AU668075B2 - Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes - Google Patents

Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes

Info

Publication number: AU668075B2
Authority: AU; Australia
Prior art keywords: outer membrane; membrane protein; protein; methods; neisseria meningitidis
Prior art date: 1990-07-06
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Fee Related

Application number

AU81873/91A

Other languages

English (en)

Other versions

AU8187391A (en

Inventor

Sarah Butcher

Ilona Idanpaan-Heikkila

Susanna Muttilainen

Marjatta Nurminen-Kalliokoski

Ritvaleena Puohiniemi

Kate Runeberg-Nyman

Matti Sarvas

Eva Wahlstrom

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Finnish National Public Health Institute

Original Assignee

Finnish National Public Health Institute

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1990-07-06

Filing date

1991-07-05

Publication date

1996-04-26

1991-07-05 Application filed by Finnish National Public Health Institute filed Critical Finnish National Public Health Institute

1992-02-04 Publication of AU8187391A publication Critical patent/AU8187391A/en

1996-04-26 Application granted granted Critical

1996-04-26 Publication of AU668075B2 publication Critical patent/AU668075B2/en

2011-07-05 Anticipated expiration legal-status Critical

Status Expired - Fee Related legal-status Critical Current

Links

238000004519 manufacturing process Methods 0.000 title claims description 24
239000012528 membrane Substances 0.000 title claims description 19
108090000623 proteins and genes Proteins 0.000 title description 113
102000004169 proteins and genes Human genes 0.000 title description 103
230000001681 protective effect Effects 0.000 title description 19
238000011084 recovery Methods 0.000 title description 6
241000192125 Firmicutes Species 0.000 title description 5
238000000034 method Methods 0.000 claims description 59
101710116435 Outer membrane protein Proteins 0.000 claims description 51
241000894006 Bacteria Species 0.000 claims description 44
241000588650 Neisseria meningitidis Species 0.000 claims description 25
241001465754 Metazoa Species 0.000 claims description 20
108091028043 Nucleic acid sequence Proteins 0.000 claims description 18
230000000844 anti-bacterial effect Effects 0.000 claims description 17
108020004414 DNA Proteins 0.000 claims description 16
208000015181 infectious disease Diseases 0.000 claims description 16
230000001717 pathogenic effect Effects 0.000 claims description 16
239000003795 chemical substances by application Substances 0.000 claims description 15
229960000789 guanidine hydrochloride Drugs 0.000 claims description 14
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims description 14
229960005486 vaccine Drugs 0.000 claims description 14
241000193830 Bacillus <bacterium> Species 0.000 claims description 13
239000000203 mixture Substances 0.000 claims description 12
235000014469 Bacillus subtilis Nutrition 0.000 claims description 11
230000001580 bacterial effect Effects 0.000 claims description 11
244000063299 Bacillus subtilis Species 0.000 claims description 10
239000004202 carbamide Substances 0.000 claims description 10
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 9
229940016590 sarkosyl Drugs 0.000 claims description 8
108700004121 sarkosyl Proteins 0.000 claims description 8
KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 claims description 8
241000124008 Mammalia Species 0.000 claims description 4
XQSBLCWFZRTIEO-UHFFFAOYSA-N hexadecan-1-amine;hydrobromide Chemical compound [Br-].CCCCCCCCCCCCCCCC[NH3+] XQSBLCWFZRTIEO-UHFFFAOYSA-N 0.000 claims description 4
241000508772 Brucella sp. Species 0.000 claims description 3
241000588652 Neisseria gonorrhoeae Species 0.000 claims description 3
241000131891 Yersinia sp. Species 0.000 claims description 3
239000002552 dosage form Substances 0.000 claims description 3
239000012678 infectious agent Substances 0.000 claims description 3
239000003755 preservative agent Substances 0.000 claims description 3
239000003153 chemical reaction reagent Substances 0.000 claims description 2
230000001900 immune effect Effects 0.000 claims description 2
150000003904 phospholipids Chemical class 0.000 claims description 2
IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 claims 2
229940067606 lecithin Drugs 0.000 claims 2
239000000787 lecithin Substances 0.000 claims 2
235000010445 lecithin Nutrition 0.000 claims 2
229940045136 urea Drugs 0.000 claims 2
CPELXLSAUQHCOX-UHFFFAOYSA-M Bromide Chemical compound [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 claims 1
241000606768 Haemophilus influenzae Species 0.000 claims 1
230000000890 antigenic effect Effects 0.000 claims 1
229940047650 haemophilus influenzae Drugs 0.000 claims 1
229940067631 phospholipid Drugs 0.000 claims 1
108010079246 OMPA outer membrane proteins Proteins 0.000 description 32
239000002158 endotoxin Substances 0.000 description 32
229920006008 lipopolysaccharide Polymers 0.000 description 30
210000003000 inclusion body Anatomy 0.000 description 19
239000013612 plasmid Substances 0.000 description 19
239000012634 fragment Substances 0.000 description 18
230000014509 gene expression Effects 0.000 description 16
230000003053 immunization Effects 0.000 description 15
239000008188 pellet Substances 0.000 description 15
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 15
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 14
239000003599 detergent Substances 0.000 description 14
210000004027 cell Anatomy 0.000 description 13
238000002360 preparation method Methods 0.000 description 13
108090000765 processed proteins & peptides Proteins 0.000 description 13
230000033228 biological regulation Effects 0.000 description 12
238000005119 centrifugation Methods 0.000 description 12
238000002649 immunization Methods 0.000 description 12
239000013598 vector Substances 0.000 description 12
241000588724 Escherichia coli Species 0.000 description 10
241000699670 Mus sp. Species 0.000 description 10
102000004196 processed proteins & peptides Human genes 0.000 description 10
239000000523 sample Substances 0.000 description 10
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 9
229920001184 polypeptide Polymers 0.000 description 9
235000019333 sodium laurylsulphate Nutrition 0.000 description 9
239000006228 supernatant Substances 0.000 description 9
238000003556 assay Methods 0.000 description 8
101710167887 Major outer membrane protein P.IA Proteins 0.000 description 7
108010076504 Protein Sorting Signals Proteins 0.000 description 7
239000000427 antigen Substances 0.000 description 7
102000036639 antigens Human genes 0.000 description 7
108091007433 antigens Proteins 0.000 description 7
210000004201 immune sera Anatomy 0.000 description 7
229940042743 immune sera Drugs 0.000 description 7
239000002773 nucleotide Substances 0.000 description 7
125000003729 nucleotide group Chemical group 0.000 description 7
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 6
230000003196 chaotropic effect Effects 0.000 description 6
238000010276 construction Methods 0.000 description 6
238000010790 dilution Methods 0.000 description 6
239000012895 dilution Substances 0.000 description 6
238000002347 injection Methods 0.000 description 6
239000007924 injection Substances 0.000 description 6
229930027917 kanamycin Natural products 0.000 description 6
229960000318 kanamycin Drugs 0.000 description 6
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 6
229930182823 kanamycin A Natural products 0.000 description 6
238000000746 purification Methods 0.000 description 6
210000002966 serum Anatomy 0.000 description 6
241000282412 Homo Species 0.000 description 5
241001625930 Luria Species 0.000 description 5
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 4
102000004190 Enzymes Human genes 0.000 description 4
108090000790 Enzymes Proteins 0.000 description 4
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
102000016943 Muramidase Human genes 0.000 description 4
108010014251 Muramidase Proteins 0.000 description 4
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 4
108091034117 Oligonucleotide Proteins 0.000 description 4
108020004511 Recombinant DNA Proteins 0.000 description 4
150000001413 amino acids Chemical class 0.000 description 4
239000000872 buffer Substances 0.000 description 4
230000003834 intracellular effect Effects 0.000 description 4
238000007912 intraperitoneal administration Methods 0.000 description 4
229960000274 lysozyme Drugs 0.000 description 4
239000004325 lysozyme Substances 0.000 description 4
235000010335 lysozyme Nutrition 0.000 description 4
238000012986 modification Methods 0.000 description 4
230000004048 modification Effects 0.000 description 4
238000003752 polymerase chain reaction Methods 0.000 description 4
238000004153 renaturation Methods 0.000 description 4
239000011780 sodium chloride Substances 0.000 description 4
239000000725 suspension Substances 0.000 description 4
238000012360 testing method Methods 0.000 description 4
229920001817 Agar Polymers 0.000 description 3
238000011537 Coomassie blue staining Methods 0.000 description 3
102000053602 DNA Human genes 0.000 description 3
201000009906 Meningitis Diseases 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
108700006385 OmpF Proteins 0.000 description 3
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
239000008272 agar Substances 0.000 description 3
125000000539 amino acid group Chemical group 0.000 description 3
230000000692 anti-sense effect Effects 0.000 description 3
239000002585 base Substances 0.000 description 3
238000006243 chemical reaction Methods 0.000 description 3
238000010367 cloning Methods 0.000 description 3
230000000694 effects Effects 0.000 description 3
229940088598 enzyme Drugs 0.000 description 3
238000000605 extraction Methods 0.000 description 3
238000010353 genetic engineering Methods 0.000 description 3
108020004707 nucleic acids Proteins 0.000 description 3
102000039446 nucleic acids Human genes 0.000 description 3
150000007523 nucleic acids Chemical class 0.000 description 3
239000000047 product Substances 0.000 description 3
230000003362 replicative effect Effects 0.000 description 3
108091008146 restriction endonucleases Proteins 0.000 description 3
238000005063 solubilization Methods 0.000 description 3
230000007928 solubilization Effects 0.000 description 3
231100000331 toxic Toxicity 0.000 description 3
230000002588 toxic effect Effects 0.000 description 3
230000009466 transformation Effects 0.000 description 3
238000005406 washing Methods 0.000 description 3
JLPULHDHAOZNQI-ZTIMHPMXSA-N 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCC\C=C/C\C=C/CCCCC JLPULHDHAOZNQI-ZTIMHPMXSA-N 0.000 description 2
208000031729 Bacteremia Diseases 0.000 description 2
108020004705 Codon Proteins 0.000 description 2
241000606790 Haemophilus Species 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
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 2
239000003513 alkali Substances 0.000 description 2
230000004071 biological effect Effects 0.000 description 2
239000002775 capsule Substances 0.000 description 2
210000000349 chromosome Anatomy 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
230000007423 decrease Effects 0.000 description 2
201000010099 disease Diseases 0.000 description 2
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
239000013604 expression vector Substances 0.000 description 2
230000036541 health Effects 0.000 description 2
210000000987 immune system Anatomy 0.000 description 2
238000003018 immunoassay Methods 0.000 description 2
238000003119 immunoblot Methods 0.000 description 2
238000012744 immunostaining Methods 0.000 description 2
230000005764 inhibitory process Effects 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
230000000813 microbial effect Effects 0.000 description 2
238000010369 molecular cloning Methods 0.000 description 2
231100000252 nontoxic Toxicity 0.000 description 2
230000003000 nontoxic effect Effects 0.000 description 2
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 2
230000008520 organization Effects 0.000 description 2
229940031937 polysaccharide vaccine Drugs 0.000 description 2
239000013641 positive control Substances 0.000 description 2
239000002244 precipitate Substances 0.000 description 2
125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
210000003705 ribosome Anatomy 0.000 description 2
239000012723 sample buffer Substances 0.000 description 2
108010073863 saruplase Proteins 0.000 description 2
238000012163 sequencing technique Methods 0.000 description 2
229940083466 soybean lecithin Drugs 0.000 description 2
241000894007 species Species 0.000 description 2
239000000126 substance Substances 0.000 description 2
238000012546 transfer Methods 0.000 description 2
230000001131 transforming effect Effects 0.000 description 2
238000001262 western blot Methods 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
101150084750 1 gene Proteins 0.000 description 1
QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-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
229920000936 Agarose Polymers 0.000 description 1
241000156724 Antirhea Species 0.000 description 1
241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
102000003813 Cis-trans-isomerases Human genes 0.000 description 1
108090000175 Cis-trans-isomerases Proteins 0.000 description 1
102000016911 Deoxyribonucleases Human genes 0.000 description 1
108010053770 Deoxyribonucleases Proteins 0.000 description 1
108010042407 Endonucleases Proteins 0.000 description 1
102000004533 Endonucleases Human genes 0.000 description 1
241000702190 Enterobacteria phage K3 Species 0.000 description 1
241001646716 Escherichia coli K-12 Species 0.000 description 1
239000012741 Laemmli sample buffer Substances 0.000 description 1
239000006137 Luria-Bertani broth Substances 0.000 description 1
FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
101710167885 Major outer membrane protein P.IB Proteins 0.000 description 1
208000034762 Meningococcal Infections Diseases 0.000 description 1
241000699666 Mus <mouse, genus> Species 0.000 description 1
241000588677 Neisseria meningitidis serogroup B Species 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
239000001888 Peptone Substances 0.000 description 1
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
239000012083 RIPA buffer Substances 0.000 description 1
241000700159 Rattus Species 0.000 description 1
241000700157 Rattus norvegicus Species 0.000 description 1
102000006382 Ribonucleases Human genes 0.000 description 1
108010083644 Ribonucleases Proteins 0.000 description 1
244000061456 Solanum tuberosum Species 0.000 description 1
235000002595 Solanum tuberosum Nutrition 0.000 description 1
241000191940 Staphylococcus Species 0.000 description 1
241000194017 Streptococcus Species 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
229930006000 Sucrose Natural products 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
238000002441 X-ray diffraction Methods 0.000 description 1
239000002253 acid Substances 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
102000004139 alpha-Amylases Human genes 0.000 description 1
108090000637 alpha-Amylases Proteins 0.000 description 1
229940024171 alpha-amylase Drugs 0.000 description 1
WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
229910021502 aluminium hydroxide Inorganic materials 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
238000004458 analytical method Methods 0.000 description 1
230000001948 anti-meningococcal effect Effects 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
230000008901 benefit Effects 0.000 description 1
238000002306 biochemical method Methods 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
150000001720 carbohydrates Chemical group 0.000 description 1
230000006037 cell lysis Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
238000007697 cis-trans-isomerization reaction Methods 0.000 description 1
239000007979 citrate buffer Substances 0.000 description 1
239000011248 coating agent Substances 0.000 description 1
238000000576 coating method Methods 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
230000034994 death Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000011161 development Methods 0.000 description 1
239000012470 diluted sample Substances 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
230000007613 environmental effect Effects 0.000 description 1
238000001502 gel electrophoresis Methods 0.000 description 1
102000034356 gene-regulatory proteins Human genes 0.000 description 1
108091006104 gene-regulatory proteins Proteins 0.000 description 1
239000011521 glass Substances 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
230000001571 immunoadjuvant effect Effects 0.000 description 1
230000002163 immunogen Effects 0.000 description 1
239000000568 immunological adjuvant Substances 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000001939 inductive effect Effects 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
239000010410 layer Substances 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
239000002502 liposome Substances 0.000 description 1
239000007788 liquid Substances 0.000 description 1
238000009630 liquid culture Methods 0.000 description 1
238000000464 low-speed centrifugation Methods 0.000 description 1
239000011777 magnesium Substances 0.000 description 1
229910052749 magnesium Inorganic materials 0.000 description 1
239000000463 material Substances 0.000 description 1
239000002609 medium Substances 0.000 description 1
244000005700 microbiome Species 0.000 description 1
230000003278 mimic effect Effects 0.000 description 1
238000002156 mixing Methods 0.000 description 1
210000004898 n-terminal fragment Anatomy 0.000 description 1
230000003204 osmotic effect Effects 0.000 description 1
239000011236 particulate material Substances 0.000 description 1
244000052769 pathogen Species 0.000 description 1
230000008506 pathogenesis Effects 0.000 description 1
238000002135 phase contrast microscopy Methods 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
230000008569 process Effects 0.000 description 1
230000012846 protein folding Effects 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
238000011552 rat model Methods 0.000 description 1
238000012216 screening Methods 0.000 description 1
239000013606 secretion vector Substances 0.000 description 1
230000035939 shock Effects 0.000 description 1
239000007787 solid Substances 0.000 description 1
230000003381 solubilizing effect Effects 0.000 description 1
239000000243 solution Substances 0.000 description 1
239000002904 solvent Substances 0.000 description 1
238000000527 sonication Methods 0.000 description 1
230000000087 stabilizing effect Effects 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
238000007920 subcutaneous administration Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
235000000346 sugar Nutrition 0.000 description 1
150000008163 sugars Chemical class 0.000 description 1
239000002344 surface layer Substances 0.000 description 1
RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
229960004906 thiomersal Drugs 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
238000013519 translation Methods 0.000 description 1
238000005829 trimerization reaction Methods 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
241001515965 unidentified phage Species 0.000 description 1
238000011179 visual inspection Methods 0.000 description 1
239000011534 wash buffer Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—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
- C07K14/245—Escherichia (G)
- 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
- 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
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/75—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Life Sciences & Earth Sciences (AREA)
General Health & Medical Sciences (AREA)
Biophysics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Engineering & Computer Science (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
General Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Biotechnology (AREA)
Biomedical Technology (AREA)
Zoology (AREA)
Bioinformatics & Cheminformatics (AREA)
Chemical Kinetics & Catalysis (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Plant Pathology (AREA)
Communicable Diseases (AREA)
Oncology (AREA)
Physics & Mathematics (AREA)
General Chemical & Material Sciences (AREA)
Microbiology (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Peptides Or Proteins (AREA)

AU81873/91A 1990-07-06 1991-07-05 Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes Expired - Fee Related AU668075B2 (en)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
FI903414		1990-07-06
FI903414A FI903414A (fi)	1990-07-06	1990-07-06	Produktion av proteiner i grampositiva bakterier.
PCT/FI1991/000212 WO1992001001A1 (en)	1990-07-06	1991-07-05	Production of outer membrane (om) proteins in gram-positive bacteria and recovery of protective epitopes

Related Child Applications (1)

Application Number	Title	Priority Date	Filing Date
AU60692/96A Division AU6069296A (en)	1990-07-06	1996-07-24	Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes

Publications (2)

Publication Number	Publication Date
AU8187391A AU8187391A (en)	1992-02-04
AU668075B2 true AU668075B2 (en)	1996-04-26

Family

ID=8530757

Family Applications (2)

Application Number	Title	Priority Date	Filing Date
AU81873/91A Expired - Fee Related AU668075B2 (en)	1990-07-06	1991-07-05	Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes
AU60692/96A Abandoned AU6069296A (en)	1990-07-06	1996-07-24	Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
AU60692/96A Abandoned AU6069296A (en)	1990-07-06	1996-07-24	Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes

Country Status (8)

Country	Link
EP (1)	EP0538318A1 (fi)
JP (1)	JPH06511140A (fi)
AU (2)	AU668075B2 (fi)
CA (1)	CA2086761A1 (fi)
FI (1)	FI903414A (fi)
IL (1)	IL98727A0 (fi)
WO (1)	WO1992001001A1 (fi)
ZA (1)	ZA915234B (fi)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
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
DE4401419C1 (de) *	1994-01-19	1994-12-22	Forschungszentrum Juelich Gmbh	Sekretion von Proteinen der äußeren Membran Gram-negativer Bakterien mittels Gram-positiver Wirtsorganismen
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
SE9702191D0 (sv) *	1997-06-09	1997-06-09	Sven Pettersson	Coposition and methods for the treatment of inflammatory dideases
FR2785293B1 (fr) *	1998-10-30	2002-07-05	Pasteur Merieux Serums Vacc	Acides nucleiques et polypeptides specifiques des souches pathogenes du genre neisseria

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2534529B2 (ja) *	1986-07-24	1996-09-18	ブリティシュ・テレコミュニケ−ションズ・パブリック・リミテッド・カンパニ	放射発生器
JPH02503196A (ja) *	1987-03-30	1990-10-04	ザ、テキサス、エー、エンド、エム、ユニバーシティ、システム	ブルセラ・アボルタスに対するワクチン

1990
- 1990-07-06 FI FI903414A patent/FI903414A/fi not_active Application Discontinuation
1991
- 1991-07-04 IL IL98727A patent/IL98727A0/xx unknown
- 1991-07-05 EP EP91912587A patent/EP0538318A1/en not_active Withdrawn
- 1991-07-05 JP JP3511658A patent/JPH06511140A/ja active Pending
- 1991-07-05 CA CA002086761A patent/CA2086761A1/en not_active Abandoned
- 1991-07-05 AU AU81873/91A patent/AU668075B2/en not_active Expired - Fee Related
- 1991-07-05 ZA ZA915234A patent/ZA915234B/xx unknown
- 1991-07-05 WO PCT/FI1991/000212 patent/WO1992001001A1/en not_active Application Discontinuation
1996
- 1996-07-24 AU AU60692/96A patent/AU6069296A/en not_active Abandoned

Also Published As

Publication number	Publication date
ZA915234B (en)	1993-02-24
IL98727A0 (en)	1992-07-15
AU6069296A (en)	1996-11-07
FI903414A0 (fi)	1990-07-06
FI903414A (fi)	1992-01-07
WO1992001001A1 (en)	1992-01-23
JPH06511140A (ja)	1994-12-15
CA2086761A1 (en)	1992-01-07
AU8187391A (en)	1992-02-04
EP0538318A1 (en)	1993-04-28

Publication	Publication Date	Title
RU2181378C2 (ru)	2002-04-20	Способ высокоуровневой экспрессии, способ очистки и способ переукладки поринового протеина внешней мембраны менингококка группы в или слитого с ним протеина, высокоочищенный пориновый протеин (варианты), высокоочищенный пориновый слитый протеин (варианты), вакцина для предупреждения бактериального менингита группы в, способ получения конъюгата протеина менингококка группы в и полисахарида, способ предупреждения бактериального менингита, штамм е.coli (варианты)
Cavalieri et al.	1984	Escherichia coli alpha-hemolysin: characteristics and probable role in pathogenicity
Seifert et al.	1990	Shuttle mutagenesis of Neisseria gonorrhoeae: pilin null mutations lower DNA transformation competence
Bilge et al.	1989	Molecular characterization of a fimbrial adhesin, F1845, mediating diffuse adherence of diarrhea-associated Escherichia coli to HEp-2 cells
Brunder et al.	2001	Novel type of fimbriae encoded by the large plasmid of sorbitol-fermenting enterohemorrhagic Escherichia coli O157: H−
Gray-Owen et al.	1995	Identification and characterization of genes encoding the human transferrin-binding proteins from Haemophilus influenzae
Varga et al.	2006	Type IV pili‐dependent gliding motility in the Gram‐positive pathogen Clostridium perfringens and other Clostridia
JP3215109B2 (ja)	2001-10-02	肺炎球菌タンパクの構造遺伝子
Nurminen et al.	1992	The class 1 outer membrane protein of Neisseria meningitidis produced in Bacillus subtilis can give rise to protective immunity
Biswas et al.	1997	Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes
WO1999010497A1 (en)	1999-03-04	Novel mutants of gram negative mucosal bacteria and application thereof in vaccines
EP1590459A2 (en)	2005-11-02	Methods for increasing neisseria protein expression and compositions thereof
US8114971B2 (en)	2012-02-14	Nucleic acid molecules encoding proteins which impart the adhesion of Neisseria cells to human cells
AU668075B2 (en)	1996-04-26	Production of outer membrane (OM) proteins in gram-positive bacteria and recovery of protective epitopes
EP0500736B1 (en)	1995-02-01	Recombinant vaccine for porcine pleuropneumonia
JP3742101B2 (ja)	2006-02-01	組換えＰｉｌＣタンパク質、それらの製造方法及び使用方法
DK175831B1 (da)	2005-03-14	Neisseria gonorrhoeae-relaterede nucleinsyrer, rekombinantvektorer, værtsorgaismer, encellede organismer, polypeptidfremstillingsmetoder, polypeptidsammensætninger, vaccinepræparater, DNA-sonder, påvisningsmetoder og diagnostiske prövesæt, .........
Mazoy et al.	2003	Isolation of mutants of Vibrio anguillarum defective in haeme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of haeme as iron source
US5747287A (en)	1998-05-05	Method for the high level expression, purification and refolding of the outer membrane group B porin proteins from Neisseria meningitidis
WO1998033386A1 (en)	1998-08-06	Method of delivering antigens for vaccination with a live vector
CN112143741B (zh)	2022-09-20	一种生物膜基因岛GIVal43097及其切除方法
Meinersmann et al.	1997	Cloning of an outer membrane protein gene from Campylobacter jejuni
CN100387718C (zh)	2008-05-14	抗蛋白酶k降解的脑膜炎奈瑟氏球菌表面蛋白
van der Ley et al.	2001	Construction of porA mutants
Hackel	1993	Genetic analysis of Moraxella bovis pilus expression