteins from Neisseria meningitidis |
| US6153406A (en) * | 1993-07-23 | 2000-11-28 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane protein P2 from Haemophilus influenzae type B |
| US5747287A (en) * | 1995-04-28 | 1998-05-05 | North American Vaccine, Inc. | Method for the high level expression, purification and refolding of the outer membrane group B porin proteins from Neisseria meningitidis |
| US5811102A (en) | 1995-06-07 | 1998-09-22 | National Research Council Of Canada | Modified meningococcal polysaccharide conjugate vaccines |
| US20020028215A1 (en) | 1999-08-09 | 2002-03-07 | Jagath L. Kadurugamuwa | Novel vaccines and pharmaceutical compositions using membrane vesicles of microorganisms, and methods for preparing same |
| CA2182637A1 (en) * | 1995-08-04 | 1997-02-05 | Jagath L. Kadurugamuwa | Novel vaccines and pharmaceutical compositions using membrane vesicles of microorganisms, and methods for preparing them |
| DK0854729T3 (da) * | 1995-09-18 | 2004-07-12 | Id Biomedical Corp Quebec | Forbedrede fremgangsmåder til fremstillingen af ikke-kovalent kompleksdannede og multivalente proteosom-subunit-vacciner |
| ES2283012T3 (es) | 1996-01-04 | 2007-10-16 | Novartis Vaccines And Diagnostics, Inc. | Bacterioferritina de helicobacter pylori. |
| GB9611673D0 (en) * | 1996-06-05 | 1996-08-07 | Peptide Therapeutics Ltd | Meningococcal vaccine |
| WO1998008874A1 (en) * | 1996-08-27 | 1998-03-05 | Chiron Corporation | Monoclonal antibodies that define unique meningococcal b epitopes and their use in the preparation of vaccine compositions |
| US6558677B2 (en) * | 1996-10-15 | 2003-05-06 | Wendell D. Zollinger | Vaccine against gram negative bacteria |
| GB9701489D0 (en) * | 1997-01-24 | 1997-03-12 | Auspharm Int Ltd | Antigen |
| ES2294629T3 (es) * | 1998-05-01 | 2008-04-01 | Novartis Vaccines And Diagnostics, Inc. | Antigenos de neisseria y composiciones. |
| EP2796148A3 (de) * | 1998-05-29 | 2015-02-25 | Novartis Vaccines and Diagnostics, Inc. | Kombinierte Meningitis B/C-Impfstoffe |
| EP1741443B1 (de) * | 1998-05-29 | 2014-05-21 | Novartis Vaccines and Diagnostics, Inc. | Kombinierte Meningitis B/C Impfstoffe |
| AU2003213540B8 (en) * | 1998-05-29 | 2006-09-28 | Novartis Vaccines And Diagnostic Inc. | Combination meningitidis B/C vaccines |
| GB9814902D0 (en) * | 1998-07-10 | 1998-09-09 | Univ Nottingham | Screening of neisserial vaccine candidates against pathogenic neisseria |
| US7252828B2 (en) | 1998-07-15 | 2007-08-07 | The Brigham And Women's Hospital, Inc. | Polysaccharide vaccine for staphylococcal infections |
| US6756493B1 (en) | 1998-09-01 | 2004-06-29 | Antex Biologics, Inc. | Nucleic acid sequence and uses thereof |
| US6693186B2 (en) | 1998-09-01 | 2004-02-17 | Antex Biologics Inc | Neisseria meningitidis polypeptide, nucleic acid sequence and uses thereof |
| GB9823978D0 (en) * | 1998-11-02 | 1998-12-30 | Microbiological Res Authority | Multicomponent meningococcal vaccine |
| US10967045B2 (en) | 1998-11-02 | 2021-04-06 | Secretary of State for Health and Social Care | Multicomponent meningococcal vaccine |
| CA2359492A1 (en) * | 1999-01-15 | 2000-07-20 | Smithkline Beecham Biologicals S.A. | Neisseria meningitidis antigen |
| ES2397918T3 (es) | 1999-04-30 | 2013-03-12 | Novartis Vaccines And Diagnostics S.R.L. | Antígenos Neisseriales conservados |
| EP1069133A1 (de) * | 1999-07-13 | 2001-01-17 | Institut National De La Sante Et De La Recherche Medicale (Inserm) | Neisseria meningitidis Zusammensetzungen und ihre Verwendungen als anti-infektionsmitteln |
| GB9916529D0 (en) | 1999-07-14 | 1999-09-15 | Chiron Spa | Antigenic peptides |
| GB9918319D0 (en) * | 1999-08-03 | 1999-10-06 | Smithkline Beecham Biolog | Vaccine composition |
| EP2275551B1 (de) * | 1999-10-29 | 2015-04-08 | Novartis Vaccines and Diagnostics S.r.l. | Antigenpeptide aus Neisseria |
| BR0015961A (pt) * | 1999-11-29 | 2003-06-10 | Chiron Spa | Antìgeno de neisseria de 85kda |
| GB9928196D0 (en) | 1999-11-29 | 2000-01-26 | Chiron Spa | Combinations of B, C and other antigens |
| EP1112747B1 (de) * | 1999-12-28 | 2004-06-16 | Akzo Nobel N.V. | Salmonella Impfstoff, der keinen Antikörper gegen Flagellin oder gegen Flagella induziert |
| BR0107679A (pt) * | 2000-01-17 | 2004-07-06 | Chiron Spa | Vacina de vesìcula de membrana externa (omv) compreendendo proteìnas de membrana externa do grupo sérico b de neisseria meningitidis |
| AU2818101A (en) * | 2000-01-25 | 2001-08-07 | University Of Queensland, The | proteins comprising conserved regions of neisseria meningitidis surface antigen NhhA |
| EP1790660B1 (de) | 2000-02-28 | 2012-06-20 | Novartis Vaccines and Diagnostics S.r.l. | Heterologe Expression von Neisseria Proteinen |
| BRPI0112928B1 (pt) | 2000-07-27 | 2017-08-29 | Children's Hospital & Research Center At Oakland | A composition comprising preparations comprising outer membrane vesicles (OMV), microvesicles (MV) or both MVO and MV |
| GB0103170D0 (en) * | 2001-02-08 | 2001-03-28 | Smithkline Beecham Biolog | Vaccine composition |
| YU66103A (sh) * | 2001-01-23 | 2006-05-25 | Aventis Pasteur | Vakcina multivalentnog konjugata meningokokalnog polisaharid-proteina |
| JP2004529643A (ja) | 2001-04-17 | 2004-09-30 | カイロン コーポレイション | 機能活性抗体を誘発する髄膜炎菌性ｂエピトープの分子模倣物 |
| GB0115176D0 (en) | 2001-06-20 | 2001-08-15 | Chiron Spa | Capular polysaccharide solubilisation and combination vaccines |
| GB0118249D0 (en) | 2001-07-26 | 2001-09-19 | Chiron Spa | Histidine vaccines |
| GB0121591D0 (en) | 2001-09-06 | 2001-10-24 | Chiron Spa | Hybrid and tandem expression of neisserial proteins |
| GB0130123D0 (en) | 2001-12-17 | 2002-02-06 | Microbiological Res Agency | Outer membrane vesicle vaccine and its preparation |
| US7405039B2 (en) | 2002-02-07 | 2008-07-29 | Austin Health | Viral variants with altered susceptibility to nucleoside analogs and uses thereof |
| EP2455390A1 (de) | 2002-04-12 | 2012-05-23 | Melbourne Health | Hepatitis-B-Virusvarianten mit reduzierter Suszeptibilität für Nukleosidanaloga und Verwendungen dafür |
| GB0220194D0 (en) | 2002-08-30 | 2002-10-09 | Chiron Spa | Improved vesicles |
| CN1809380B (zh) | 2002-10-11 | 2010-05-12 | 启龙有限公司 | 广泛防御高毒性脑膜炎球菌谱系的多肽-疫苗 |
| WO2004043405A2 (en) | 2002-11-12 | 2004-05-27 | The Brigham And Women's Hospital, Inc. | Polysaccharide vaccine for staphylococcal infections |
| WO2004043407A2 (en) | 2002-11-12 | 2004-05-27 | The Brigham And Women's Hospital, Inc. | Methods and products for treating staphylococcal infections |
| US20070059329A1 (en) | 2002-11-15 | 2007-03-15 | Nathalie Norais | Unexpected surface proteins in meningococcus |
| GB0227346D0 (en) | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
| CN102319427A (zh) | 2003-01-30 | 2012-01-18 | 诺华疫苗和诊断有限公司 | 抗多种脑膜炎球菌血清组的可注射性疫苗 |
| GB0323103D0 (en) | 2003-10-02 | 2003-11-05 | Chiron Srl | De-acetylated saccharides |
| WO2005042564A1 (en) * | 2003-10-20 | 2005-05-12 | Sidney Kimmel Cancer Center | Flagellin fusion proteins as adjuvants or vaccines and methods of use |
| EP2468769A1 (de) | 2004-04-21 | 2012-06-27 | The Brigham and Women's Hospital, Inc. | Poly-N-acetylglucosamin (PNAG/DPNAG)-bindenden Peptide und Verwendungsverfahren dafür |
| GB0408977D0 (en) | 2004-04-22 | 2004-05-26 | Chiron Srl | Immunising against meningococcal serogroup Y using proteins |
| GB0424092D0 (en) | 2004-10-29 | 2004-12-01 | Chiron Srl | Immunogenic bacterial vesicles with outer membrane proteins |
| EP2433647A3 (de) | 2005-01-27 | 2012-06-06 | Children's Hospital & Research Center at Oakland | Gna1870-basierte vesikelimpfstoffe für breitbandschutz gegen neisseria meningitidis-bedingte erkrankungen |
| US8211443B2 (en) | 2005-04-08 | 2012-07-03 | Melbourne Health | Variants of hepatitis B virus with resistance to anti-viral nucleoside agents and applications thereof |
| WO2006105597A1 (en) | 2005-04-08 | 2006-10-12 | Melbourne Health | Variants of hepatitis b virus with resistance to anti-viral nucleoside agents and applications thereof |
| GB0524066D0 (en) | 2005-11-25 | 2006-01-04 | Chiron Srl | 741 ii |
| GB0611914D0 (en) | 2006-06-15 | 2006-07-26 | Teti Giuseppe | Peptides that mimic non-human cross-reactive protective epitopes of the group Bmeningococcal capsulsar polysaccharide |
| NZ587382A (en) | 2008-02-21 | 2012-01-12 | Novartis Ag | Meningococcal fhbp polypeptides |
| GB0809659D0 (en) * | 2008-05-28 | 2008-07-02 | Univ Nottingham | Polypeptides |
| AU2009262893B2 (en) | 2008-05-30 | 2015-05-21 | The U.S.A., as represented by The Secretary of the Army, on behalf of Walter Reed Army Institute Of Research | Meningococcal multivalent native outer membrane vesicle vaccine, methods of making and use thereof |
| KR20110031393A (ko) | 2008-07-21 | 2011-03-25 | 더 브리검 앤드 우먼즈 하스피털, 인크. | 합성 베타-1,6 글루코사민 올리고당에 관한 방법 및 조성물 |
| WO2010027499A2 (en) * | 2008-09-05 | 2010-03-11 | University Of Massachusetts Medical School | Methods, compositions and vaccines relating to neisseria meningitidis antibodies |
| ES2562259T3 (es) | 2009-08-27 | 2016-03-03 | Glaxosmithkline Biologicals Sa | Polipéptidos híbridos que incluyen secuencias fHBP meningocócicas |
| CA2776004A1 (en) | 2009-09-30 | 2011-04-07 | Novartis Ag | Expression of meningococcal fhbp polypeptides |
| EP2493499A1 (de) | 2009-10-27 | 2012-09-05 | Novartis AG | Modifizierte meningokokken-fhbp-polypeptide |
| BR112013005626B1 (pt) | 2010-09-10 | 2022-07-26 | Glaxosmithkline Biologicals Sa | Meningococo, processo para a preparação de uma cepa meningocócica, vesículas de membrana externa, composição farmacêutica imunogênica, e, uso de uma composição |
| JP2012090571A (ja) * | 2010-10-27 | 2012-05-17 | Sekisui Chem Co Ltd | 動物の免疫方法、免疫用組成物、抗体の製造方法、並びに、ハイブリドーマの製造方法 |
| AU2013276083B2 (en) | 2012-06-14 | 2018-04-05 | Institut Pasteur | Vaccines for serogroup X meningococcus |
| CA2940447C (en) | 2014-02-28 | 2023-07-11 | Glaxosmithkline Biologicals Sa | Modified meningococcal fhbp polypeptides |
| US10870822B2 (en) * | 2014-04-17 | 2020-12-22 | Corning Incorporated | Vessel for growth of biological entities |
| BR112017001796A2 (pt) * | 2014-07-30 | 2018-02-14 | Cleveland Biolabs, Inc. | composições de flagelina e seus usos |
| JP2023542141A (ja) * | 2020-09-15 | 2023-10-05 | ザ ユニバーシティー オブ モンタナ | 繊維状バクテリオファージを標的化する組成物および方法 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4673574A (en) * | 1981-08-31 | 1987-06-16 | Anderson Porter W | Immunogenic conjugates |
| WO1983003354A1 (en) * | 1982-03-30 | 1983-10-13 | Us Army | Neisseria gonorrhoeae vaccine |
| EP0145359B1 (de) * | 1983-11-21 | 1991-01-16 | The Wellcome Foundation Limited | Komplexe, Verfahren zu ihrer Herstellung und dieselben enthaltende Formulierungen |
| US4601903A (en) * | 1985-05-01 | 1986-07-22 | The United States Of America As Represented By The Department Of Health And Human Services | Vaccine against Neisseria meningitidis Group B serotype 2 invasive disease |
| JPH01125328A (ja) * | 1987-07-30 | 1989-05-17 | Centro Natl De Biopreparados | 髄膜炎菌ワクチン |
| WO1989010967A1 (en) * | 1988-05-05 | 1989-11-16 | Praxis Biologics, Inc. | Recombinant flagellin vaccines |
-
1989
- 1989-12-19 EP EP90901397A patent/EP0449958B9/de not_active Expired - Lifetime
- 1989-12-19 AT AT90901397T patent/ATE120093T1/de not_active IP Right Cessation
- 1989-12-19 WO PCT/US1989/005678 patent/WO1990006696A2/en active IP Right Grant
- 1989-12-19 ES ES90901397T patent/ES2070312T5/es not_active Expired - Lifetime
- 1989-12-19 AU AU48219/90A patent/AU640118B2/en not_active Expired
- 1989-12-19 JP JP50166290A patent/JP3436756B2/ja not_active Expired - Lifetime
- 1989-12-19 DE DE68921895T patent/DE68921895T3/de not_active Expired - Lifetime
-
1991
- 1991-06-18 NO NO912369A patent/NO305463B1/no not_active IP Right Cessation
- 1991-06-18 FI FI912965A patent/FI113009B/fi active
- 1991-06-18 DK DK199101174A patent/DK175788B1/da not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| JPH06503465A (ja) | 1994-04-21 |
| AU640118B2 (en) | 1993-08-19 |
| DE68921895T2 (de) | 1995-09-07 |
| NO912369L (no) | 1991-08-06 |
| EP0449958B1 (de) | 1995-03-22 |
| FI912965A0 (fi) | 1991-06-18 |
| DK117491A (da) | 1991-08-15 |
| WO1990006696A2 (en) | 1990-06-28 |
| DE68921895D1 (de) | 1995-04-27 |
| DK117491D0 (da) | 1991-06-18 |
| EP0449958B9 (de) | 2003-05-28 |
| WO1990006696A3 (en) | 1990-07-12 |
| EP0449958A1 (de) | 1991-10-09 |
| AU4821990A (en) | 1990-07-10 |
| ES2070312T5 (es) | 2003-05-16 |
| ATE120093T1 (de) | 1995-04-15 |
| FI113009B (fi) | 2004-02-27 |
| DE68921895T3 (de) | 2003-05-22 |
| DK175788B1 (da) | 2005-02-21 |
| JP3436756B2 (ja) | 2003-08-18 |
| EP0449958B2 (de) | 2002-11-13 |
| ES2070312T3 (es) | 1995-06-01 |
| NO912369D0 (no) | 1991-06-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO305463B1 (no) | FremgangsmÕte for fremstilling av en vaksine mot Neisseria meningitidis, klasse 2/3 minusmutant av Neisseria Neisseria meningitidis stamme, samt mikroorganisme som uttrykker et fusjonsprotein | |
| US7238345B1 (en) | Recombinant microorganism expressing meningococcal class 1 outer membrane protein | |
| Martin et al. | Highly conserved Neisseria meningitidis surface protein confers protection against experimental infection | |
| Barlow et al. | The class 1 outer membrane protein of Neisseria meningitidis: gene sequence and structural and immunological similarities to gonococcal porins | |
| CA2215161C (en) | Proteinase k resistant surface protein of neisseria meningitidis | |
| US7786286B2 (en) | Proteinase K resistant surface protein of Neisseria meningitidis | |
| JP5566684B2 (ja) | Ｃｌｏｓｔｒｉｄｉｕｍｄｉｆｆｉｃｉｌｅに対する、組換え毒素Ａ／毒素Ｂワクチン | |
| NO321651B1 (no) | Immunogent meningokokk-lipopoly-sakkarid, ytter-membranvesikler, samt vaksine fremstilt derav. | |
| JP2011168611A (ja) | 髄膜炎菌類タンパク質ｎｍｂ１８７０のドメインおよびエピトープ | |
| NO302031B1 (no) | Rekombinant gen omfattende en nukleotidsekvens som koder for et flagellinfusjonsprotein, genmodifisert mikroorganisme omfattende det rekombinante genet og fremgangsmåte for ekspresjon av det | |
| KR20230035455A (ko) | 변형된 수막구균 fhbp 폴리펩티드 | |
| van der Ley et al. | Use of transformation to construct antigenic hybrids of the class 1 outer membrane protein in Neisseria meningitidis | |
| Haeuw et al. | The recombinant Klebsiella pneumoniae outer membrane protein OmpA has carrier properties for conjugated antigenic peptides | |
| Ciabattini et al. | Intranasal immunization of mice with recombinant Streptococcus gordonii expressing NadA of Neisseria meningitidis induces systemic bactericidal antibodies and local IgA | |
| Tagawa et al. | Purification and partial characterization of the major outer membrane protein of Haemophilus somnus | |
| US5985288A (en) | Outer membrane protein P1 and peptides of Haemophilus influenzae type B | |
| EP1572729B1 (de) | Frpb proteinmutante und verfahren zur erneuten faltung | |
| CA3035159A1 (en) | Modified factor h binding protein | |
| CA2007248C (en) | Meningococcal class 1 outer-membrane protein vaccine | |
| AU2015321698B2 (en) | Combined enterotoxigenic Escherichia coli and Campylobacter jejuni recombinant construct | |
| AU695173B2 (en) | Novel opacity associated proteins, DNA encoding the same, and methods of use thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK1K | Patent expired |