NZ567312A - Botulinum neurotoxin a protein receptor and uses thereof - Google Patents
Botulinum neurotoxin a protein receptor and uses thereofInfo
- Publication number
- NZ567312A NZ567312A NZ567312A NZ56731206A NZ567312A NZ 567312 A NZ567312 A NZ 567312A NZ 567312 A NZ567312 A NZ 567312A NZ 56731206 A NZ56731206 A NZ 56731206A NZ 567312 A NZ567312 A NZ 567312A
- Authority
- NZ
- New Zealand
- Prior art keywords
- bont
- homo sapiens
- amino acids
- binding
- synaptic vesicle
- Prior art date
Links
- 108010057266 Type A Botulinum Toxins Proteins 0.000 title claims abstract description 15
- 150000001413 amino acids Chemical class 0.000 claims abstract description 113
- 101710084143 Synaptic vesicle glycoprotein 2C Proteins 0.000 claims abstract description 94
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 85
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 77
- 229920001184 polypeptide Polymers 0.000 claims abstract description 76
- 241000282414 Homo sapiens Species 0.000 claims abstract description 70
- 102100030637 Synaptic vesicle glycoprotein 2C Human genes 0.000 claims abstract description 65
- 230000027455 binding Effects 0.000 claims abstract description 61
- 239000012634 fragment Substances 0.000 claims abstract description 49
- 206010029350 Neurotoxicity Diseases 0.000 claims abstract description 27
- 206010044221 Toxic encephalopathy Diseases 0.000 claims abstract description 27
- 230000007135 neurotoxicity Effects 0.000 claims abstract description 27
- 231100000228 neurotoxicity Toxicity 0.000 claims abstract description 27
- 241000124008 Mammalia Species 0.000 claims abstract description 18
- 230000009467 reduction Effects 0.000 claims abstract description 9
- 101710117542 Botulinum neurotoxin type A Proteins 0.000 claims description 143
- 238000000034 method Methods 0.000 claims description 30
- 150000007523 nucleic acids Chemical class 0.000 claims description 29
- 108020004707 nucleic acids Proteins 0.000 claims description 28
- 102000039446 nucleic acids Human genes 0.000 claims description 28
- 102000004169 proteins and genes Human genes 0.000 claims description 26
- 108090000623 proteins and genes Proteins 0.000 claims description 26
- 230000008569 process Effects 0.000 claims description 21
- 210000004027 cell Anatomy 0.000 claims description 18
- 239000013598 vector Substances 0.000 claims description 15
- 102100030701 Synaptic vesicle glycoprotein 2A Human genes 0.000 claims description 12
- 239000000203 mixture Substances 0.000 claims description 11
- 239000003814 drug Substances 0.000 claims description 10
- 230000003993 interaction Effects 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 208000003508 Botulism Diseases 0.000 claims description 8
- 241000193155 Clostridium botulinum Species 0.000 claims description 7
- 241001465754 Metazoa Species 0.000 claims description 7
- 210000000170 cell membrane Anatomy 0.000 claims description 7
- 238000012217 deletion Methods 0.000 claims description 7
- 230000037430 deletion Effects 0.000 claims description 7
- 239000008194 pharmaceutical composition Substances 0.000 claims description 7
- 101000584505 Homo sapiens Synaptic vesicle glycoprotein 2A Proteins 0.000 claims description 6
- 239000002537 cosmetic Substances 0.000 claims description 6
- 238000003780 insertion Methods 0.000 claims description 6
- 230000037431 insertion Effects 0.000 claims description 6
- 231100000566 intoxication Toxicity 0.000 claims description 6
- 230000035987 intoxication Effects 0.000 claims description 6
- 230000000069 prophylactic effect Effects 0.000 claims description 6
- 239000007790 solid phase Substances 0.000 claims description 6
- 238000006467 substitution reaction Methods 0.000 claims description 6
- 230000001225 therapeutic effect Effects 0.000 claims description 6
- 102100030700 Synaptic vesicle glycoprotein 2B Human genes 0.000 claims description 5
- 238000007792 addition Methods 0.000 claims description 5
- 102000037865 fusion proteins Human genes 0.000 claims description 5
- 108020001507 fusion proteins Proteins 0.000 claims description 5
- 238000002360 preparation method Methods 0.000 claims description 5
- 230000000692 anti-sense effect Effects 0.000 claims description 4
- 238000003259 recombinant expression Methods 0.000 claims description 3
- 238000012360 testing method Methods 0.000 claims description 3
- 230000003247 decreasing effect Effects 0.000 claims description 2
- 230000002829 reductive effect Effects 0.000 claims description 2
- 238000004904 shortening Methods 0.000 claims description 2
- 101000584382 Homo sapiens Synaptic vesicle glycoprotein 2C Proteins 0.000 claims 4
- FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 0.000 claims 2
- 241000880493 Leptailurus serval Species 0.000 claims 2
- SHYYAQLDNVHPFT-DLOVCJGASA-N Ala-Asn-Phe Chemical compound C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 SHYYAQLDNVHPFT-DLOVCJGASA-N 0.000 claims 1
- QRHYAUYXBVVDSB-LKXGYXEUSA-N Asn-Cys-Thr Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H]([C@@H](C)O)C(O)=O QRHYAUYXBVVDSB-LKXGYXEUSA-N 0.000 claims 1
- OMSMPWHEGLNQOD-UWVGGRQHSA-N Asn-Phe Chemical compound NC(=O)C[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 OMSMPWHEGLNQOD-UWVGGRQHSA-N 0.000 claims 1
- GWTLRDMPMJCNMH-WHFBIAKZSA-N Asp-Asn-Gly Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(O)=O GWTLRDMPMJCNMH-WHFBIAKZSA-N 0.000 claims 1
- VZNOVQKGJQJOCS-SRVKXCTJSA-N Asp-Asp-Tyr Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O VZNOVQKGJQJOCS-SRVKXCTJSA-N 0.000 claims 1
- RXBGWGRSWXOBGK-KKUMJFAQSA-N Asp-Lys-Tyr Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O RXBGWGRSWXOBGK-KKUMJFAQSA-N 0.000 claims 1
- BRRPVTUFESPTCP-ACZMJKKPSA-N Asp-Ser-Glu Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(O)=O BRRPVTUFESPTCP-ACZMJKKPSA-N 0.000 claims 1
- ITGFVUYOLWBPQW-KKHAAJSZSA-N Asp-Thr-Val Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(O)=O ITGFVUYOLWBPQW-KKHAAJSZSA-N 0.000 claims 1
- RKXVTTIQNKPCHU-KKHAAJSZSA-N Asp-Val-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](N)CC(O)=O RKXVTTIQNKPCHU-KKHAAJSZSA-N 0.000 claims 1
- HJXSYJVCMUOUNY-SRVKXCTJSA-N Cys-Ser-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CS)N HJXSYJVCMUOUNY-SRVKXCTJSA-N 0.000 claims 1
- FNXSYBOHALPRHV-ONGXEEELSA-N Gly-Val-Lys Chemical compound NCC(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCCCN FNXSYBOHALPRHV-ONGXEEELSA-N 0.000 claims 1
- MDOBWSFNSNPENN-PMVVWTBXSA-N His-Thr-Gly Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O MDOBWSFNSNPENN-PMVVWTBXSA-N 0.000 claims 1
- 101000584515 Homo sapiens Synaptic vesicle glycoprotein 2B Proteins 0.000 claims 1
- NRQRKMYZONPCTM-CIUDSAMLSA-N Lys-Asp-Ser Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(O)=O NRQRKMYZONPCTM-CIUDSAMLSA-N 0.000 claims 1
- HYSVGEAWTGPMOA-IHRRRGAJSA-N Lys-Pro-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(O)=O HYSVGEAWTGPMOA-IHRRRGAJSA-N 0.000 claims 1
- CTJUSALVKAWFFU-CIUDSAMLSA-N Lys-Ser-Cys Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)O)N CTJUSALVKAWFFU-CIUDSAMLSA-N 0.000 claims 1
- JHNOXVASMSXSNB-WEDXCCLWSA-N Lys-Thr-Gly Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O JHNOXVASMSXSNB-WEDXCCLWSA-N 0.000 claims 1
- STTRPDDKDVKIDF-KKUMJFAQSA-N Met-Glu-Tyr Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 STTRPDDKDVKIDF-KKUMJFAQSA-N 0.000 claims 1
- 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 claims 1
- 108010047562 NGR peptide Proteins 0.000 claims 1
- WMGVYPPIMZPWPN-SRVKXCTJSA-N Phe-Asp-Asn Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)N)C(=O)O)N WMGVYPPIMZPWPN-SRVKXCTJSA-N 0.000 claims 1
- RVRRHFPCEOVRKQ-KKUMJFAQSA-N Phe-His-Asn Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC2=CN=CN2)C(=O)N[C@@H](CC(=O)N)C(=O)O)N RVRRHFPCEOVRKQ-KKUMJFAQSA-N 0.000 claims 1
- RMKGXGPQIPLTFC-KKUMJFAQSA-N Phe-Lys-Asn Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(O)=O RMKGXGPQIPLTFC-KKUMJFAQSA-N 0.000 claims 1
- SCKXGHWQPPURGT-KKUMJFAQSA-N Phe-Lys-Ser Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O SCKXGHWQPPURGT-KKUMJFAQSA-N 0.000 claims 1
- AAERWTUHZKLDLC-IHRRRGAJSA-N Phe-Pro-Asp Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(O)=O AAERWTUHZKLDLC-IHRRRGAJSA-N 0.000 claims 1
- FTVRVZNYIYWJGB-ACZMJKKPSA-N Ser-Asp-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O FTVRVZNYIYWJGB-ACZMJKKPSA-N 0.000 claims 1
- PCMZJFMUYWIERL-ZKWXMUAHSA-N Ser-Val-Asn Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O PCMZJFMUYWIERL-ZKWXMUAHSA-N 0.000 claims 1
- JMZKMSTYXHFYAK-VEVYYDQMSA-N Thr-Arg-Asn Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(=O)N)C(=O)O)N)O JMZKMSTYXHFYAK-VEVYYDQMSA-N 0.000 claims 1
- KRPKYGOFYUNIGM-XVSYOHENSA-N Thr-Asp-Phe Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)N)O KRPKYGOFYUNIGM-XVSYOHENSA-N 0.000 claims 1
- MCDVZTRGHNXTGK-HJGDQZAQSA-N Thr-Met-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(O)=O MCDVZTRGHNXTGK-HJGDQZAQSA-N 0.000 claims 1
- WYLAVUAWOUVUCA-XVSYOHENSA-N Thr-Phe-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O WYLAVUAWOUVUCA-XVSYOHENSA-N 0.000 claims 1
- NZRUWPIYECBYRK-HTUGSXCWSA-N Thr-Phe-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(O)=O)C(O)=O NZRUWPIYECBYRK-HTUGSXCWSA-N 0.000 claims 1
- XVHAUVJXBFGUPC-RPTUDFQQSA-N Thr-Tyr-Phe Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O XVHAUVJXBFGUPC-RPTUDFQQSA-N 0.000 claims 1
- TVOGEPLDNYTAHD-CQDKDKBSSA-N Tyr-Ala-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 TVOGEPLDNYTAHD-CQDKDKBSSA-N 0.000 claims 1
- CWVHKVVKAQIJKY-ACRUOGEOSA-N Tyr-Lys-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC2=CC=C(C=C2)O)N CWVHKVVKAQIJKY-ACRUOGEOSA-N 0.000 claims 1
- BRPKEERLGYNCNC-NHCYSSNCSA-N Val-Glu-Arg Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N BRPKEERLGYNCNC-NHCYSSNCSA-N 0.000 claims 1
- PDDJTOSAVNRJRH-UNQGMJICSA-N Val-Thr-Phe Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)NC(=O)[C@H](C(C)C)N)O PDDJTOSAVNRJRH-UNQGMJICSA-N 0.000 claims 1
- 108010040443 aspartyl-aspartic acid Proteins 0.000 claims 1
- 108010057952 lysyl-phenylalanyl-lysine Proteins 0.000 claims 1
- 108010073025 phenylalanylphenylalanine Proteins 0.000 claims 1
- 108030001720 Bontoxilysin Proteins 0.000 description 19
- 239000003795 chemical substances by application Substances 0.000 description 15
- 239000012528 membrane Substances 0.000 description 15
- 102000005962 receptors Human genes 0.000 description 12
- 210000002569 neuron Anatomy 0.000 description 11
- 239000002581 neurotoxin Substances 0.000 description 11
- 231100000618 neurotoxin Toxicity 0.000 description 11
- 108020003175 receptors Proteins 0.000 description 11
- 101710117524 Botulinum neurotoxin type B Proteins 0.000 description 9
- 108030001722 Tentoxilysin Proteins 0.000 description 9
- 231100001103 botulinum neurotoxin Toxicity 0.000 description 9
- 210000002504 synaptic vesicle Anatomy 0.000 description 9
- 150000002270 gangliosides Chemical class 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 102000005720 Glutathione transferase Human genes 0.000 description 6
- 108010070675 Glutathione transferase Proteins 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 101710084141 Synaptic vesicle glycoprotein 2A Proteins 0.000 description 6
- 239000011325 microbead Substances 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 241001112695 Clostridiales Species 0.000 description 5
- 101710138657 Neurotoxin Proteins 0.000 description 5
- 229920002684 Sepharose Polymers 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 102000003137 synaptotagmin Human genes 0.000 description 5
- 108060008004 synaptotagmin Proteins 0.000 description 5
- 206010033799 Paralysis Diseases 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 101710084139 Synaptic vesicle glycoprotein 2B Proteins 0.000 description 4
- 102000004874 Synaptophysin Human genes 0.000 description 4
- 108090001076 Synaptophysin Proteins 0.000 description 4
- 102100035596 Synaptoporin Human genes 0.000 description 4
- 101710146449 Synaptoporin Proteins 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 210000000172 cytosol Anatomy 0.000 description 4
- 230000028023 exocytosis Effects 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 238000011537 Coomassie blue staining Methods 0.000 description 3
- 108090000288 Glycoproteins Proteins 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 102000005280 Synaptogyrin Human genes 0.000 description 3
- 108010057722 Synaptosomal-Associated Protein 25 Proteins 0.000 description 3
- 102000004183 Synaptosomal-Associated Protein 25 Human genes 0.000 description 3
- 108010055445 Synaptotagmin II Proteins 0.000 description 3
- 102100036151 Synaptotagmin-2 Human genes 0.000 description 3
- 102000013265 Syntaxin 1 Human genes 0.000 description 3
- 108010090618 Syntaxin 1 Proteins 0.000 description 3
- 102000003786 Vesicle-associated membrane protein 2 Human genes 0.000 description 3
- 108090000169 Vesicle-associated membrane protein 2 Proteins 0.000 description 3
- 239000005557 antagonist Substances 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 231100000668 minimum lethal dose Toxicity 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 108060008001 synaptogyrin Proteins 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 102000005917 R-SNARE Proteins Human genes 0.000 description 2
- 108010005730 R-SNARE Proteins Proteins 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- OIPILFWXSMYKGL-UHFFFAOYSA-N acetylcholine Chemical compound CC(=O)OCC[N+](C)(C)C OIPILFWXSMYKGL-UHFFFAOYSA-N 0.000 description 2
- 229960004373 acetylcholine Drugs 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000008602 contraction Effects 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 210000004412 neuroendocrine cell Anatomy 0.000 description 2
- 230000001769 paralizing effect Effects 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 230000003518 presynaptic effect Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000010379 pull-down assay Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 108020001568 subdomains Proteins 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101710117515 Botulinum neurotoxin type E Proteins 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 241000186542 Clostridium baratii Species 0.000 description 1
- 101000933563 Clostridium botulinum Botulinum neurotoxin type G Proteins 0.000 description 1
- 101000985023 Clostridium botulinum C phage Botulinum neurotoxin type C Proteins 0.000 description 1
- 241000193171 Clostridium butyricum Species 0.000 description 1
- 241000193449 Clostridium tetani Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 241001596967 Escherichia coli M15 Species 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
- 108010024636 Glutathione Proteins 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 208000008454 Hyperhidrosis Diseases 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- FFEARJCKVFRZRR-UHFFFAOYSA-N L-Methionine Natural products CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 208000007101 Muscle Cramp Diseases 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 101710118538 Protease Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 239000012722 SDS sample buffer Substances 0.000 description 1
- 208000005392 Spasm Diseases 0.000 description 1
- 108010055170 Synaptotagmin I Proteins 0.000 description 1
- 102100036417 Synaptotagmin-1 Human genes 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 231100001133 acute intoxication condition Toxicity 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000002869 basic local alignment search tool Methods 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 206010005159 blepharospasm Diseases 0.000 description 1
- 230000000744 blepharospasm Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000008499 blood brain barrier function Effects 0.000 description 1
- 210000001218 blood-brain barrier Anatomy 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 210000005013 brain tissue Anatomy 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000001713 cholinergic effect Effects 0.000 description 1
- 210000002932 cholinergic neuron Anatomy 0.000 description 1
- 230000007012 clinical effect Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229930186900 holotoxin Natural products 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 208000013403 hyperactivity Diseases 0.000 description 1
- 230000037315 hyperhidrosis Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 210000002161 motor neuron Anatomy 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000004118 muscle contraction Effects 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000002232 neuromuscular Effects 0.000 description 1
- 208000018360 neuromuscular disease Diseases 0.000 description 1
- 210000000715 neuromuscular junction Anatomy 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000000578 peripheral nerve Anatomy 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000005191 phase separation Methods 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 210000001995 reticulocyte Anatomy 0.000 description 1
- 238000009666 routine test Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000003699 striated muscle Anatomy 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 210000000106 sweat gland Anatomy 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 210000000225 synapse Anatomy 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 210000002182 synaptic membrane Anatomy 0.000 description 1
- 230000016978 synaptic transmission, cholinergic Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 230000037303 wrinkles Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/33—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Clostridium (G)
-
- 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
- C07K14/70571—Receptors; Cell surface antigens; Cell surface determinants for neuromediators, e.g. serotonin receptor, dopamine receptor
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/02—Drugs for disorders of the nervous system for peripheral neuropathies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/08—Antiepileptics; Anticonvulsants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/02—Antidotes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Biomedical Technology (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Neurology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Cell Biology (AREA)
- Neurosurgery (AREA)
- Pain & Pain Management (AREA)
- Ophthalmology & Optometry (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE102005051789.7A DE102005051789B4 (de) | 2005-10-28 | 2005-10-28 | Der Botulinus Neurotoxin A Proteinrezeptor und seine Anwendungen |
| PCT/EP2006/010420 WO2007048638A2 (de) | 2005-10-28 | 2006-10-30 | Der botulinus neurotoxin a proteinrezeptor und seine anwendungen |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ567312A true NZ567312A (en) | 2011-09-30 |
Family
ID=37770829
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ567312A NZ567312A (en) | 2005-10-28 | 2006-10-30 | Botulinum neurotoxin a protein receptor and uses thereof |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US8476024B2 (https=) |
| EP (1) | EP1940874B1 (https=) |
| JP (1) | JP2009513118A (https=) |
| KR (1) | KR20080068069A (https=) |
| AT (1) | ATE539088T1 (https=) |
| AU (1) | AU2006308122B2 (https=) |
| CA (1) | CA2627457C (https=) |
| DE (1) | DE102005051789B4 (https=) |
| ES (1) | ES2379513T3 (https=) |
| NZ (1) | NZ567312A (https=) |
| WO (1) | WO2007048638A2 (https=) |
| ZA (1) | ZA200803403B (https=) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE102004043009A1 (de) | 2004-09-06 | 2006-03-23 | Toxogen Gmbh | Transportprotein zum Einbringen chemischer Verbindungen in Nervenzellen |
| DE102005019302A1 (de) * | 2005-04-26 | 2006-11-16 | Toxogen Gmbh | Carrier zum Targeting von Nervenzellen |
| US7985554B2 (en) | 2005-10-14 | 2011-07-26 | Wisconsin Alumni Research Foundation | Botulinum neurotoxin A receptor and the use thereof |
| WO2009008916A2 (en) | 2007-03-22 | 2009-01-15 | The Regents Of The University Of Californina | Therapeutic monoclonal antibodies that neutralize botulinum neurotoxins |
| US9000131B2 (en) * | 2008-07-31 | 2015-04-07 | The Regents Of The University Of California | Antibodies that neutralize botulinum neurotoxins |
| US8771707B2 (en) * | 2008-09-30 | 2014-07-08 | Wisconsin Alumni Research Foundation | Botulinum neurotoxin E receptors and uses thereof |
| US9243057B2 (en) | 2010-08-31 | 2016-01-26 | The Regents Of The University Of California | Antibodies for botulinum neurotoxins |
| UA116985C2 (uk) | 2012-05-30 | 2018-06-11 | Президент Енд Феллоуз Оф Гарвард Колледж | Рекомбінантний ботулінічний нейротоксин |
| WO2014079495A1 (en) * | 2012-11-21 | 2014-05-30 | Syntaxin Limited | Methods for the manufacture of proteolytically processed polypeptides |
| PT3274364T (pt) | 2015-03-26 | 2021-11-05 | Harvard College | Neurotoxina botulínica manipulada |
| KR101670188B1 (ko) | 2015-11-09 | 2016-10-27 | 충북대학교 산학협력단 | 보툴리눔 신경독소 ｅ형에 특이적인 폴리펩타이드 및 이의 용도 |
| EP3504226A1 (en) | 2016-08-24 | 2019-07-03 | President and Fellows of Harvard College | Engineered botulinum neurotoxin |
| KR102480965B1 (ko) | 2016-09-13 | 2022-12-26 | 알레간 인코포레이티드 | 안정화된 비단백질 클로스트리듐 독소 조성물 |
| KR101958312B1 (ko) * | 2017-09-06 | 2019-07-02 | 국방과학연구소 | 보툴리눔 a형 독소에 대한 항체 |
| IL272002A (en) | 2020-01-13 | 2021-07-29 | The Israel Institute Of Biological Res Iibr | Methods for identifying anti clostridial neurotoxin compounds |
| WO2023210585A1 (ja) * | 2022-04-25 | 2023-11-02 | 株式会社Jiksak Bioengineering | 標的化剤 |
| WO2025089343A1 (ja) * | 2023-10-25 | 2025-05-01 | 株式会社Jiksak Bioengineering | 抗シナプス小胞糖タンパク質２ｃ抗体 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005016233A2 (en) | 2002-10-31 | 2005-02-24 | Wisconsin Alumni Research Foundation | Botulinum neurotoxin b receptors and use thereof |
| CA2484115C (en) * | 2002-12-03 | 2007-01-30 | Ucb, S.A. | Methods for the identification of agents for the treatment of seizures, neurological diseases, endocrinopathies and hormonal diseases |
| US7985554B2 (en) * | 2005-10-14 | 2011-07-26 | Wisconsin Alumni Research Foundation | Botulinum neurotoxin A receptor and the use thereof |
-
2005
- 2005-10-28 DE DE102005051789.7A patent/DE102005051789B4/de not_active Expired - Fee Related
-
2006
- 2006-10-30 JP JP2008537015A patent/JP2009513118A/ja active Pending
- 2006-10-30 AT AT06806613T patent/ATE539088T1/de active
- 2006-10-30 AU AU2006308122A patent/AU2006308122B2/en not_active Ceased
- 2006-10-30 US US12/084,074 patent/US8476024B2/en active Active
- 2006-10-30 ES ES06806613T patent/ES2379513T3/es active Active
- 2006-10-30 NZ NZ567312A patent/NZ567312A/en not_active IP Right Cessation
- 2006-10-30 WO PCT/EP2006/010420 patent/WO2007048638A2/de not_active Ceased
- 2006-10-30 KR KR1020087011531A patent/KR20080068069A/ko not_active Ceased
- 2006-10-30 CA CA2627457A patent/CA2627457C/en active Active
- 2006-10-30 EP EP06806613A patent/EP1940874B1/de not_active Not-in-force
-
2008
- 2008-04-17 ZA ZA200803403A patent/ZA200803403B/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| US8476024B2 (en) | 2013-07-02 |
| AU2006308122B2 (en) | 2011-06-30 |
| EP1940874A2 (de) | 2008-07-09 |
| EP1940874B1 (de) | 2011-12-28 |
| DE102005051789B4 (de) | 2014-08-07 |
| DE102005051789A1 (de) | 2007-05-10 |
| WO2007048638A2 (de) | 2007-05-03 |
| KR20080068069A (ko) | 2008-07-22 |
| US20090252722A1 (en) | 2009-10-08 |
| ZA200803403B (en) | 2009-02-25 |
| CA2627457C (en) | 2014-05-13 |
| JP2009513118A (ja) | 2009-04-02 |
| WO2007048638A3 (de) | 2007-07-26 |
| CA2627457A1 (en) | 2007-05-03 |
| ES2379513T3 (es) | 2012-04-26 |
| AU2006308122A1 (en) | 2007-05-03 |
| ATE539088T1 (de) | 2012-01-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2627457C (en) | Botulinum neurotoxin a protein receptor and uses thereof | |
| Rummel et al. | Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation‐dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor | |
| Gaisano et al. | Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion. | |
| Rummel et al. | The HCC‐domain of botulinum neurotoxins A and B exhibits a singular ganglioside binding site displaying serotype specific carbohydrate interaction | |
| Dong et al. | Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells | |
| Leveque et al. | Purification of the N-type calcium channel associated with syntaxin and synaptotagmin. A complex implicated in synaptic vesicle exocytosis. | |
| AU2007347781B2 (en) | Modified clostridial toxins with enhanced translocation capability and enhanced targeting activity | |
| AU2010267963B2 (en) | Neurotoxins exhibiting shortened biological activity | |
| US7491799B2 (en) | Modified botulinum neurotoxins | |
| Fan et al. | Differential effects of pro‐BDNF on sensory neurons after sciatic nerve transection in neonatal rats | |
| US20220033447A1 (en) | Engineered botulinum neurotoxin | |
| US20090118475A1 (en) | Clostridial Neurotoxin Compositions and Modified Clostridial Neurotoxins | |
| JP2008538902A (ja) | 神経細胞をターゲッティングするための担体 | |
| KR20020034178A (ko) | 활성화가능한 재조합 신경독 | |
| Wang et al. | Novel chimeras of botulinum and tetanus neurotoxins yield insights into their distinct sites of neuroparalysis | |
| Baldwin et al. | Association of botulinum neurotoxin serotypes a and B with synaptic vesicle protein complexes | |
| JP7458999B2 (ja) | ボツリヌス神経毒バイオハイブリッド | |
| Li et al. | Recombinant forms of tetanus toxin engineered for examining and exploiting neuronal trafficking pathways | |
| Apland et al. | Inhibition of neurotransmitter release by peptides that mimic the N-terminal domain of SNAP-25 | |
| RU2816855C2 (ru) | Биогибрид ботулинического нейротоксина | |
| WO2021190987A1 (en) | Engineered botulinum neurotoxin serotype e | |
| Rummel | The Dual-Receptor Recognition of Botulinum Neurotoxins: Polysialo-Gangliosides and Synaptic Vesicle Proteins Mediate the Neuronal Entry of Botulinum Neurotoxins by Binding to its C-terminal 50-kDa HC fragment | |
| Larsen | The role of calcium ion-dependent interactions between synaptotagmin and SNARE complexes in regulated exocytosis | |
| Olivares et al. | glycine. zyxwvutsrqponml | |
| Yan | Structure-activity Relationship of CbnB2 and LeuA, and the Search for the Putative Receptor of LeuA. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PSEA | Patent sealed | ||
| RENW | Renewal (renewal fees accepted) | ||
| RENW | Renewal (renewal fees accepted) |
Free format text: PATENT RENEWED FOR 3 YEARS UNTIL 30 OCT 2016 BY JAMES + WELLS Effective date: 20131009 |
|
| LAPS | Patent lapsed |