ZA200208835B - Compounds and methods for the treatment and prevention of bacterial infection. - Google Patents
Compounds and methods for the treatment and prevention of bacterial infection. Download PDFInfo
- Publication number
- ZA200208835B ZA200208835B ZA200208835A ZA200208835A ZA200208835B ZA 200208835 B ZA200208835 B ZA 200208835B ZA 200208835 A ZA200208835 A ZA 200208835A ZA 200208835 A ZA200208835 A ZA 200208835A ZA 200208835 B ZA200208835 B ZA 200208835B
- Authority
- ZA
- South Africa
- Prior art keywords
- moiety
- mutation
- pore
- toxin
- mutant
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 28
- 208000035143 Bacterial infection Diseases 0.000 title claims description 16
- 208000022362 bacterial infectious disease Diseases 0.000 title claims description 16
- 230000002265 prevention Effects 0.000 title description 8
- 150000001875 compounds Chemical class 0.000 title description 5
- 101710194807 Protective antigen Proteins 0.000 claims description 380
- 239000003053 toxin Substances 0.000 claims description 141
- 108700012359 toxins Proteins 0.000 claims description 139
- 231100000765 toxin Toxicity 0.000 claims description 138
- 230000035772 mutation Effects 0.000 claims description 103
- 241000193738 Bacillus anthracis Species 0.000 claims description 65
- 239000011148 porous material Substances 0.000 claims description 64
- 239000000203 mixture Substances 0.000 claims description 44
- 150000001413 amino acids Chemical class 0.000 claims description 43
- 239000012634 fragment Substances 0.000 claims description 43
- 235000001014 amino acid Nutrition 0.000 claims description 35
- 235000018102 proteins Nutrition 0.000 claims description 33
- 108090000623 proteins and genes Proteins 0.000 claims description 33
- 102000004169 proteins and genes Human genes 0.000 claims description 33
- 230000004075 alteration Effects 0.000 claims description 28
- 229960005486 vaccine Drugs 0.000 claims description 25
- 241000124008 Mammalia Species 0.000 claims description 24
- 101500000960 Bacillus anthracis Protective antigen PA-63 Proteins 0.000 claims description 23
- 238000012217 deletion Methods 0.000 claims description 22
- 230000037430 deletion Effects 0.000 claims description 22
- 208000022338 anthrax infection Diseases 0.000 claims description 17
- 239000003937 drug carrier Substances 0.000 claims description 16
- 239000003814 drug Substances 0.000 claims description 13
- 230000002163 immunogen Effects 0.000 claims description 13
- 102000005962 receptors Human genes 0.000 claims description 13
- 230000002829 reductive effect Effects 0.000 claims description 13
- 102000037865 fusion proteins Human genes 0.000 claims description 11
- 108020001507 fusion proteins Proteins 0.000 claims description 11
- 238000004519 manufacturing process Methods 0.000 claims description 11
- 241000193163 Clostridioides difficile Species 0.000 claims description 7
- 241000193155 Clostridium botulinum Species 0.000 claims description 7
- 241000193468 Clostridium perfringens Species 0.000 claims description 7
- 241001147796 [Clostridium] spiroforme Species 0.000 claims description 7
- 231100000518 lethal Toxicity 0.000 claims description 7
- 230000001665 lethal effect Effects 0.000 claims description 7
- 230000001681 protective effect Effects 0.000 claims description 7
- 241000193755 Bacillus cereus Species 0.000 claims description 6
- 206010030113 Oedema Diseases 0.000 claims description 6
- 239000002671 adjuvant Substances 0.000 claims description 5
- 229940065181 bacillus anthracis Drugs 0.000 claims description 5
- 235000018417 cysteine Nutrition 0.000 claims description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 5
- 210000004962 mammalian cell Anatomy 0.000 claims description 4
- 239000000126 substance Substances 0.000 claims description 4
- 108030001720 Bontoxilysin Proteins 0.000 claims description 3
- 229940053031 botulinum toxin Drugs 0.000 claims description 2
- 230000028993 immune response Effects 0.000 claims description 2
- 101710182223 Toxin B Proteins 0.000 claims 15
- 125000003275 alpha amino acid group Chemical group 0.000 claims 12
- 239000000427 antigen Substances 0.000 claims 2
- 102000036639 antigens Human genes 0.000 claims 2
- 108091007433 antigens Proteins 0.000 claims 2
- 235000010582 Pisum sativum Nutrition 0.000 claims 1
- 240000004713 Pisum sativum Species 0.000 claims 1
- 230000004992 fission Effects 0.000 claims 1
- 230000001939 inductive effect Effects 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 73
- 230000005945 translocation Effects 0.000 description 45
- 230000005764 inhibitory process Effects 0.000 description 41
- 230000000694 effects Effects 0.000 description 37
- 230000015572 biosynthetic process Effects 0.000 description 35
- 238000003556 assay Methods 0.000 description 33
- 239000012528 membrane Substances 0.000 description 27
- 229940024606 amino acid Drugs 0.000 description 26
- 239000003446 ligand Substances 0.000 description 23
- 238000001243 protein synthesis Methods 0.000 description 20
- 230000014616 translation Effects 0.000 description 20
- 230000001404 mediated effect Effects 0.000 description 19
- 230000000875 corresponding effect Effects 0.000 description 17
- 108090000765 processed proteins & peptides Proteins 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 16
- 229920001184 polypeptide Polymers 0.000 description 15
- 241001465754 Metazoa Species 0.000 description 14
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 13
- 238000001727 in vivo Methods 0.000 description 12
- 238000002723 toxicity assay Methods 0.000 description 11
- 230000009471 action Effects 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 241000700159 Rattus Species 0.000 description 8
- 230000002401 inhibitory effect Effects 0.000 description 8
- 238000002347 injection Methods 0.000 description 8
- 239000007924 injection Substances 0.000 description 8
- 108090000631 Trypsin Proteins 0.000 description 7
- 102000004142 Trypsin Human genes 0.000 description 7
- 210000000170 cell membrane Anatomy 0.000 description 7
- 230000002596 correlated effect Effects 0.000 description 7
- 210000000805 cytoplasm Anatomy 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 229910052701 rubidium Inorganic materials 0.000 description 7
- IGLNJRXAVVLDKE-UHFFFAOYSA-N rubidium atom Chemical compound [Rb] IGLNJRXAVVLDKE-UHFFFAOYSA-N 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 7
- 239000012588 trypsin Substances 0.000 description 7
- 241000894006 Bacteria Species 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 230000003472 neutralizing effect Effects 0.000 description 6
- 231100000419 toxicity Toxicity 0.000 description 6
- 230000001988 toxicity Effects 0.000 description 6
- 102000008300 Mutant Proteins Human genes 0.000 description 5
- 108010021466 Mutant Proteins Proteins 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 230000001225 therapeutic effect Effects 0.000 description 5
- 241000193388 Bacillus thuringiensis Species 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 101000606032 Pomacea maculata Perivitellin-2 31 kDa subunit Proteins 0.000 description 4
- 101000606027 Pomacea maculata Perivitellin-2 67 kDa subunit Proteins 0.000 description 4
- 210000004899 c-terminal region Anatomy 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 4
- 230000002950 deficient Effects 0.000 description 4
- 239000003112 inhibitor Substances 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 230000035987 intoxication Effects 0.000 description 4
- 231100000566 intoxication Toxicity 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 238000002255 vaccination Methods 0.000 description 4
- 102000016607 Diphtheria Toxin Human genes 0.000 description 3
- 108010053187 Diphtheria Toxin Proteins 0.000 description 3
- 102000004961 Furin Human genes 0.000 description 3
- 108090001126 Furin Proteins 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 108010059712 Pronase Proteins 0.000 description 3
- 206010043376 Tetanus Diseases 0.000 description 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 238000006384 oligomerization reaction Methods 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 239000003981 vehicle Substances 0.000 description 3
- 241000607528 Aeromonas hydrophila Species 0.000 description 2
- 101000585552 Bacillus anthracis Protective antigen Proteins 0.000 description 2
- 101500000959 Bacillus anthracis Protective antigen PA-20 Proteins 0.000 description 2
- 108010001857 Cell Surface Receptors Proteins 0.000 description 2
- 241000193466 Clostridium septicum Species 0.000 description 2
- 101710112752 Cytotoxin Proteins 0.000 description 2
- WHUUTDBJXJRKMK-GSVOUGTGSA-N D-glutamic acid Chemical compound OC(=O)[C@H](N)CCC(O)=O WHUUTDBJXJRKMK-GSVOUGTGSA-N 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 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
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000191967 Staphylococcus aureus Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 108010014387 aerolysin Proteins 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 238000005349 anion exchange Methods 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 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 2
- 239000012472 biological sample Substances 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 235000012000 cholesterol Nutrition 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- 231100000599 cytotoxic agent Toxicity 0.000 description 2
- 239000002619 cytotoxin Substances 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000034994 death Effects 0.000 description 2
- 206010013023 diphtheria Diseases 0.000 description 2
- 210000001163 endosome Anatomy 0.000 description 2
- 239000011544 gradient gel Substances 0.000 description 2
- 239000003228 hemolysin Substances 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 125000001165 hydrophobic group Chemical group 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 231100000636 lethal dose Toxicity 0.000 description 2
- 238000004811 liquid chromatography Methods 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 102000006240 membrane receptors Human genes 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 210000001539 phagocyte Anatomy 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 229960004319 trichloroacetic acid Drugs 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 239000000304 virulence factor Substances 0.000 description 2
- 230000007923 virulence factor Effects 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- WEEMDRWIKYCTQM-UHFFFAOYSA-N 2,6-dimethoxybenzenecarbothioamide Chemical compound COC1=CC=CC(OC)=C1C(N)=S WEEMDRWIKYCTQM-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- 102000009062 ADP Ribose Transferases Human genes 0.000 description 1
- 108010049290 ADP Ribose Transferases Proteins 0.000 description 1
- 102100026291 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 Human genes 0.000 description 1
- 101710112065 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 244000075850 Avena orientalis Species 0.000 description 1
- 235000007319 Avena orientalis Nutrition 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 239000008000 CHES buffer Substances 0.000 description 1
- 101100245381 Caenorhabditis elegans pbs-6 gene Proteins 0.000 description 1
- 102000000584 Calmodulin Human genes 0.000 description 1
- 108010041952 Calmodulin Proteins 0.000 description 1
- 241001660259 Cereus <cactus> Species 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 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 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 206010017711 Gangrene Diseases 0.000 description 1
- 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 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 241000590002 Helicobacter pylori Species 0.000 description 1
- 101000953492 Homo sapiens Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 Proteins 0.000 description 1
- 101001036448 Homo sapiens Myelin and lymphocyte protein Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102100037739 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 Human genes 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 102100039459 Myelin and lymphocyte protein Human genes 0.000 description 1
- MKWKNSIESPFAQN-UHFFFAOYSA-N N-cyclohexyl-2-aminoethanesulfonic acid Chemical compound OS(=O)(=O)CCNC1CCCCC1 MKWKNSIESPFAQN-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 101150105115 PA gene Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 239000012614 Q-Sepharose Substances 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- PTTGRYBBCYZPSL-UHFFFAOYSA-H [Al+3].[Al+3].OOP([O-])([O-])=O.OOP([O-])([O-])=O.OOP([O-])([O-])=O Chemical compound [Al+3].[Al+3].OOP([O-])([O-])=O.OOP([O-])([O-])=O.OOP([O-])([O-])=O PTTGRYBBCYZPSL-UHFFFAOYSA-H 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 102000030621 adenylate cyclase Human genes 0.000 description 1
- 108060000200 adenylate cyclase Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- 229940047712 aluminum hydroxyphosphate Drugs 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 239000000729 antidote Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229910052797 bismuth Inorganic materials 0.000 description 1
- JCXGWMGPZLAOME-UHFFFAOYSA-N bismuth atom Chemical compound [Bi] JCXGWMGPZLAOME-UHFFFAOYSA-N 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 229940001442 combination vaccine Drugs 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000008602 contraction Effects 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
- 239000013078 crystal Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 102220500036 eIF5-mimic protein 2_D45K_mutation Human genes 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000017188 evasion or tolerance of host immune response Effects 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000035784 germination Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 235000004554 glutamine Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229940037467 helicobacter pylori Drugs 0.000 description 1
- ZKVLEFBKBNUQHK-UHFFFAOYSA-N helium;molecular nitrogen;molecular oxygen Chemical compound [He].N#N.O=O ZKVLEFBKBNUQHK-UHFFFAOYSA-N 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000000749 insecticidal effect Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000002955 isolation 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
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000008384 membrane barrier Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 231100000668 minimum lethal dose Toxicity 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 229940056360 penicillin g Drugs 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 150000003109 potassium Chemical class 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 238000011552 rat model Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 229960002385 streptomycin sulfate Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
-
- 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
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (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
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Molecular Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US20180000P | 2000-05-04 | 2000-05-04 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ZA200208835B true ZA200208835B (en) | 2004-02-09 |
Family
ID=22747352
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ZA200208835A ZA200208835B (en) | 2000-05-04 | 2002-10-31 | Compounds and methods for the treatment and prevention of bacterial infection. |
Country Status (15)
| Country | Link |
|---|---|
| US (1) | US7037503B2 (xx) |
| EP (1) | EP1278764A4 (xx) |
| JP (1) | JP2003531841A (xx) |
| KR (1) | KR20030019366A (xx) |
| CN (1) | CN1440419A (xx) |
| AU (1) | AU2001261171A1 (xx) |
| CA (1) | CA2407443A1 (xx) |
| CZ (1) | CZ20023662A3 (xx) |
| HU (1) | HUP0301658A2 (xx) |
| IL (1) | IL152553A0 (xx) |
| MX (1) | MXPA02010826A (xx) |
| NO (1) | NO20025204L (xx) |
| PL (1) | PL365453A1 (xx) |
| WO (1) | WO2001082788A2 (xx) |
| ZA (1) | ZA200208835B (xx) |
Families Citing this family (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6455673B1 (en) * | 1994-06-08 | 2002-09-24 | President And Fellows Of Harvard College | Multi-mutant diphtheria toxin vaccines |
| AU2002239229A1 (en) | 2000-12-05 | 2002-06-18 | Wisconsin Alumni Research Foundation | Receptor for b. anthracis toxin |
| US7763451B2 (en) | 2001-11-09 | 2010-07-27 | The United States Of America As Represented By The Department Of Health And Human Services | Methods for preparing Bacillus anthracis protective antigen for use in vaccines |
| JP2005511059A (ja) * | 2001-12-05 | 2005-04-28 | バートナガー ラケシュ | 非毒性炭疽ワクチンの調製のためのプロセス |
| AU2003213022A1 (en) * | 2002-02-11 | 2003-09-22 | Alexion Pharmaceuticals, Inc. | Immunotherapeutics for biodefense |
| US20040258699A1 (en) * | 2002-02-11 | 2004-12-23 | Bowdish Katherine S. | Immunotherapeutics for biodefense |
| US7201912B2 (en) * | 2002-04-12 | 2007-04-10 | Emergent Biodefense Operation Lansing Inc. | Recombinant immunogenic compositions and methods for protecting against lethal infections from Bacillus anthracis |
| EP1530634A4 (en) | 2002-06-26 | 2005-11-02 | Human Genome Sciences Inc | SHINE-DALGARNO SEQUENCES AND METHODS OF USE |
| US7601351B1 (en) | 2002-06-26 | 2009-10-13 | Human Genome Sciences, Inc. | Antibodies against protective antigen |
| AU2003278776A1 (en) * | 2002-09-10 | 2004-04-30 | Vical Incorporated | Codon-optimized polynucleotide-based vaccines against bacillus anthracis infection |
| AU2003304316A1 (en) * | 2002-11-08 | 2005-01-28 | President And Fellows Of Harvard College | Compounds and methods for the treatment and prevention of bacterial infection |
| US20060014248A1 (en) * | 2003-01-06 | 2006-01-19 | Xencor, Inc. | TNF super family members with altered immunogenicity |
| US20050130892A1 (en) * | 2003-03-07 | 2005-06-16 | Xencor, Inc. | BAFF variants and methods thereof |
| US20050221443A1 (en) * | 2003-01-06 | 2005-10-06 | Xencor, Inc. | Tumor necrosis factor super family agonists |
| US7553930B2 (en) * | 2003-01-06 | 2009-06-30 | Xencor, Inc. | BAFF variants and methods thereof |
| JP4545151B2 (ja) * | 2003-02-06 | 2010-09-15 | シーラス コーポレイション | 非食細胞中への侵入について減弱化されているリステリア、そのリステリアを含むワクチン、およびそれらの使用法 |
| US7695725B2 (en) * | 2003-02-06 | 2010-04-13 | Aduro Biotech | Modified free-living microbes, vaccine compositions and methods of use thereof |
| KR101173871B1 (ko) * | 2003-02-06 | 2012-08-16 | 앤저 테라퓨틱스 인코퍼레이티드 | 변형된 독립생존 미생물, 백신 조성물 및 그것의 사용방법 |
| US7842289B2 (en) * | 2003-12-24 | 2010-11-30 | Aduro Biotech | Recombinant nucleic acid molecules, expression cassettes, and bacteria, and methods of use thereof |
| US20100003276A1 (en) * | 2004-12-07 | 2010-01-07 | Hermes Jeffery D | Methods for treating anthrax and inhibiting lethal factor |
| US20080206276A1 (en) * | 2005-07-08 | 2008-08-28 | Michael Otto | Targeting Poly-Gamma-Glutamic Acid to Treat Staphylococcus Epidermidis and Related Infections |
| AU2007259329A1 (en) * | 2006-05-12 | 2007-12-21 | Farris, Darise | Anthrax compositions and methods of use and production |
| WO2009126355A2 (en) * | 2008-01-28 | 2009-10-15 | Baxter International, Inc. | Methods of increasing recombinant production of bacillus anthracis protective antigen |
| US20110110968A1 (en) * | 2009-11-12 | 2011-05-12 | Stanley Goldman | Human optimized Bacillus anthracis protective antigen |
| DK3549949T5 (da) | 2011-04-22 | 2024-09-02 | Wyeth Llc | Sammensætninger vedrørende et mutant Clostridium-difficile-toksin og fremgangsmåder dertil |
| BR122016023101B1 (pt) | 2012-10-21 | 2022-03-22 | Pfizer Inc | Polipeptídeo, composição imunogênica que o compreende, bem como célula recombinante derivada de clostridium difficile |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5792458A (en) * | 1987-10-05 | 1998-08-11 | The United States Of America As Represented By The Department Of Health And Human Services | Mutant diphtheria toxin conjugates |
| US5591631A (en) | 1993-02-12 | 1997-01-07 | The United States Of America As Represented By The Department Of Health And Human Services | Anthrax toxin fusion proteins, nucleic acid encoding same |
| US5677274A (en) * | 1993-02-12 | 1997-10-14 | The Government Of The United States As Represented By The Secretary Of The Department Of Health And Human Services | Anthrax toxin fusion proteins and related methods |
| US5917017A (en) * | 1994-06-08 | 1999-06-29 | President And Fellows Of Harvard College | Diphtheria toxin vaccines bearing a mutated R domain |
| US6455673B1 (en) * | 1994-06-08 | 2002-09-24 | President And Fellows Of Harvard College | Multi-mutant diphtheria toxin vaccines |
| EP0866718A1 (en) | 1995-12-13 | 1998-09-30 | President And Fellows Of Harvard College | Use of toxin peptides and/or affinity handles for the delivering compounds into cells |
| GB9618107D0 (en) * | 1996-08-30 | 1996-10-09 | Secr Defence | Vaccine production |
| AU2771099A (en) | 1998-02-18 | 1999-09-06 | President And Fellows Of Harvard College | Inhibition of toxin translocation |
| US6426231B1 (en) * | 1998-11-18 | 2002-07-30 | The Texas A&M University System | Analyte sensing mediated by adapter/carrier molecules |
| US6413768B1 (en) * | 1998-12-02 | 2002-07-02 | University Of Maryland | Expression plasmids |
| US6329156B1 (en) * | 1999-03-22 | 2001-12-11 | The Regents Of The University Of California | Method for screening inhibitors of the toxicity of Bacillus anthracis |
-
2001
- 2001-05-04 IL IL15255301A patent/IL152553A0/xx unknown
- 2001-05-04 WO PCT/US2001/014372 patent/WO2001082788A2/en not_active Application Discontinuation
- 2001-05-04 CN CN01812400A patent/CN1440419A/zh active Pending
- 2001-05-04 EP EP01935043A patent/EP1278764A4/en not_active Withdrawn
- 2001-05-04 JP JP2001579671A patent/JP2003531841A/ja active Pending
- 2001-05-04 HU HU0301658A patent/HUP0301658A2/hu unknown
- 2001-05-04 MX MXPA02010826A patent/MXPA02010826A/es unknown
- 2001-05-04 US US09/848,909 patent/US7037503B2/en not_active Expired - Fee Related
- 2001-05-04 KR KR1020027014690A patent/KR20030019366A/ko not_active Application Discontinuation
- 2001-05-04 AU AU2001261171A patent/AU2001261171A1/en not_active Abandoned
- 2001-05-04 PL PL01365453A patent/PL365453A1/xx unknown
- 2001-05-04 CA CA002407443A patent/CA2407443A1/en not_active Abandoned
- 2001-05-04 CZ CZ20023662A patent/CZ20023662A3/cs unknown
-
2002
- 2002-10-30 NO NO20025204A patent/NO20025204L/no not_active Application Discontinuation
- 2002-10-31 ZA ZA200208835A patent/ZA200208835B/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CZ20023662A3 (cs) | 2003-04-16 |
| EP1278764A2 (en) | 2003-01-29 |
| CN1440419A (zh) | 2003-09-03 |
| HUP0301658A2 (hu) | 2003-08-28 |
| NO20025204D0 (no) | 2002-10-30 |
| WO2001082788A2 (en) | 2001-11-08 |
| US20020039588A1 (en) | 2002-04-04 |
| PL365453A1 (en) | 2005-01-10 |
| WO2001082788A3 (en) | 2002-07-25 |
| KR20030019366A (ko) | 2003-03-06 |
| WO2001082788A9 (en) | 2002-12-19 |
| NO20025204L (no) | 2002-12-16 |
| IL152553A0 (en) | 2003-05-29 |
| EP1278764A4 (en) | 2004-05-19 |
| CA2407443A1 (en) | 2001-11-08 |
| JP2003531841A (ja) | 2003-10-28 |
| AU2001261171A1 (en) | 2001-11-12 |
| US7037503B2 (en) | 2006-05-02 |
| MXPA02010826A (es) | 2006-03-09 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7037503B2 (en) | Compounds and methods for the treatment and prevention of bacterial infection | |
| US8067015B2 (en) | Methods and compositions for the treatment and prevention of Staphylococcus and other bacterial infections | |
| Sinha et al. | Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus | |
| KR20130093084A (ko) | 단백질 Ａ(ＳｐＡ) 변이체와 관련된 조성물 및 방법 | |
| AU2006257774B2 (en) | Use of Panton-Valentine Leukocidin for treating and preventing Staphylococcus infections | |
| JP6084631B2 (ja) | Ｃｌｏｓｔｒｉｄｉｕｍｄｉｆｆｉｃｉｌｅ毒素ベースのワクチン | |
| KR20110138397A (ko) | 단백질 Ａ(ＳｐＡ) 변이체와 관련된 조성물 및 방법 | |
| KR20120034612A (ko) | 황색 포도상구균에 대한 면역화를 위한 조성물 | |
| EP1037650B1 (en) | Compositions for the treatment of staphylococcus aureus infections | |
| US20140302084A1 (en) | Immunogenic protein conjugates and method for making and using the same | |
| US7901692B2 (en) | Nontypeable Haemophilus influenzae virulence factors | |
| US20160074497A1 (en) | Staphylococcus live cell vaccines | |
| König et al. | Multi-antigen outer membrane vesicle engineering to develop polyvalent vaccines: the Staphylococcus aureus case | |
| US20080152701A1 (en) | Methods and Compositions for the Treatment and Prevention of Staphylococcus Infections | |
| WO2005004791A2 (en) | Compounds and methods for the treatment and prevention of bacterial infection | |
| US20090123458A1 (en) | Protective Antigen Having Fluorinated Histidine Residues | |
| EP1980267A1 (en) | S. pneumoniae transcytosis protein | |
| Caproni et al. | Multi-Antigen Outer Membrane Vesicle Engineering to Develop Polyvalent Vaccines: The | |
| JPH1169982A (ja) | 新規Ｄｉｖ１ｂ |