JP2002527041A - 淋菌(Neisseriagonorrhoeae)または髄膜炎菌(Neisseriameningitidis)に対する組換えピリンを含有するワクチン - Google Patents
淋菌(Neisseriagonorrhoeae)または髄膜炎菌(Neisseriameningitidis)に対する組換えピリンを含有するワクチンInfo
- Publication number
- JP2002527041A JP2002527041A JP2000546019A JP2000546019A JP2002527041A JP 2002527041 A JP2002527041 A JP 2002527041A JP 2000546019 A JP2000546019 A JP 2000546019A JP 2000546019 A JP2000546019 A JP 2000546019A JP 2002527041 A JP2002527041 A JP 2002527041A
- Authority
- JP
- Japan
- Prior art keywords
- pilin
- class
- amino acid
- neisseria
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 108010000916 Fimbriae Proteins Proteins 0.000 title claims abstract description 211
- 241000588652 Neisseria gonorrhoeae Species 0.000 title claims abstract description 116
- 241000588650 Neisseria meningitidis Species 0.000 title claims abstract description 106
- 229960005486 vaccine Drugs 0.000 title claims abstract description 60
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 112
- 102000004169 proteins and genes Human genes 0.000 claims description 99
- 241000588724 Escherichia coli Species 0.000 claims description 58
- 239000013612 plasmid Substances 0.000 claims description 57
- 150000001413 amino acids Chemical class 0.000 claims description 56
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 48
- 108020004414 DNA Proteins 0.000 claims description 47
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 47
- 238000000034 method Methods 0.000 claims description 37
- 238000012545 processing Methods 0.000 claims description 30
- 239000000203 mixture Substances 0.000 claims description 29
- DRHZYJAUECRAJM-DWSYSWFDSA-N (2s,3s,4s,5r,6r)-6-[[(3s,4s,4ar,6ar,6bs,8r,8ar,12as,14ar,14br)-8a-[(2s,3r,4s,5r,6r)-3-[(2s,3r,4s,5r,6s)-5-[(2s,3r,4s,5r)-4-[(2s,3r,4r)-3,4-dihydroxy-4-(hydroxymethyl)oxolan-2-yl]oxy-3,5-dihydroxyoxan-2-yl]oxy-3,4-dihydroxy-6-methyloxan-2-yl]oxy-5-[(3s,5s, Chemical compound O([C@H]1[C@H](O)[C@H](O[C@H]([C@@H]1O[C@H]1[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O1)O)O[C@H]1CC[C@]2(C)[C@H]3CC=C4[C@@H]5CC(C)(C)CC[C@@]5([C@@H](C[C@@]4(C)[C@]3(C)CC[C@H]2[C@@]1(C=O)C)O)C(=O)O[C@@H]1O[C@H](C)[C@@H]([C@@H]([C@H]1O[C@H]1[C@@H]([C@H](O)[C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@](O)(CO)CO3)O)[C@H](O)CO2)O)[C@H](C)O1)O)O)OC(=O)C[C@@H](O)C[C@H](OC(=O)C[C@@H](O)C[C@@H]([C@@H](C)CC)O[C@H]1[C@@H]([C@@H](O)[C@H](CO)O1)O)[C@@H](C)CC)C(O)=O)[C@@H]1OC[C@@H](O)[C@H](O)[C@H]1O DRHZYJAUECRAJM-DWSYSWFDSA-N 0.000 claims description 26
- 230000028993 immune response Effects 0.000 claims description 26
- 239000002773 nucleotide Substances 0.000 claims description 26
- 125000003729 nucleotide group Chemical group 0.000 claims description 26
- 230000003053 immunization Effects 0.000 claims description 24
- 239000002671 adjuvant Substances 0.000 claims description 19
- 102000009016 Cholera Toxin Human genes 0.000 claims description 17
- 108010049048 Cholera Toxin Proteins 0.000 claims description 17
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 15
- 241000588653 Neisseria Species 0.000 claims description 13
- 101001059401 Moraxella bovis Type IV major alpha-pilin Proteins 0.000 claims description 12
- 230000002163 immunogen Effects 0.000 claims description 10
- 238000002105 Southern blotting Methods 0.000 claims description 9
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 claims description 8
- 230000001681 protective effect Effects 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 4
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical group [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 claims description 3
- 239000003085 diluting agent Substances 0.000 claims description 3
- 229940035032 monophosphoryl lipid a Drugs 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims 2
- 230000001131 transforming effect Effects 0.000 claims 2
- 230000014616 translation Effects 0.000 claims 2
- 201000010099 disease Diseases 0.000 abstract description 13
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 13
- 229940052778 neisseria meningitidis Drugs 0.000 abstract description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 abstract description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 abstract description 2
- 101150013191 E gene Proteins 0.000 abstract 6
- 210000004027 cell Anatomy 0.000 description 139
- 235000018102 proteins Nutrition 0.000 description 88
- 101150002077 pilE gene Proteins 0.000 description 54
- 235000001014 amino acid Nutrition 0.000 description 39
- 229940024606 amino acid Drugs 0.000 description 37
- 241000894006 Bacteria Species 0.000 description 33
- 238000002965 ELISA Methods 0.000 description 30
- IZWSFJTYBVKZNK-UHFFFAOYSA-N lauryl sulfobetaine Chemical compound CCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O IZWSFJTYBVKZNK-UHFFFAOYSA-N 0.000 description 27
- 239000000047 product Substances 0.000 description 26
- 241000699670 Mus sp. Species 0.000 description 25
- 238000004458 analytical method Methods 0.000 description 25
- 241000700199 Cavia porcellus Species 0.000 description 23
- 210000002966 serum Anatomy 0.000 description 20
- 241001465754 Metazoa Species 0.000 description 19
- 239000002609 medium Substances 0.000 description 19
- 230000001580 bacterial effect Effects 0.000 description 18
- 241000700198 Cavia Species 0.000 description 17
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 17
- 238000005119 centrifugation Methods 0.000 description 17
- 238000002474 experimental method Methods 0.000 description 16
- 229960000723 ampicillin Drugs 0.000 description 15
- 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 15
- 239000000427 antigen Substances 0.000 description 13
- 102000036639 antigens Human genes 0.000 description 13
- 108091007433 antigens Proteins 0.000 description 13
- 238000010367 cloning Methods 0.000 description 13
- 239000000463 material Substances 0.000 description 13
- 239000007983 Tris buffer Substances 0.000 description 12
- 238000002649 immunization Methods 0.000 description 12
- 108091008146 restriction endonucleases Proteins 0.000 description 12
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 12
- 238000001262 western blot Methods 0.000 description 12
- 108010076504 Protein Sorting Signals Proteins 0.000 description 11
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 11
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 11
- 239000012634 fragment Substances 0.000 description 11
- 239000012528 membrane Substances 0.000 description 11
- 239000012980 RPMI-1640 medium Substances 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 229930027917 kanamycin Natural products 0.000 description 10
- 229960000318 kanamycin Drugs 0.000 description 10
- 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 10
- 229930182823 kanamycin A Natural products 0.000 description 10
- 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 10
- 239000000523 sample Substances 0.000 description 10
- 239000011780 sodium chloride Substances 0.000 description 10
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 10
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 9
- 239000003599 detergent Substances 0.000 description 9
- 239000000499 gel Substances 0.000 description 9
- 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 9
- 239000008188 pellet Substances 0.000 description 9
- 230000004044 response Effects 0.000 description 9
- 238000012163 sequencing technique Methods 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 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 8
- 229920001817 Agar Polymers 0.000 description 8
- 239000008272 agar Substances 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 210000002919 epithelial cell Anatomy 0.000 description 8
- 230000035772 mutation Effects 0.000 description 8
- HEGSGKPQLMEBJL-UHFFFAOYSA-N n-octyl beta-D-glucopyranoside Natural products CCCCCCCCOC1OC(CO)C(O)C(O)C1O HEGSGKPQLMEBJL-UHFFFAOYSA-N 0.000 description 8
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 7
- 241000605721 Dichelobacter nodosus Species 0.000 description 7
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 7
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 7
- 230000000890 antigenic effect Effects 0.000 description 7
- 235000013922 glutamic acid Nutrition 0.000 description 7
- 239000004220 glutamic acid Substances 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- JUJWROOIHBZHMG-UHFFFAOYSA-O pyridinium Chemical compound C1=CC=[NH+]C=C1 JUJWROOIHBZHMG-UHFFFAOYSA-O 0.000 description 7
- 239000006228 supernatant Substances 0.000 description 7
- 239000012130 whole-cell lysate Substances 0.000 description 7
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 6
- 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 6
- 241000282412 Homo Species 0.000 description 6
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 238000004220 aggregation Methods 0.000 description 6
- 238000000502 dialysis Methods 0.000 description 6
- 230000005847 immunogenicity Effects 0.000 description 6
- 238000011534 incubation Methods 0.000 description 6
- 230000006698 induction Effects 0.000 description 6
- 238000002955 isolation Methods 0.000 description 6
- 239000007788 liquid Substances 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 238000000386 microscopy Methods 0.000 description 6
- 229920000136 polysorbate Polymers 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 229940125575 vaccine candidate Drugs 0.000 description 6
- 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 5
- 206010018612 Gonorrhoea Diseases 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 241001460678 Napo <wasp> Species 0.000 description 5
- 102000005583 Pyrin Human genes 0.000 description 5
- 108010059278 Pyrin Proteins 0.000 description 5
- 230000002776 aggregation Effects 0.000 description 5
- 239000013592 cell lysate Substances 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 239000008121 dextrose Substances 0.000 description 5
- 230000029087 digestion Effects 0.000 description 5
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 5
- 208000001786 gonorrhea Diseases 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 238000004949 mass spectrometry Methods 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 239000000725 suspension Substances 0.000 description 5
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 241001646716 Escherichia coli K-12 Species 0.000 description 4
- 108010010803 Gelatin Proteins 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 4
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 4
- 241000589516 Pseudomonas Species 0.000 description 4
- 235000003704 aspartic acid Nutrition 0.000 description 4
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 238000004440 column chromatography Methods 0.000 description 4
- 238000000326 densiometry Methods 0.000 description 4
- 230000007717 exclusion Effects 0.000 description 4
- 239000012091 fetal bovine serum Substances 0.000 description 4
- 239000012530 fluid Substances 0.000 description 4
- 238000005194 fractionation Methods 0.000 description 4
- 239000008273 gelatin Substances 0.000 description 4
- 229920000159 gelatin Polymers 0.000 description 4
- 235000019322 gelatine Nutrition 0.000 description 4
- 235000011852 gelatine desserts Nutrition 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 238000009630 liquid culture Methods 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 230000016379 mucosal immune response Effects 0.000 description 4
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 101150079601 recA gene Proteins 0.000 description 4
- 239000002356 single layer Substances 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 229910017119 AlPO Inorganic materials 0.000 description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 3
- 208000031729 Bacteremia Diseases 0.000 description 3
- 238000011537 Coomassie blue staining Methods 0.000 description 3
- 229920002307 Dextran Polymers 0.000 description 3
- 241000283074 Equus asinus Species 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 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
- 241001377010 Pila Species 0.000 description 3
- 208000029221 Primary intralymphatic angioendothelioma Diseases 0.000 description 3
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- 239000004098 Tetracycline Substances 0.000 description 3
- 230000004520 agglutination Effects 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 229940088710 antibiotic agent Drugs 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 235000009582 asparagine Nutrition 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 210000000170 cell membrane Anatomy 0.000 description 3
- 239000006285 cell suspension Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000005352 clarification Methods 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 239000012894 fetal calf serum Substances 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 229910052737 gold Inorganic materials 0.000 description 3
- 239000010931 gold Substances 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 229910052742 iron Inorganic materials 0.000 description 3
- 230000002262 irrigation Effects 0.000 description 3
- 238000003973 irrigation Methods 0.000 description 3
- 239000006194 liquid suspension Substances 0.000 description 3
- 229960005037 meningococcal vaccines Drugs 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 210000004877 mucosa Anatomy 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 239000013600 plasmid vector Substances 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000012266 salt solution Substances 0.000 description 3
- 239000001488 sodium phosphate Substances 0.000 description 3
- 229910000162 sodium phosphate Inorganic materials 0.000 description 3
- 229960002180 tetracycline Drugs 0.000 description 3
- 229930101283 tetracycline Natural products 0.000 description 3
- 235000019364 tetracycline Nutrition 0.000 description 3
- 150000003522 tetracyclines Chemical class 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000004627 transmission electron microscopy Methods 0.000 description 3
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 3
- 210000001215 vagina Anatomy 0.000 description 3
- 238000012800 visualization Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 206010008342 Cervix carcinoma Diseases 0.000 description 2
- 206010068051 Chimerism Diseases 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 229920004934 Dacron® Polymers 0.000 description 2
- 206010012735 Diarrhoea Diseases 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 206010058858 Meningococcal bacteraemia Diseases 0.000 description 2
- 101001059392 Neisseria gonorrhoeae Type IV major pilin protein PilE Proteins 0.000 description 2
- 101001059397 Neisseria gonorrhoeae Type IV major pilin protein PilE1 Proteins 0.000 description 2
- 101100446858 Neisseria gonorrhoeae pilE gene Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 238000003917 TEM image Methods 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 208000006105 Uterine Cervical Neoplasms Diseases 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 201000010881 cervical cancer Diseases 0.000 description 2
- 239000013611 chromosomal DNA Substances 0.000 description 2
- 230000001332 colony forming effect Effects 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 230000007850 degeneration Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000001493 electron microscopy Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000006167 equilibration buffer Substances 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000007667 floating Methods 0.000 description 2
- 230000005714 functional activity Effects 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000028996 humoral immune response Effects 0.000 description 2
- 125000001165 hydrophobic group Chemical group 0.000 description 2
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 208000002864 infectious keratoconjunctivitis Diseases 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 239000007928 intraperitoneal injection Substances 0.000 description 2
- MVFCKEFYUDZOCX-UHFFFAOYSA-N iron(2+);dinitrate Chemical compound [Fe+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O MVFCKEFYUDZOCX-UHFFFAOYSA-N 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- DVEKCXOJTLDBFE-UHFFFAOYSA-N n-dodecyl-n,n-dimethylglycinate Chemical compound CCCCCCCCCCCC[N+](C)(C)CC([O-])=O DVEKCXOJTLDBFE-UHFFFAOYSA-N 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 2
- 235000015047 pilsener Nutrition 0.000 description 2
- 239000005020 polyethylene terephthalate Substances 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 2
- HEGSGKPQLMEBJL-RQICVUQASA-N (2r,3s,4s,5r)-2-(hydroxymethyl)-6-octoxyoxane-3,4,5-triol Chemical compound CCCCCCCCOC1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RQICVUQASA-N 0.000 description 1
- PWKSKIMOESPYIA-UHFFFAOYSA-N 2-acetamido-3-sulfanylpropanoic acid Chemical compound CC(=O)NC(CS)C(O)=O PWKSKIMOESPYIA-UHFFFAOYSA-N 0.000 description 1
- OZDAOHVKBFBBMZ-UHFFFAOYSA-N 2-aminopentanedioic acid;hydrate Chemical compound O.OC(=O)C(N)CCC(O)=O OZDAOHVKBFBBMZ-UHFFFAOYSA-N 0.000 description 1
- IIZVTUWSIKTFKO-UHFFFAOYSA-N 2-hydroxypropanoic acid;5-[(3,4,5-trimethoxyphenyl)methyl]pyrimidine-2,4-diamine Chemical compound CC(O)C(O)=O.COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IIZVTUWSIKTFKO-UHFFFAOYSA-N 0.000 description 1
- IITIZHOBOIBGBW-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole Chemical compound C1=CC=C2N(CC)CSC2=C1 IITIZHOBOIBGBW-UHFFFAOYSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- 241000272478 Aquila Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000034309 Bacterial disease carrier Diseases 0.000 description 1
- 241000606125 Bacteroides Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 1
- 101000795655 Canis lupus familiaris Thymic stromal cotransporter homolog Proteins 0.000 description 1
- 102100033029 Carbonic anhydrase-related protein 11 Human genes 0.000 description 1
- 108010078777 Colistin Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102100024607 DNA topoisomerase 1 Human genes 0.000 description 1
- 241000606006 Dichelobacter Species 0.000 description 1
- 241000588878 Eikenella corrodens Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 240000002727 Fimbristylis littoralis Species 0.000 description 1
- 208000007212 Foot-and-Mouth Disease Diseases 0.000 description 1
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 1
- 102100036738 Guanine nucleotide-binding protein subunit alpha-11 Human genes 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000867841 Homo sapiens Carbonic anhydrase-related protein 11 Proteins 0.000 description 1
- 101000830681 Homo sapiens DNA topoisomerase 1 Proteins 0.000 description 1
- 101100283445 Homo sapiens GNA11 gene Proteins 0.000 description 1
- 101001075218 Homo sapiens Gastrokine-1 Proteins 0.000 description 1
- 101100293260 Homo sapiens NAA15 gene Proteins 0.000 description 1
- 241000589015 Kingella denitrificans Species 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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-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
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-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
- FQZPTCNSNPWHLJ-AVGNSLFASA-N Leu-Gln-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O FQZPTCNSNPWHLJ-AVGNSLFASA-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
- 206010027249 Meningitis meningococcal Diseases 0.000 description 1
- 201000010924 Meningococcal meningitis Diseases 0.000 description 1
- MCNGIXXCMJAURZ-VEVYYDQMSA-N Met-Asp-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCSC)N)O MCNGIXXCMJAURZ-VEVYYDQMSA-N 0.000 description 1
- 241000588622 Moraxella bovis Species 0.000 description 1
- 241000588629 Moraxella lacunata Species 0.000 description 1
- 241000588630 Moraxella nonliquefaciens Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 102100030856 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 0.000 description 1
- SCIFESDRCALIIM-UHFFFAOYSA-N N-Me-Phenylalanine Natural products CNC(C(O)=O)CC1=CC=CC=C1 SCIFESDRCALIIM-UHFFFAOYSA-N 0.000 description 1
- 102100026781 N-alpha-acetyltransferase 15, NatA auxiliary subunit Human genes 0.000 description 1
- SCIFESDRCALIIM-VIFPVBQESA-N N-methyl-L-phenylalanine Chemical compound C[NH2+][C@H](C([O-])=O)CC1=CC=CC=C1 SCIFESDRCALIIM-VIFPVBQESA-N 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 241000432851 Neisseria meningitidis FAM18 Species 0.000 description 1
- 241000897304 Neisseria meningitidis H44/76 Species 0.000 description 1
- 108700001237 Nucleic Acid-Based Vaccines Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 229930040373 Paraformaldehyde Natural products 0.000 description 1
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 108010013381 Porins Proteins 0.000 description 1
- 102000002067 Protein Subunits Human genes 0.000 description 1
- 108010001267 Protein Subunits Proteins 0.000 description 1
- 241000220324 Pyrus Species 0.000 description 1
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 108010057517 Strep-avidin conjugated horseradish peroxidase Proteins 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 108010059993 Vancomycin Proteins 0.000 description 1
- 241000607626 Vibrio cholerae Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000025845 adhesion to host Effects 0.000 description 1
- 230000004523 agglutinating effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 230000010065 bacterial adhesion Effects 0.000 description 1
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 210000000621 bronchi Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 229910002091 carbon monoxide Inorganic materials 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000013553 cell monolayer Substances 0.000 description 1
- 229940030156 cell vaccine Drugs 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 235000019365 chlortetracycline Nutrition 0.000 description 1
- AGOYDEPGAOXOCK-KCBOHYOISA-N clarithromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@](C)([C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)OC)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 AGOYDEPGAOXOCK-KCBOHYOISA-N 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 229950001485 cocarboxylase Drugs 0.000 description 1
- 229960001127 colistin sulfate Drugs 0.000 description 1
- 239000000084 colloidal system Substances 0.000 description 1
- 230000005757 colony formation Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- QCHSEDTUUKDTIG-UHFFFAOYSA-L dipotassium clorazepate Chemical compound [OH-].[K+].[K+].C12=CC(Cl)=CC=C2NC(=O)C(C(=O)[O-])N=C1C1=CC=CC=C1 QCHSEDTUUKDTIG-UHFFFAOYSA-L 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 229910001651 emery Inorganic materials 0.000 description 1
- 244000000021 enteric pathogen Species 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000013213 extrapolation Methods 0.000 description 1
- 210000004700 fetal blood Anatomy 0.000 description 1
- 244000144992 flock Species 0.000 description 1
- 208000010801 foot rot Diseases 0.000 description 1
- 239000012520 frozen sample Substances 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 210000004392 genitalia Anatomy 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 238000000703 high-speed centrifugation Methods 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000004201 immune sera Anatomy 0.000 description 1
- 229940042743 immune sera Drugs 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 230000006799 invasive growth in response to glucose limitation Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000005342 ion exchange 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
- 230000002147 killing effect Effects 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 210000002418 meninge Anatomy 0.000 description 1
- 208000037941 meningococcal disease Diseases 0.000 description 1
- 230000031864 metaphase Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- ZESIAEVDVPWEKB-ORCFLVBFSA-N n-[(2s)-4-amino-1-[[(2s,3r)-1-[[(2s)-4-amino-1-oxo-1-[[(3s,6s,9s,12s,15r,18s,21s)-6,9,18-tris(2-aminoethyl)-3-[(1r)-1-hydroxyethyl]-12,15-bis(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-h Chemical compound OS(O)(=O)=O.OS(O)(=O)=O.CC(C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@H]([C@@H](C)O)CN[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CCN)NC1=O.CCC(C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@H]([C@@H](C)O)CN[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CCN)NC1=O ZESIAEVDVPWEKB-ORCFLVBFSA-N 0.000 description 1
- 210000001989 nasopharynx Anatomy 0.000 description 1
- 229960000988 nystatin Drugs 0.000 description 1
- VQOXZBDYSJBXMA-NQTDYLQESA-N nystatin A1 Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/CC/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 VQOXZBDYSJBXMA-NQTDYLQESA-N 0.000 description 1
- 210000000287 oocyte Anatomy 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 229920002866 paraformaldehyde Polymers 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 229940056360 penicillin g Drugs 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
- 239000006187 pill Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 102000007739 porin activity proteins Human genes 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000007781 pre-processing Methods 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 238000011552 rat model Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 229940016590 sarkosyl Drugs 0.000 description 1
- 108700004121 sarkosyl Proteins 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 230000009528 severe injury Effects 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 206010041823 squamous cell carcinoma Diseases 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- YXVCLPJQTZXJLH-UHFFFAOYSA-N thiamine(1+) diphosphate chloride Chemical compound [Cl-].CC1=C(CCOP(O)(=O)OP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1N YXVCLPJQTZXJLH-UHFFFAOYSA-N 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 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
- 238000013519 translation Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 229960001937 trimethoprim lactate Drugs 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 229960003165 vancomycin Drugs 0.000 description 1
- MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- AFVLVVWMAFSXCK-UHFFFAOYSA-N α-cyano-4-hydroxycinnamic acid Chemical compound OC(=O)C(C#N)=CC1=CC=C(O)C=C1 AFVLVVWMAFSXCK-UHFFFAOYSA-N 0.000 description 1
- 150000008505 β-D-glucopyranosides Chemical class 0.000 description 1
Classifications
-
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- 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)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Communicable Diseases (AREA)
- Plant Pathology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Oncology (AREA)
- Pharmacology & Pharmacy (AREA)
- Physics & Mathematics (AREA)
- Gastroenterology & Hepatology (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US8340598P | 1998-04-29 | 1998-04-29 | |
US60/083,405 | 1998-04-29 | ||
PCT/US1999/009486 WO1999055875A2 (en) | 1998-04-29 | 1999-04-29 | VACCINES CONTAINING RECOMBINANT PILIN AGAINST NEISSERIA GONORRHOEAE OR $i(NEISSERIA MENINGITIDIS) |
Publications (1)
Publication Number | Publication Date |
---|---|
JP2002527041A true JP2002527041A (ja) | 2002-08-27 |
Family
ID=22178094
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2000546019A Withdrawn JP2002527041A (ja) | 1998-04-29 | 1999-04-29 | 淋菌(Neisseriagonorrhoeae)または髄膜炎菌(Neisseriameningitidis)に対する組換えピリンを含有するワクチン |
Country Status (9)
Country | Link |
---|---|
EP (1) | EP1073748A2 (ko) |
JP (1) | JP2002527041A (ko) |
KR (4) | KR20060118629A (ko) |
CN (1) | CN1245512C (ko) |
AU (2) | AU3968599A (ko) |
BR (1) | BR9910005A (ko) |
CA (1) | CA2325055A1 (ko) |
IL (1) | IL139311A0 (ko) |
WO (1) | WO1999055875A2 (ko) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014006587A (ja) * | 2012-06-21 | 2014-01-16 | Canon Inc | ライセンス管理装置、ライセンス管理方法、およびプログラム |
Families Citing this family (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB0011108D0 (en) * | 2000-05-08 | 2000-06-28 | Microscience Ltd | Virulence gene and protein and their use |
GB0118249D0 (en) * | 2001-07-26 | 2001-09-19 | Chiron Spa | Histidine vaccines |
EP1733048B1 (en) * | 2004-04-08 | 2010-12-29 | The State of Queensland acting through Queensland Health | Neisseria gonorrhoeae detection |
US20110182981A1 (en) * | 2008-08-25 | 2011-07-28 | Peixuan Zhu | Gonococcal vaccines |
US9802988B2 (en) * | 2009-05-20 | 2017-10-31 | University Of Maryland, Baltimore | Engineered type IV pilin of Clostridium difficile |
EP2635593B1 (en) * | 2010-11-05 | 2016-09-14 | Institut National de la Sante et de la Recherche Medicale (INSERM) | Vaccines for preventing meningococcal infections |
CN104736563A (zh) * | 2012-07-27 | 2015-06-24 | 国家健康与医学研究院 | Cd147作为受体用于脑膜炎球菌至血管内皮的菌毛介导的粘附 |
CN103405760A (zh) * | 2013-06-19 | 2013-11-27 | 中国科学院海洋研究所 | 迟缓爱德华氏菌菌毛蛋白FimA的应用 |
CN106290849A (zh) * | 2015-05-13 | 2017-01-04 | 上海凯创生物技术有限公司 | 一种脑膜炎菌胶体金检测试剂盒 |
Family Cites Families (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
BE841068A (fr) * | 1975-04-25 | 1976-10-25 | Procede de preparation de cristaux de poils gonococciques et leurs applications a la detection et a la prevention des infections dues a neisseria gonorrhoeae | |
EP0049945A3 (en) * | 1980-09-15 | 1982-12-01 | Bactex Incorporated | Determining a hierarchy of piliated organisms and a vaccine prepared from such organisms |
US4443431A (en) * | 1981-05-27 | 1984-04-17 | The United States Of America As Represented By The Department Of Health And Human Services | Neisseria gonorrhoeae vaccine |
EP0177583A4 (en) * | 1984-04-06 | 1988-06-08 | Scripps Clinic Res | PEPTIDE VACCINE OR DIAGNOSTIC, AND POLYPEPTIDE FOR USE THEREOF. |
CU22302A1 (es) * | 1990-09-07 | 1995-01-31 | Cigb | Secuencia nucleotidica codificante para una proteina de la membrana externa de neisseria meningitidis y uso de dicha proteina en preparados vacunales |
WO1992013871A1 (en) * | 1991-01-31 | 1992-08-20 | Washington University | Polypeptides and polynucleotides useful for the diagnosis and treatment of pathogenic neisseria |
AU3416693A (en) * | 1991-12-18 | 1993-07-19 | State Of Oregon Acting By And Through The Oregon State Board Of Higher Education On Behalf Of Oregon State University, The | Antigenic preparations that stimulate production of antibodies which bind to the pili of type IV piliated bacteria |
DK0761231T3 (da) * | 1992-06-25 | 2000-05-08 | Smithkline Beecham Biolog | Vaccinepræparat indeholdende adjuvanser |
AU5403594A (en) * | 1992-10-07 | 1994-04-26 | State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education On Behalf Of The Oregon Health Sciences University | Pilin variants and uses thereof |
US6265567B1 (en) * | 1995-04-07 | 2001-07-24 | University Of North Carolina At Chapel Hill | Isolated FrpB nucleic acid molecule |
-
1999
- 1999-04-29 KR KR1020067022728A patent/KR20060118629A/ko not_active Application Discontinuation
- 1999-04-29 BR BR9910005-3A patent/BR9910005A/pt not_active IP Right Cessation
- 1999-04-29 CA CA002325055A patent/CA2325055A1/en not_active Abandoned
- 1999-04-29 CN CNB998056014A patent/CN1245512C/zh not_active Expired - Fee Related
- 1999-04-29 AU AU39685/99A patent/AU3968599A/en not_active Abandoned
- 1999-04-29 EP EP99922760A patent/EP1073748A2/en not_active Withdrawn
- 1999-04-29 KR KR1020067022726A patent/KR20060118628A/ko not_active Application Discontinuation
- 1999-04-29 KR KR1020067022731A patent/KR20060118630A/ko not_active Application Discontinuation
- 1999-04-29 JP JP2000546019A patent/JP2002527041A/ja not_active Withdrawn
- 1999-04-29 IL IL13931199A patent/IL139311A0/xx unknown
- 1999-04-29 KR KR1020007011991A patent/KR20010043105A/ko not_active Application Discontinuation
- 1999-04-29 WO PCT/US1999/009486 patent/WO1999055875A2/en active Application Filing
-
2003
- 2003-06-16 AU AU2003204738A patent/AU2003204738B2/en not_active Ceased
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014006587A (ja) * | 2012-06-21 | 2014-01-16 | Canon Inc | ライセンス管理装置、ライセンス管理方法、およびプログラム |
Also Published As
Publication number | Publication date |
---|---|
AU2003204738B2 (en) | 2006-09-14 |
WO1999055875A2 (en) | 1999-11-04 |
CN1245512C (zh) | 2006-03-15 |
KR20010043105A (ko) | 2001-05-25 |
AU3968599A (en) | 1999-11-16 |
WO1999055875A3 (en) | 2000-04-13 |
IL139311A0 (en) | 2001-11-25 |
CA2325055A1 (en) | 1999-11-04 |
BR9910005A (pt) | 2001-01-16 |
KR20060118629A (ko) | 2006-11-23 |
KR20060118628A (ko) | 2006-11-23 |
EP1073748A2 (en) | 2001-02-07 |
KR20060118630A (ko) | 2006-11-23 |
CN1298446A (zh) | 2001-06-06 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP3253327B2 (ja) | 髄膜炎菌外層膜蛋白質をコードするヌクレオチド配列を有するポリヌクレオチドおよびワクチン組成物 | |
JP5566684B2 (ja) | Clostridiumdifficileに対する、組換え毒素A/毒素Bワクチン | |
JP4005634B2 (ja) | モラクセラ属菌由来トランスフェリン受容体タンパク質 | |
JP2907552B2 (ja) | ヘモフィルス外膜タンパク質 | |
EP0639081B1 (en) | Vaccine compositions for mucosal delivery | |
CA2040544C (en) | Actinobacillus pleuropneumoniae subunit vaccine | |
Nurminen et al. | The class 1 outer membrane protein of Neisseria meningitidis produced in Bacillus subtilis can give rise to protective immunity | |
NZ234933A (en) | Vaccine against e.coli infection and toxin therefor derived from flagella of a single e.coli strain | |
US6733760B1 (en) | Recombinant toxin A/toxin B vaccine against Clostridium difficile | |
JP2002527041A (ja) | 淋菌(Neisseriagonorrhoeae)または髄膜炎菌(Neisseriameningitidis)に対する組換えピリンを含有するワクチン | |
EP0815236B1 (en) | Haemophilus adhesion proteins | |
JP2002505083A (ja) | 組換え脂質化PsaAタンパク質、調製法および使用 | |
USRE37741E1 (en) | Purified nontypable Haemophilus influenzae P5 protein as a vaccine for nontypable Haemophilus influenzae infection | |
CA2203540C (en) | Major outer membrane protein cd of moraxella | |
JP2001503602A (ja) | 非共通形態型好血菌属の高分子量表面タンパク質 | |
US20030165526A1 (en) | Vaccines and agents for inducing immunity against rickettsial diseases, and associated preventative therapy | |
Ward et al. | Expression ofNeisseria meningitidisclass 1 porin as a fusion protein inEscherichia colli: the influence of liposomes and adjuvants on the production of a bactericidal immune reesponse | |
EP1688428A1 (en) | Method of antigen incorporation into neisseria bacterial outer membrane vesicles and resulting vaccine formulations | |
JP2002538169A (ja) | インフルエンザ菌に起因する疾患を防御するための、少なくとも3つの抗原を含む多成分系ワクチン | |
AU2004200152A1 (en) | Vaccines Containing Recombinant Pilin Against Neisseria Gonorrhoeae or Neisseria Meningitidis | |
Active | Protection against Development of Otitis | |
JP2001078765A (ja) | シュードモナス菌の融合タンパク質ワクチン | |
EP1078988A1 (en) | Pseudomonas fusion protein vaccines | |
AU4716200A (en) | Haemophilus adhesion proteins |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20060323 |
|
A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20070914 |