IL100121A - Recombinant avirulent salmonella that express gamete-specific antigens and antifertility vaccines thereof - Google Patents
Recombinant avirulent salmonella that express gamete-specific antigens and antifertility vaccines thereofInfo
- Publication number
- IL100121A IL100121A IL100121A IL10012191A IL100121A IL 100121 A IL100121 A IL 100121A IL 100121 A IL100121 A IL 100121A IL 10012191 A IL10012191 A IL 10012191A IL 100121 A IL100121 A IL 100121A
- Authority
- IL
- Israel
- Prior art keywords
- microbe
- avirulent
- gamete
- ldh
- acrp
- Prior art date
Links
- 102000036639 antigens Human genes 0.000 title claims abstract description 128
- 108091007433 antigens Proteins 0.000 title claims abstract description 128
- 239000000427 antigen Substances 0.000 title claims abstract description 126
- 229960005486 vaccine Drugs 0.000 title claims description 44
- 241000607142 Salmonella Species 0.000 title claims description 24
- 230000003509 anti-fertility effect Effects 0.000 title description 11
- 239000000203 mixture Substances 0.000 claims abstract description 26
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims abstract description 7
- 238000003259 recombinant expression Methods 0.000 claims abstract description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 142
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 claims description 54
- 101150006779 crp gene Proteins 0.000 claims description 35
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 18
- 230000004720 fertilization Effects 0.000 claims description 14
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 13
- 229920001184 polypeptide Polymers 0.000 claims description 11
- 230000001939 inductive effect Effects 0.000 claims description 6
- 101710154303 Cyclic AMP receptor protein Proteins 0.000 claims description 5
- 101150084863 cya gene Proteins 0.000 claims description 5
- 101710088194 Dehydrogenase Proteins 0.000 claims description 4
- 108060000200 adenylate cyclase Proteins 0.000 claims description 4
- 102000030621 adenylate cyclase Human genes 0.000 claims description 4
- 230000002759 chromosomal effect Effects 0.000 claims description 2
- 244000000010 microbial pathogen Species 0.000 claims description 2
- 230000016379 mucosal immune response Effects 0.000 claims description 2
- 239000004098 Tetracycline Substances 0.000 description 80
- 229960002180 tetracycline Drugs 0.000 description 80
- 229930101283 tetracycline Natural products 0.000 description 80
- 235000019364 tetracycline Nutrition 0.000 description 80
- 150000003522 tetracyclines Chemical class 0.000 description 80
- 230000035772 mutation Effects 0.000 description 71
- 239000013612 plasmid Substances 0.000 description 62
- 241000699670 Mus sp. Species 0.000 description 61
- 239000013598 vector Substances 0.000 description 61
- 238000000034 method Methods 0.000 description 58
- 235000018102 proteins Nutrition 0.000 description 55
- 102000004169 proteins and genes Human genes 0.000 description 55
- DGMPVYSXXIOGJY-UHFFFAOYSA-N Fusaric acid Chemical compound CCCCC1=CC=C(C(O)=O)N=C1 DGMPVYSXXIOGJY-UHFFFAOYSA-N 0.000 description 52
- 210000004027 cell Anatomy 0.000 description 49
- 108091026890 Coding region Proteins 0.000 description 35
- 241000282414 Homo sapiens Species 0.000 description 35
- 229960000723 ampicillin Drugs 0.000 description 35
- 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 35
- 238000010276 construction Methods 0.000 description 35
- 230000004927 fusion Effects 0.000 description 32
- 108020004414 DNA Proteins 0.000 description 31
- 230000003053 immunization Effects 0.000 description 30
- 101100270918 Drosophila melanogaster Arp6 gene Proteins 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 28
- 238000012217 deletion Methods 0.000 description 28
- 239000012634 fragment Substances 0.000 description 28
- 229940024606 amino acid Drugs 0.000 description 27
- 230000037430 deletion Effects 0.000 description 27
- 238000002649 immunization Methods 0.000 description 27
- 108020004705 Codon Proteins 0.000 description 26
- 150000001413 amino acids Chemical class 0.000 description 26
- 230000028993 immune response Effects 0.000 description 24
- 238000010367 cloning Methods 0.000 description 23
- 230000012010 growth Effects 0.000 description 22
- 230000001018 virulence Effects 0.000 description 22
- 241001465754 Metazoa Species 0.000 description 21
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 20
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 20
- 102000037865 fusion proteins Human genes 0.000 description 19
- 108020001507 fusion proteins Proteins 0.000 description 19
- 241000894006 Bacteria Species 0.000 description 18
- 230000015572 biosynthetic process Effects 0.000 description 18
- 238000011081 inoculation Methods 0.000 description 18
- 238000003786 synthesis reaction Methods 0.000 description 18
- 238000010361 transduction Methods 0.000 description 18
- 230000026683 transduction Effects 0.000 description 18
- 239000006154 MacConkey agar Substances 0.000 description 17
- 230000035945 sensitivity Effects 0.000 description 17
- 229920001817 Agar Polymers 0.000 description 16
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 16
- 239000008272 agar Substances 0.000 description 16
- 238000003780 insertion Methods 0.000 description 16
- 230000037431 insertion Effects 0.000 description 16
- 210000001519 tissue Anatomy 0.000 description 16
- 125000003275 alpha amino acid group Chemical group 0.000 description 15
- 230000001580 bacterial effect Effects 0.000 description 15
- 238000002474 experimental method Methods 0.000 description 15
- 230000002068 genetic effect Effects 0.000 description 15
- 238000004519 manufacturing process Methods 0.000 description 15
- 241000588724 Escherichia coli Species 0.000 description 14
- 241000283973 Oryctolagus cuniculus Species 0.000 description 14
- 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 14
- 239000000047 product Substances 0.000 description 14
- 101150098466 rpsL gene Proteins 0.000 description 14
- 230000003248 secreting effect Effects 0.000 description 14
- 241001529936 Murinae Species 0.000 description 13
- 239000002299 complementary DNA Substances 0.000 description 13
- 239000000523 sample Substances 0.000 description 13
- GMKMEZVLHJARHF-UHFFFAOYSA-N (2R,6R)-form-2.6-Diaminoheptanedioic acid Natural products OC(=O)C(N)CCCC(N)C(O)=O GMKMEZVLHJARHF-UHFFFAOYSA-N 0.000 description 12
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 12
- 108091028043 Nucleic acid sequence Proteins 0.000 description 12
- 230000027455 binding Effects 0.000 description 12
- 239000006166 lysate Substances 0.000 description 12
- GMKMEZVLHJARHF-SYDPRGILSA-N meso-2,6-diaminopimelic acid Chemical compound [O-]C(=O)[C@@H]([NH3+])CCC[C@@H]([NH3+])C([O-])=O GMKMEZVLHJARHF-SYDPRGILSA-N 0.000 description 12
- 101150063569 slgA gene Proteins 0.000 description 12
- 210000004899 c-terminal region Anatomy 0.000 description 11
- 230000036039 immunity Effects 0.000 description 11
- 230000005847 immunogenicity Effects 0.000 description 11
- 239000002609 medium Substances 0.000 description 11
- 210000001322 periplasm Anatomy 0.000 description 11
- 238000000746 purification Methods 0.000 description 11
- 238000012216 screening Methods 0.000 description 11
- 108091034117 Oligonucleotide Proteins 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 230000000680 avirulence Effects 0.000 description 10
- 101150105804 cysG gene Proteins 0.000 description 10
- 101150032598 hisG gene Proteins 0.000 description 10
- 230000004044 response Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 238000002965 ELISA Methods 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 9
- 230000000295 complement effect Effects 0.000 description 9
- 238000009795 derivation Methods 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- 208000015181 infectious disease Diseases 0.000 description 9
- 239000002773 nucleotide Substances 0.000 description 9
- 125000003729 nucleotide group Chemical group 0.000 description 9
- 230000001717 pathogenic effect Effects 0.000 description 9
- 230000001105 regulatory effect Effects 0.000 description 9
- 210000000952 spleen Anatomy 0.000 description 9
- 241001515965 unidentified phage Species 0.000 description 9
- 239000003981 vehicle Substances 0.000 description 9
- 238000001262 western blot Methods 0.000 description 9
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 230000000890 antigenic effect Effects 0.000 description 8
- 210000000349 chromosome Anatomy 0.000 description 8
- 230000035558 fertility Effects 0.000 description 8
- 210000000987 immune system Anatomy 0.000 description 8
- 230000002163 immunogen Effects 0.000 description 8
- 230000000644 propagated effect Effects 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 210000004340 zona pellucida Anatomy 0.000 description 8
- 238000011725 BALB/c mouse Methods 0.000 description 7
- 108020005038 Terminator Codon Proteins 0.000 description 7
- 230000001419 dependent effect Effects 0.000 description 7
- 238000009396 hybridization Methods 0.000 description 7
- 230000006698 induction Effects 0.000 description 7
- 208000000509 infertility Diseases 0.000 description 7
- 230000036512 infertility Effects 0.000 description 7
- 230000003204 osmotic effect Effects 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 230000035939 shock Effects 0.000 description 7
- 238000010561 standard procedure Methods 0.000 description 7
- 238000013519 translation Methods 0.000 description 7
- 241001244729 Apalis Species 0.000 description 6
- 239000004475 Arginine Substances 0.000 description 6
- 108010010803 Gelatin Proteins 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- 101000976442 Homo sapiens Zona pellucida sperm-binding protein 3 Proteins 0.000 description 6
- 102100023634 Zona pellucida sperm-binding protein 3 Human genes 0.000 description 6
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 6
- 239000007975 buffered saline Substances 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- 238000010586 diagram Methods 0.000 description 6
- 201000010099 disease Diseases 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 239000008273 gelatin Substances 0.000 description 6
- 229920000159 gelatin Polymers 0.000 description 6
- 235000019322 gelatine Nutrition 0.000 description 6
- 235000011852 gelatine desserts Nutrition 0.000 description 6
- 231100000535 infertility Toxicity 0.000 description 6
- 238000002955 isolation Methods 0.000 description 6
- 230000004899 motility Effects 0.000 description 6
- 210000004681 ovum Anatomy 0.000 description 6
- 101150079601 recA gene Proteins 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 238000003860 storage Methods 0.000 description 6
- 241000271566 Aves Species 0.000 description 5
- 108010028554 LDL Cholesterol Proteins 0.000 description 5
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 239000013599 cloning vector Substances 0.000 description 5
- 210000003495 flagella Anatomy 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 229940099472 immunoglobulin a Drugs 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 238000007912 intraperitoneal administration Methods 0.000 description 5
- 238000007899 nucleic acid hybridization Methods 0.000 description 5
- 108091033319 polynucleotide Proteins 0.000 description 5
- 102000040430 polynucleotide Human genes 0.000 description 5
- 239000002157 polynucleotide Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000001681 protective effect Effects 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 229920000936 Agarose Polymers 0.000 description 4
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 4
- 102000004594 DNA Polymerase I Human genes 0.000 description 4
- 108010017826 DNA Polymerase I Proteins 0.000 description 4
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 4
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 4
- 101001130171 Homo sapiens L-lactate dehydrogenase C chain Proteins 0.000 description 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
- 102100031357 L-lactate dehydrogenase C chain Human genes 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 241000282898 Sus scrofa Species 0.000 description 4
- 241001467018 Typhis Species 0.000 description 4
- 210000003719 b-lymphocyte Anatomy 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 230000007423 decrease Effects 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 230000002496 gastric effect Effects 0.000 description 4
- 210000001035 gastrointestinal tract Anatomy 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 230000036961 partial effect Effects 0.000 description 4
- 230000006798 recombination Effects 0.000 description 4
- 238000005215 recombination Methods 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 230000002441 reversible effect Effects 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- 210000001550 testis Anatomy 0.000 description 4
- 229920000856 Amylose Polymers 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 3
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 3
- 108010000912 Egg Proteins Proteins 0.000 description 3
- 102000002322 Egg Proteins Human genes 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000283073 Equus caballus Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 108010074860 Factor Xa Proteins 0.000 description 3
- -1 LDH-C Proteins 0.000 description 3
- 241001625930 Luria Species 0.000 description 3
- 239000006137 Luria-Bertani broth Substances 0.000 description 3
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 3
- 102100023058 NHP2-like protein 1 Human genes 0.000 description 3
- 101710177157 NHP2-like protein 1 Proteins 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 101100217185 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) aruC gene Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 241001138501 Salmonella enterica Species 0.000 description 3
- 241001354013 Salmonella enterica subsp. enterica serovar Enteritidis Species 0.000 description 3
- 241000607683 Salmonella enterica subsp. enterica serovar Pullorum Species 0.000 description 3
- 101100022072 Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) lysJ gene Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 230000030120 acrosome reaction Effects 0.000 description 3
- 238000005273 aeration Methods 0.000 description 3
- 239000000443 aerosol Substances 0.000 description 3
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 3
- 101150050866 argD gene Proteins 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 3
- 229910052799 carbon Inorganic materials 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 210000003756 cervix mucus Anatomy 0.000 description 3
- 239000011248 coating agent Substances 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 231100000502 fertility decrease Toxicity 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 238000012224 gene deletion Methods 0.000 description 3
- 210000004907 gland Anatomy 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 238000011835 investigation Methods 0.000 description 3
- 238000012423 maintenance Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 150000007523 nucleic acids Chemical group 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 238000002515 oligonucleotide synthesis Methods 0.000 description 3
- 230000002611 ovarian Effects 0.000 description 3
- 210000001986 peyer's patch Anatomy 0.000 description 3
- 230000012743 protein tagging Effects 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 231100000765 toxin Toxicity 0.000 description 3
- 230000002463 transducing effect Effects 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 108010077805 Bacterial Proteins Proteins 0.000 description 2
- 108010023063 Bacto-peptone Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 102000009016 Cholera Toxin Human genes 0.000 description 2
- 108010049048 Cholera Toxin Proteins 0.000 description 2
- 108091035707 Consensus sequence Proteins 0.000 description 2
- IVOMOUWHDPKRLL-KQYNXXCUSA-N Cyclic adenosine monophosphate Chemical compound C([C@H]1O2)OP(O)(=O)O[C@H]1[C@@H](O)[C@@H]2N1C(N=CN=C2N)=C2N=C1 IVOMOUWHDPKRLL-KQYNXXCUSA-N 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- 108010086093 Mung Bean Nuclease Proteins 0.000 description 2
- XMBSYZWANAQXEV-UHFFFAOYSA-N N-alpha-L-glutamyl-L-phenylalanine Natural products OC(=O)CCC(N)C(=O)NC(C(O)=O)CC1=CC=CC=C1 XMBSYZWANAQXEV-UHFFFAOYSA-N 0.000 description 2
- 101710163270 Nuclease Proteins 0.000 description 2
- 241000282520 Papio Species 0.000 description 2
- 241000235070 Saccharomyces Species 0.000 description 2
- 241000392514 Salmonella enterica subsp. enterica serovar Dublin Species 0.000 description 2
- 241000293871 Salmonella enterica subsp. enterica serovar Typhi Species 0.000 description 2
- 241001607429 Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 Species 0.000 description 2
- 229940124842 Salmonella vaccine Drugs 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 206010041660 Splenomegaly Diseases 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 230000024932 T cell mediated immunity Effects 0.000 description 2
- IVOMOUWHDPKRLL-UHFFFAOYSA-N UNPD107823 Natural products O1C2COP(O)(=O)OC2C(O)C1N1C(N=CN=C2N)=C2N=C1 IVOMOUWHDPKRLL-UHFFFAOYSA-N 0.000 description 2
- 108010074006 Zona Pellucida Glycoproteins Proteins 0.000 description 2
- 102000008937 Zona Pellucida Glycoproteins Human genes 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 230000004520 agglutination Effects 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 208000006424 autoimmune oophoritis Diseases 0.000 description 2
- 238000003287 bathing Methods 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000001925 catabolic effect Effects 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 230000001332 colony forming effect Effects 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 238000012790 confirmation Methods 0.000 description 2
- 229940095074 cyclic amp Drugs 0.000 description 2
- 230000006735 deficit Effects 0.000 description 2
- 230000002939 deleterious effect Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 230000003467 diminishing effect Effects 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 230000009931 harmful effect Effects 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 210000002443 helper t lymphocyte Anatomy 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
- 238000005286 illumination Methods 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 239000000411 inducer Substances 0.000 description 2
- 208000021267 infertility disease Diseases 0.000 description 2
- 230000009545 invasion Effects 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000001483 mobilizing effect Effects 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 210000002850 nasal mucosa Anatomy 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 238000007747 plating Methods 0.000 description 2
- 235000021251 pulses Nutrition 0.000 description 2
- 101150002589 recF gene Proteins 0.000 description 2
- 210000005000 reproductive tract Anatomy 0.000 description 2
- 230000000241 respiratory effect Effects 0.000 description 2
- 210000003296 saliva Anatomy 0.000 description 2
- 239000006152 selective media Substances 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000013112 stability test Methods 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 230000002381 testicular Effects 0.000 description 2
- 230000005030 transcription termination Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 101150010782 trpp-3 gene Proteins 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 230000035899 viability Effects 0.000 description 2
- NWXMGUDVXFXRIG-WESIUVDSSA-N (4s,4as,5as,6s,12ar)-4-(dimethylamino)-1,6,10,11,12a-pentahydroxy-6-methyl-3,12-dioxo-4,4a,5,5a-tetrahydrotetracene-2-carboxamide Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(=O)C(C(N)=O)=C(O)[C@@]4(O)C(=O)C3=C(O)C2=C1O NWXMGUDVXFXRIG-WESIUVDSSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- WWSJZGAPAVMETJ-UHFFFAOYSA-N 2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-3-ethoxypyrazol-1-yl]-1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C=1C(=NN(C=1)CC(=O)N1CC2=C(CC1)NN=N2)OCC WWSJZGAPAVMETJ-UHFFFAOYSA-N 0.000 description 1
- QHKABHOOEWYVLI-UHFFFAOYSA-N 3-methyl-2-oxobutanoic acid Chemical compound CC(C)C(=O)C(O)=O QHKABHOOEWYVLI-UHFFFAOYSA-N 0.000 description 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- DLQPMEMYCIGJIM-UHFFFAOYSA-N Adjuvant peptide Natural products CC(NC(=O)CCOC1C(O)C(CO)OC(O)C1NC(=O)C)C(=O)NC(CCC(=O)O)C(=O)N DLQPMEMYCIGJIM-UHFFFAOYSA-N 0.000 description 1
- 241001167018 Aroa Species 0.000 description 1
- SNYCNNPOFYBCEK-ZLUOBGJFSA-N Asn-Ser-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O SNYCNNPOFYBCEK-ZLUOBGJFSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 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
- 101100216993 Bacillus subtilis (strain 168) aroD gene Proteins 0.000 description 1
- 241000701822 Bovine papillomavirus Species 0.000 description 1
- 238000009631 Broth culture Methods 0.000 description 1
- 101150003886 CRYZ gene Proteins 0.000 description 1
- 101100310222 Caenorhabditis briggsae she-1 gene Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241000251556 Chordata Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010073254 Colicins Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000938605 Crocodylia Species 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 101100491986 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) aromA gene Proteins 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 102000009338 Gastric Mucins Human genes 0.000 description 1
- 108010009066 Gastric Mucins Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 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
- 206010019842 Hepatomegaly Diseases 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- 108010044467 Isoenzymes Proteins 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 1
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 1
- SHZGCJCMOBCMKK-JFNONXLTSA-N L-rhamnopyranose Chemical compound C[C@@H]1OC(O)[C@H](O)[C@H](O)[C@H]1O SHZGCJCMOBCMKK-JFNONXLTSA-N 0.000 description 1
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 1
- 231100000416 LDH assay Toxicity 0.000 description 1
- AAXCQFOXUJMCCW-PETQGJDISA-N LPS core Chemical compound O([C@H]1[C@H](NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC)[C@H]([C@@H]([C@@H](CO[C@]2(O[C@@H]([C@@H](OC3[C@H]([C@@H](OC4[C@H]([C@@H](OC5[C@@H]([C@@H](O[C@@H]6[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O6)OC6[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O6)O[C@H]6[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O6)NC(C)=O)[C@H](O)[C@@H](CO[C@@H]6[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O6)O)O5)O)[C@H](O)[C@@H]([C@@H](O)COC5[C@H]([C@@H](O)[C@H](OP(O)(O)=O)[C@@H]([C@@H](O)CO)O5)O)O4)O)[C@H](OP(O)(=O)OP(O)(=O)OCCN)[C@@H]([C@@H](O)CO)O3)O)[C@H](O[C@]3(O[C@@H]([C@@H](O)[C@H](O[C@]4(O[C@@H]([C@@H](O)[C@H](OP(O)(=O)OCCN)C4)[C@@H](O)CO)C(O)=O)C3)[C@@H](O)CO)C(O)=O)C2)[C@@H](O)CO)C(O)=O)O1)OP(O)(O)=O)OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC)C[C@H]1O[C@H](OP(O)(O)=O)[C@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H]1O AAXCQFOXUJMCCW-PETQGJDISA-N 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 235000019687 Lamb Nutrition 0.000 description 1
- 241000408529 Libra Species 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- ONGCSGVHCSAATF-CIUDSAMLSA-N Met-Ala-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CCC(O)=O ONGCSGVHCSAATF-CIUDSAMLSA-N 0.000 description 1
- BQHLZUMZOXUWNU-DCAQKATOSA-N Met-Pro-Glu Chemical compound CSCC[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N BQHLZUMZOXUWNU-DCAQKATOSA-N 0.000 description 1
- PQMWYJDJHJQZDE-UHFFFAOYSA-M Methantheline bromide Chemical compound [Br-].C1=CC=C2C(C(=O)OCC[N+](C)(CC)CC)C3=CC=CC=C3OC2=C1 PQMWYJDJHJQZDE-UHFFFAOYSA-M 0.000 description 1
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 1
- 101001130170 Mus musculus L-lactate dehydrogenase C chain Proteins 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010013639 Peptidoglycan Proteins 0.000 description 1
- 108010090127 Periplasmic Proteins Proteins 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 230000004570 RNA-binding Effects 0.000 description 1
- 101100173636 Rattus norvegicus Fhl2 gene Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000531795 Salmonella enterica subsp. enterica serovar Paratyphi A Species 0.000 description 1
- 241000577475 Salmonella enterica subsp. enterica serovar Paratyphi C Species 0.000 description 1
- 241000701835 Salmonella virus P22 Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 210000004712 air sac Anatomy 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 230000009833 antibody interaction Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 230000036528 appetite Effects 0.000 description 1
- 235000019789 appetite Nutrition 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 101150037081 aroA gene Proteins 0.000 description 1
- 101150042732 aroC gene Proteins 0.000 description 1
- 101150102858 aroD gene Proteins 0.000 description 1
- 101150040872 aroE gene Proteins 0.000 description 1
- 101150108612 aroQ gene Proteins 0.000 description 1
- 101150107204 asd gene Proteins 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- WXNRAKRZUCLRBP-UHFFFAOYSA-N avridine Chemical compound CCCCCCCCCCCCCCCCCCN(CCCN(CCO)CCO)CCCCCCCCCCCCCCCCCC WXNRAKRZUCLRBP-UHFFFAOYSA-N 0.000 description 1
- 229950010555 avridine Drugs 0.000 description 1
- 210000003578 bacterial chromosome Anatomy 0.000 description 1
- 230000037429 base substitution Effects 0.000 description 1
- 229960000686 benzalkonium chloride Drugs 0.000 description 1
- CADWTSSKOVRVJC-UHFFFAOYSA-N benzyl(dimethyl)azanium;chloride Chemical compound [Cl-].C[NH+](C)CC1=CC=CC=C1 CADWTSSKOVRVJC-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- DLRVVLDZNNYCBX-ZZFZYMBESA-N beta-melibiose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)O1 DLRVVLDZNNYCBX-ZZFZYMBESA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000000621 bronchi Anatomy 0.000 description 1
- OSQPUMRCKZAIOZ-UHFFFAOYSA-N carbon dioxide;ethanol Chemical compound CCO.O=C=O OSQPUMRCKZAIOZ-UHFFFAOYSA-N 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000001886 ciliary effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 description 1
- 239000012470 diluted sample Substances 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000000688 enterotoxigenic effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 239000006153 eosin methylene blue Substances 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 210000003722 extracellular fluid Anatomy 0.000 description 1
- 101150110316 eya gene Proteins 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000012631 food intake Nutrition 0.000 description 1
- QPJBWNIQKHGLAU-IQZHVAEDSA-N ganglioside GM1 Chemical compound O[C@@H]1[C@@H](O)[C@H](OC[C@H](NC(=O)CCCCCCCCCCCCCCCCC)[C@H](O)\C=C\CCCCCCCCCCCCC)O[C@H](CO)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@]2(O[C@H]([C@H](NC(C)=O)[C@@H](O)C2)[C@H](O)[C@H](O)CO)C(O)=O)[C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O3)O)[C@@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](CO)O1 QPJBWNIQKHGLAU-IQZHVAEDSA-N 0.000 description 1
- 150000002270 gangliosides Chemical class 0.000 description 1
- 210000003736 gastrointestinal content Anatomy 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960002743 glutamine Drugs 0.000 description 1
- 235000004554 glutamine Nutrition 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 101150063579 hisQ gene Proteins 0.000 description 1
- 101150085823 hsdR gene Proteins 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 230000008348 humoral response Effects 0.000 description 1
- 210000003405 ileum Anatomy 0.000 description 1
- 230000009851 immunogenic response Effects 0.000 description 1
- 230000017555 immunoglobulin mediated immune response Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000013383 initial experiment Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 150000004715 keto acids Chemical class 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 238000002843 lactate dehydrogenase assay Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000225 lethality Toxicity 0.000 description 1
- AIHDCSAXVMAMJH-GFBKWZILSA-N levan Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)OC[C@@H]1[C@@H](O)[C@H](O)[C@](CO)(CO[C@@H]2[C@H]([C@H](O)[C@@](O)(CO)O2)O)O1 AIHDCSAXVMAMJH-GFBKWZILSA-N 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000003794 male germ cell Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 210000003470 mitochondria Anatomy 0.000 description 1
- 238000000329 molecular dynamics simulation Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- BSOQXXWZTUDTEL-QAQREVAFSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-QAQREVAFSA-N 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 101150091444 ompR gene Proteins 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 210000000287 oocyte Anatomy 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 210000001539 phagocyte Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 101150028857 phoP gene Proteins 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 244000144977 poultry Species 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000009877 rendering Methods 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 235000017709 saponins Nutrition 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 108010093841 spermadhesin Proteins 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000002627 tracheal intubation Methods 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 229940125575 vaccine candidate Drugs 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 101150075472 ycf27 gene Proteins 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0008—Oxidoreductases (1.) acting on the aldehyde or oxo group of donors (1.2)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- 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
- C12N15/01—Preparation of mutants without inserting foreign genetic material therein; Screening processes therefor
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y102/00—Oxidoreductases acting on the aldehyde or oxo group of donors (1.2)
- C12Y102/01—Oxidoreductases acting on the aldehyde or oxo group of donors (1.2) with NAD+ or NADP+ as acceptor (1.2.1)
- C12Y102/01011—Aspartate-semialdehyde dehydrogenase (1.2.1.11)
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Plant Pathology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US61572090A | 1990-11-21 | 1990-11-21 | |
| US79134791A | 1991-11-18 | 1991-11-18 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IL100121A true IL100121A (en) | 1998-06-15 |
Family
ID=27087577
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL100121A IL100121A (en) | 1990-11-21 | 1991-11-21 | Recombinant avirulent salmonella that express gamete-specific antigens and antifertility vaccines thereof |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US5656488A (fr) |
| EP (1) | EP0558631B1 (fr) |
| AT (1) | ATE177787T1 (fr) |
| AU (1) | AU9094191A (fr) |
| CA (1) | CA2096529C (fr) |
| DE (1) | DE69131014T2 (fr) |
| ES (1) | ES2133311T3 (fr) |
| IL (1) | IL100121A (fr) |
| WO (1) | WO1992009684A1 (fr) |
Families Citing this family (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1992008486A1 (fr) * | 1990-11-09 | 1992-05-29 | Washington University | Microbes avirulents et leurs applications: salmonella typhi |
| US5480799A (en) * | 1993-12-10 | 1996-01-02 | The University Of North Carolina At Chapel Hill | Sperm antigen corresponding to a sperm zona binding protein autoantigenic epitope |
| ATE312934T1 (de) * | 1995-06-07 | 2005-12-15 | Univ Washington | Rekombinant bakterielle system mit umweltbeschränkte lebensfähigkeit |
| US5922583A (en) * | 1995-10-17 | 1999-07-13 | Biostar Inc. | Methods for production of recombinant plasmids |
| DE69734605T2 (de) * | 1997-04-18 | 2006-08-03 | GESELLSCHAFT FüR BIOTECHNOLOGISCHE FORSCHUNG MBH (GBF) | Abgeschwächter salmonellenstamm, gebraucht als vehikel zur oralen immunisierung |
| DE19720761A1 (de) * | 1997-05-07 | 1998-11-12 | Schering Ag | Verfahren zur Synthese und Sekretion von zur Kontrazeption geeigneter Proteine oder Proteinfragmente durch attenuierte Salmonellen oder einen anderen Gram-negativen attenuierten Impfstamm zur Erzeugung einer oralen Vakzinierung |
| US6024961A (en) | 1997-11-14 | 2000-02-15 | Washington University | Recombinant avirulent immunogenic S typhi having rpos positive phenotype |
| AU1765300A (en) * | 1998-12-22 | 2000-07-12 | Dalhousie University | Compositions and methods for reducing or preventing fertilization in fish and birds |
| WO2001002000A2 (fr) * | 1999-07-01 | 2001-01-11 | The University Of Georgia Research Foundation, Inc. | Procede et composition permettant d'affecter les systemes de reproduction |
| US6846488B2 (en) * | 2000-04-03 | 2005-01-25 | The Uab Research Foundation | Chimeric antigen-enterotoxin mucosal immunogens |
| US6780405B1 (en) | 2000-04-28 | 2004-08-24 | Avant Immunotherapeutics, Inc. | Regulated antigen delivery system (RADS) |
| US6872547B1 (en) | 2000-10-11 | 2005-03-29 | Washington University | Functional balanced-lethal host-vector systems |
| ES2316492T3 (es) * | 2000-11-16 | 2009-04-16 | Intervet International Bv | Vacuna contra la salmonella. |
| US20040137003A1 (en) * | 2001-04-30 | 2004-07-15 | Curtiss Iii Roy | Regulated antigen delivery system (rads) |
| US20050096283A1 (en) * | 2001-12-14 | 2005-05-05 | The Regents Of University Of California | Methods of inhibiting fertility |
| US20050009188A1 (en) * | 2002-09-19 | 2005-01-13 | Kitto G. Barrie | Animal immunocontraceptives expressed in plants and uses thereof |
| WO2004062597A2 (fr) * | 2003-01-09 | 2004-07-29 | The Trustees Of The University Of Pennsylvania | Compositions, methodes et trousses renforçant l'immunogenecite d'un vecteur de vaccin bacterien |
| WO2005093043A1 (fr) * | 2004-02-27 | 2005-10-06 | Research Development Foundation | Vaccins immunocontraceptifs par adn et utilisations de ceux-ci |
| WO2007106073A2 (fr) | 2006-03-02 | 2007-09-20 | University Of Massachusetts | agents pathogenes modifies a utiliser en tant que vaccins |
| EP2150616A4 (fr) | 2007-05-10 | 2011-07-27 | Univ Arizona | Expression régulée d'antigène et/ou atténuation régulée pour accroître l'immunogénicité et/ou la sécurité de vaccins |
| EP2152883A4 (fr) * | 2007-05-10 | 2010-10-27 | Univ Arizona | Bactéries recombinantes comprenant des vecteurs pour l'expression de séquences d'acide nucléique codant des antigènes |
| US8465755B2 (en) | 2007-10-05 | 2013-06-18 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Recombinant bacterium capable of eliciting an immune response against enteric pathogens |
| WO2010045620A1 (fr) | 2008-10-17 | 2010-04-22 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Bactérie recombinante pouvant éliciter une réponse immunitaire contre le streptococcus pneumoniae |
| US9163219B2 (en) | 2009-04-14 | 2015-10-20 | Arizona Board Of Regents On Behalf Of Arizona State University | Single expression vector for generation of a virus with a segmented genome |
| GB2483595B (en) | 2009-05-22 | 2017-03-29 | The Arizona Board Of Regents For And On Behalf Of Arizona State Univ | Recombinant bacterium and methods of antigen and nucleic acid delivery |
| US9045742B2 (en) | 2009-05-29 | 2015-06-02 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Recombinant Edwardsiella bacterium |
| US9062297B2 (en) | 2010-01-13 | 2015-06-23 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Yersinia pestis vaccine |
| WO2011091291A1 (fr) | 2010-01-22 | 2011-07-28 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Bactérie renfermant un acide nucléique régulé par le rfah |
| US9598697B2 (en) | 2010-05-28 | 2017-03-21 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Recombinant bacterium to decrease tumor growth |
| WO2012003460A2 (fr) | 2010-07-02 | 2012-01-05 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Compositions et procédés pour la lyse bactérienne et la production de lipides neutres |
| US9303264B2 (en) | 2012-05-18 | 2016-04-05 | The Arizona Board Of Regents For And On Behalf Of Arizona State University | Photosynthetic microorganisms expressing thermostable lipase |
| US9580718B2 (en) | 2013-06-17 | 2017-02-28 | Arizona Board Of Regents On Behalf Of Arizona State University | Attenuated live bacteria with increased acid resistance and methods of use thereof |
| US10973908B1 (en) | 2020-05-14 | 2021-04-13 | David Gordon Bermudes | Expression of SARS-CoV-2 spike protein receptor binding domain in attenuated salmonella as a vaccine |
| CN112618706B (zh) * | 2020-11-21 | 2021-09-14 | 青岛博霖生物科技有限公司 | 沙门氏菌、鸭疫里默氏杆菌、大肠埃希氏杆菌病三联疫苗 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3992520A (en) * | 1974-11-27 | 1976-11-16 | Merck & Co., Inc. | Anti-fertility vaccine comprising solubilized zona pellucida and anti-serum |
| US4968619A (en) * | 1976-09-27 | 1990-11-06 | Research Corporation | Modified microorganisms and method of preparing and using same |
| US4190495A (en) * | 1976-09-27 | 1980-02-26 | Research Corporation | Modified microorganisms and method of preparing and using same |
| US4585651A (en) * | 1978-10-17 | 1986-04-29 | Stolle Research & Development Corporation | Active/passive immunization of the internal female reproductive organs |
| US4392997A (en) * | 1981-07-06 | 1983-07-12 | Northwestern University | Antigenic peptide compounds |
| US4888170A (en) * | 1981-10-22 | 1989-12-19 | Research Corporation | Vaccines obtained from antigenic gene products of recombinant genes |
| US4585587A (en) * | 1984-10-19 | 1986-04-29 | Northwestern University | Antigenic peptide compounds |
| US4795634A (en) * | 1986-03-14 | 1989-01-03 | Aphton Corporation | Method for contraception by immunization against the zona pellucida |
| AU8192987A (en) * | 1986-12-01 | 1988-06-16 | Northwestern University | Human ldh-c4 cdna sequences encoding antigenic regions |
| US4996297A (en) * | 1987-10-07 | 1991-02-26 | Zonagen, Inc. | Recombinantly expressed rabbit zona pellucida polypeptides |
| US4990596A (en) * | 1989-02-16 | 1991-02-05 | Northwestern University | Synthetic peptide producing antibodies of enhanced binding to human LDH-C4 |
| CA2058999A1 (fr) * | 1989-06-12 | 1990-12-13 | Jurrien Dean | Vaccin contraceptif base sur un gene clone de la zone pellucide |
| IE912872A1 (en) * | 1990-08-27 | 1992-03-11 | Akzo Nv | Human zona pellucida protein zp3 |
-
1991
- 1991-11-20 CA CA002096529A patent/CA2096529C/fr not_active Expired - Fee Related
- 1991-11-20 EP EP92901072A patent/EP0558631B1/fr not_active Expired - Lifetime
- 1991-11-20 AU AU90941/91A patent/AU9094191A/en not_active Abandoned
- 1991-11-20 ES ES92901072T patent/ES2133311T3/es not_active Expired - Lifetime
- 1991-11-20 DE DE69131014T patent/DE69131014T2/de not_active Expired - Fee Related
- 1991-11-20 WO PCT/US1991/008688 patent/WO1992009684A1/fr active IP Right Grant
- 1991-11-20 AT AT92901072T patent/ATE177787T1/de active
- 1991-11-21 IL IL100121A patent/IL100121A/en active IP Right Grant
-
1994
- 1994-04-01 US US08/222,182 patent/US5656488A/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| US5656488A (en) | 1997-08-12 |
| WO1992009684A1 (fr) | 1992-06-11 |
| CA2096529A1 (fr) | 1992-05-22 |
| DE69131014D1 (de) | 1999-04-22 |
| ATE177787T1 (de) | 1999-04-15 |
| CA2096529C (fr) | 2003-01-21 |
| EP0558631A4 (en) | 1995-11-22 |
| EP0558631A1 (fr) | 1993-09-08 |
| EP0558631B1 (fr) | 1999-03-17 |
| AU9094191A (en) | 1992-06-25 |
| ES2133311T3 (es) | 1999-09-16 |
| DE69131014T2 (de) | 1999-10-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5656488A (en) | Recombinant avirulent salmonella antifertility vaccines | |
| US4888170A (en) | Vaccines obtained from antigenic gene products of recombinant genes | |
| JP3428646B2 (ja) | ジフテリア毒素ワクチン | |
| EP0465560B1 (fr) | VACCINS CONTENANT DES MICROORGANISMES AVIRULENTS DU TYPE phoP | |
| US6936425B1 (en) | Attenuated salmonella SP12 mutants as antigen carriers | |
| US9050285B2 (en) | Recombinant bacterium capable of eliciting an immune response against Streptococcus pneumoniae | |
| CA1338705C (fr) | Vaccins obtenus a partir de genes, antigenes de genes recombinants | |
| US6537558B2 (en) | Methods of producing and using virulence attenuated poxR mutant bacteria | |
| US20050260223A1 (en) | Salmonella vaccine materials and methods | |
| EP1154797A2 (fr) | Vaccins base de toxine dipht rique mutations multiples | |
| EP0584284A1 (fr) | Analogues de sous-unites de toxine du cholera derives d'adn recombine------------------------------------------------------------ | |
| JPH11235191A (ja) | 細胞の遺伝的集団において所望の組換え遺伝子を維持する方法 | |
| AU2001256957A1 (en) | Salmonella vaccine materials and methods | |
| JP3388171B2 (ja) | 淋菌ｐｉタンパク質およびワクチンの製造 | |
| EP0931093B1 (fr) | Vaccin vivant contre helicobacter pylori | |
| EP1443959A1 (fr) | Vaccin anti-salmonella | |
| JPH09507028A (ja) | イエルシニア ペスチス （Ｙｅｒｓｉｎｉａ ｐｅｓｔｉｓ）感染から防御するための生細菌ベクターを含むワクチン組成物 | |
| US20020161192A1 (en) | Helicobacter pylori live vaccine | |
| JPH11501203A (ja) | 大腸菌およびサルモネラ菌中における淋菌ｐｉタンパクおよびワクチンの製造 | |
| US20040241190A1 (en) | Vaccine preparations | |
| AU2002223922A1 (en) | Salmonella vaccine | |
| CZ123699A3 (cs) | Rekombinantní oslabený mikrobiální patogen obsahující alespoň jednu molekulu nukleové kyseliny kódující antigen pocházející z mikroorganizmu Helicobacter |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FF | Patent granted | ||
| KB | Patent renewed | ||
| KB | Patent renewed |