Neurotoxicity of clostridium toxins (Homo sapiens)

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7, 23, 29, 33, 43...16292, 4814, 26, 432912, 29, 31, 326, 41, 5114, 26, 4326, 432929398, 284329, 32, 35, 3714, 26, 431, 18, 3816, 5029, 32, 51, 553, 13, 29, 349, 21, 22, 29, 3213, 29, 32, 344321, 29, 3221, 29, 3210, 30, 423324, 30, 4025, 385, 29, 31, 3212, 29, 32, 35, 3714, 26, 43, 45299, 21, 22, 29, 322919, 47, 49432936, 47, 4927, 47, 49synaptic vesicle lumensynaptic vesicle lumencytosolclathrin-coated endocytic vesicleendocytic vesiclecytosolZn2+ H+Zn2+ BoNT/G HCBoNT/A LC disulfidebonded SYT2 Zn2+ GD3 SV2A SV2A,B,CTeNT HC disulfidebonded BoNT/E HC disulfidebonded BoNT/B HC disulfidebonded Zn2+ GT1bNTNHAGT1bVAMP1BoNT/C:GT1bBoNT/B LC disulfidebonded GD3ha33BoNT/B HC disulfidebonded GM1a SV2A TeNT HCBoNT/F HC disulfidebonded BoNT/C HC:LC dimerSV2A BoNT/F:SV2:GT1bBoNT/A HC:LC dimerBoNT/F LC disulfidebonded Zn2+ SNAP25(1-198)BoNT/E LC:Zn2+BoNT/E LC disulfidebonded GT1b BoNT/F LC Zn2+ ha17 SNAP25SV2A BoNT/E:NTNHASV2B BoNT/C HC disulfidebonded SYT1VAMP1(61-118)GT1b Zn2+ Zn2+ BoNT/D:SV2:GD2BoNT/C LC:Zn2+BoNT/G LC disulfidebonded GT1b VAMP2(59-116)H+BoNT/F HCBoNT/B:NTNHA:HAH+Zn2+ BoNT/A LC SV2C GM1a BoNT/D LC disulfidebonded TeNT:gangliosidesha70BoNT/E HCSV2C BoNT/A LC disulfidebonded Zn2+ GT1bBoNT/B HC disulfidebonded SYT1,2BoNT/E LC BoNT/A:NTNHA:HABoNT/E LC disulfidebonded BoNT/B LC:Zn2+Zn2+ ha17 SNAP25(198-206)VAMP1(84-118)GD3 BoNT/C LC disulfidebonded BoNT/G HC disulfidebonded BoNT/D LC disulfidebonded NTNHABoNT/F LC disulfidebonded GT1b VAMP1(1-83)SV2A SV2A SNAP25(199-206)VAMP2(77-116)BoNT/C LC VAMP2(60-116)BoNT/E:SV2:GT1bSTX1(1-?)TeNT LC disulfidebonded SYT1 VAMP1(62-118)Zn2+ BoNT/G LC disulfidebonded TeNT:gangliosidesBoNT/F LC disulfidebonded GD2 Zn2+ TeNT LC disulfidebonded BoNT/D HC disulfidebonded Zn2+ GT1bSYT1 SV2B BoNT/F:SV2:GT1bVAMP2(2-76)SNAP25(1-198)Zn2+ BoNT/A:SV2:GT1bZn2+ BoNT/C HCBoNT/A HC disulfidebonded Zn2+ BoNT/E HC:LC dimerZn2+ GM1aBoNT/F LC:Zn2+VAMP2(2-81)Zn2+ ha17SYT1,2Zn2+ SV2A,B,CH+H+SYT2 Zn2+ TeNT HC disulfidebonded SV2A,BGT1bTeNT LC NTNHA BoNT/D HC:LC dimerBoNT/A LC disulfidebonded GD2 BoNT/D HCBoNT/D LC disulfidebonded SV2C GT1b BoNT/D LC Zn2+ SV2A,B,CTeNT LC disulfidebonded SNAP25BoNT/G LC:Zn2+BoNT/B LC disulfidebonded GD2BoNT/D HC disulfidebonded GT1b Zn2+ SV2A,B,CSV2B GD3BoNT/F HC:LC dimerSV2C Zn2+ GT1bGT1bBoNT/C LC disulfidebonded BoNT/G:SYT1:GT1bNTNHA STX1(?-288)BoNT/G:SYT1:GT1bSNAP25GT1b GT1b SV2A SNAP25(1-197)GT1b GT1b Zn2+ VAMP1(1-60)GT1bSV2C BoNT/C HC disulfidebonded NTNHA BoNT/B:SYT:GT1bVAMP2(2-59)GT1b SNAP25(199-206)H+Zn2+ VAMP2(2-58)TeNT LC:Zn2+STX1VAMP2(2-76)ha33 SV2B BoNT/B LC disulfidebonded VAMP2VAMP2(77-116)BoNT/A HC disulfidebonded BoNT/B:SYT:GT1bSV2B BoNT/A:SV2:GT1bBoNT/G LC disulfidebonded BoNT/G HC disulfidebonded BoNT/B HC disulfidebonded GD2BoNT/E HC disulfidebonded BoNT/E HC disulfidebonded BoNT/G HC disulfidebonded SV2A,BBoNT/E LC disulfidebonded TeNT HC disulfidebonded BoNT/F HC disulfidebonded GM1a BoNT/C:GT1bZn2+ Zn2+ GT1bBoNT/B HCH+TeNT:gangliosidesBoNT/B LC disulfidebonded BoNT/D HC disulfidebonded VAMP2(82-116)GD3 Zn2+ SV2A,B,CVAMP2SYT1GT1b SV2A Zn2+ SYT1 ha70 BoNT/A HCZn2+ BoNT/G LC TeNT HC disulfidebonded Zn2+ Zn2+ BoNT/A HC disulfidebonded BoNT/F HC disulfidebonded Zn2+ SV2A,B,CBoNT/C HC disulfidebonded BoNT/D LC:Zn2+Zn2+ SV2B H+VAMP1(1-61)GM1aSV2C VAMP1GT1bBoNT/A HC disulfidebonded SV2B BoNT/E HC disulfidebonded ha33 SYT1 TeNT HC:LC dimerBoNT/A LC:Zn2+BoNT/E:SV2:GT1bSV2B TeNT LC disulfidebonded VAMP2GT1bBoNT/B LC ha70 BoNT/A LC disulfidebonded BoNT/E LC disulfidebonded VAMP2BoNT/D:SV2:GD2BoNT/C LC disulfidebonded BoNT/B HC:LC dimerBoNT/G HC:LC dimerZn2+ 30, 405, 3117441920, 542420, 542194320, 5410, 308, 284531820, 54424, 651, 555351, 5512, 3515392, 4817531113, 342753211724111120, 5453171153114, 6, 504, 6, 16, 505353214129, 2113, 3417111241753421120, 541713, 343611116, 4412, 354, 6, 5039945312420, 541721, 25119, 2113, 345, 312151, 55531, 1153244175351, 555320, 5420, 5441117124


Description

Clostridial neurotoxins, when taken up by human neurons, block synaptic transmission by cleaving proteins required for the fusion of synaptic vesicles with the plasma membrane. They are remarkably efficient so that very small doses cause paralysis of an affected person (Lalli et al. 2003; Turton et al. 2002). All characterized clostridial neurotoxins are synthesized as products of chromosomal, plasmid or prophage-borne bacterial genes. The nascent toxin may be cleaved into light (LC) and heavy (HC) chain moieties that remain attached by noncovalent interactions and a disulfide bond (Turton et al. 2002).

Strains of Clostridium botulinum produce seven serologically distinct toxins, BoNT/A, B, C, D, E, F, and G. An eighth toxin, BoNT/H has recently been identified (Barash & Arnon 2014) but its molecular properties have not yet been described. Human poisoning most commonly result from ingestion of toxin contaminated food. More rarely, it is due to wound infection or clostridial colonization of the gut of an infant whose own gut flora have not yet developed or of an older individual whose flora have been suppressed. While all seven characterized toxins can cleave human target proteins, three, BoNT/A, B, and E, are most commonly associated with human disease (Hatheway 1995; Sakaguchi 1982). BoNT/F is also able to cause human botulism.<p>Once ingested, the botulinum toxin must be taken up from the gut lumen into the circulation, a process mediated by four accessory proteins. These proteins form a complex that mediates transcytosis of the toxin molecule across the gut epithelium, allowing its entry into the circulation. The accessory proteins produced by different C. botulinum strains differ in their affinities for polarized epithelia of different species (e.g., human versus canine), and may thus be a key factor in human susceptibility to the toxins of strains A, B, and E and resistance to the others (Simpson 2004).<p>Clostridium tetani produces TeNT toxin. Human poisoning is the result of toxin secretion by bacteria growing in an infected wound and the toxin is released directly into the circulation.<p>Circulating clostridial toxins are taken up by neurons at neuromuscular junctions. They bind to specific gangliosides (BoNT/C, TeNT) or to both gangliosides and synaptic vesicle proteins (BoNT/A, B, D G) exposed on the neuronal plasma membrane during vesicle exocytosis (Montal 2010). All seven characterized forms of BoNT are thought to be taken up into synaptic vesicles as these re-form at the neuromuscular junction. These vesicles remain close to the site of uptake and are rapidly re-loaded with neurotransmitter and acidified (Sudhoff 2004). TeNT, in contrast, is taken up into clathrin coated vesicles that reach the neuron cell body by retrograde transport and then possibly other neurons before undergoing acidification. Vesicle acidification causes a conformational change in the toxin, allowing its HC part to function as a channel through which its LC part is extruded into the neuronal cytosol. The HC - LC disulfide bond is cleaved and the cytosolic LC functions as a zinc metalloprotease to cleave specific bonds in proteins on the cytosolic faces of synaptic vesicles and plasma membranes that normally mediate exocytosis (Lalli et al. 2003; Montal 2010). Source:Reactome.</div>

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Bibliography

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  1. Montal M.; ''Botulinum neurotoxin: a marvel of protein design.''; PubMed Europe PMC Scholia
  2. Dasgupta BR, Datta A.; ''Botulinum neurotoxin type B (strain 657): partial sequence and similarity with tetanus toxin.''; PubMed Europe PMC Scholia
  3. Giménez JA, DasGupta BR.; ''Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin.''; PubMed Europe PMC Scholia
  4. Foran P, Shone CC, Dolly JO.; ''Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments.''; PubMed Europe PMC Scholia
  5. Schiavo G, Santucci A, Dasgupta BR, Mehta PP, Jontes J, Benfenati F, Wilson MC, Montecucco C.; ''Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds.''; PubMed Europe PMC Scholia
  6. Binz T, Blasi J, Yamasaki S, Baumeister A, Link E, Südhof TC, Jahn R, Niemann H.; ''Proteolysis of SNAP-25 by types E and A botulinal neurotoxins.''; PubMed Europe PMC Scholia
  7. Dong M, Yeh F, Tepp WH, Dean C, Johnson EA, Janz R, Chapman ER.; ''SV2 is the protein receptor for botulinum neurotoxin A.''; PubMed Europe PMC Scholia
  8. Schiavo G, Benfenati F, Poulain B, Rossetto O, Polverino de Laureto P, DasGupta BR, Montecucco C.; ''Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin.''; PubMed Europe PMC Scholia
  9. Krieglstein K, Henschen A, Weller U, Habermann E.; ''Arrangement of disulfide bridges and positions of sulfhydryl groups in tetanus toxin.''; PubMed Europe PMC Scholia
  10. Rummel A, Häfner K, Mahrhold S, Darashchonak N, Holt M, Jahn R, Beermann S, Karnath T, Bigalke H, Binz T.; ''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.''; PubMed Europe PMC Scholia
  11. Hatheway CL.; ''Botulism: the present status of the disease.''; PubMed Europe PMC Scholia
  12. Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC.; ''Crystal structure of botulinum neurotoxin type A and implications for toxicity.''; PubMed Europe PMC Scholia
  13. Schiavo G, Rossetto O, Catsicas S, Polverino de Laureto P, DasGupta BR, Benfenati F, Montecucco C.; ''Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D, and E.''; PubMed Europe PMC Scholia
  14. Yamasaki S, Binz T, Hayashi T, Szabo E, Yamasaki N, Eklund M, Jahn R, Niemann H.; ''Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2.''; PubMed Europe PMC Scholia
  15. Montecucco C, Schiavo G.; ''Mechanism of action of tetanus and botulinum neurotoxins.''; PubMed Europe PMC Scholia
  16. Lalli G, Bohnert S, Deinhardt K, Verastegui C, Schiavo G.; ''The journey of tetanus and botulinum neurotoxins in neurons.''; PubMed Europe PMC Scholia
  17. Link E, Edelmann L, Chou JH, Binz T, Yamasaki S, Eisel U, Baumert M, Südhof TC, Niemann H, Jahn R.; ''Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis.''; PubMed Europe PMC Scholia
  18. Karalewitz AP, Fu Z, Baldwin MR, Kim JJ, Barbieri JT.; ''Botulinum neurotoxin serotype C associates with dual ganglioside receptors to facilitate cell entry.''; PubMed Europe PMC Scholia
  19. Simpson LL.; ''Identification of the major steps in botulinum toxin action.''; PubMed Europe PMC Scholia
  20. Sun S, Suresh S, Liu H, Tepp WH, Johnson EA, Edwardson JM, Chapman ER.; ''Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly.''; PubMed Europe PMC Scholia
  21. Barash JR, Arnon SS.; ''A novel strain of Clostridium botulinum that produces type B and type H botulinum toxins.''; PubMed Europe PMC Scholia
  22. Chen C, Fu Z, Kim JJ, Barbieri JT, Baldwin MR.; ''Gangliosides as high affinity receptors for tetanus neurotoxin.''; PubMed Europe PMC Scholia
  23. Kumaran D, Eswaramoorthy S, Furey W, Navaza J, Sax M, Swaminathan S.; ''Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation.''; PubMed Europe PMC Scholia
  24. Schiavo G, Poulain B, Rossetto O, Benfenati F, Tauc L, Montecucco C.; ''Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc.''; PubMed Europe PMC Scholia
  25. Peng L, Tepp WH, Johnson EA, Dong M.; ''Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors.''; PubMed Europe PMC Scholia
  26. Dong M, Richards DA, Goodnough MC, Tepp WH, Johnson EA, Chapman ER.; ''Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells.''; PubMed Europe PMC Scholia
  27. Sun S, Tepp WH, Johnson EA, Chapman ER.; ''Botulinum neurotoxins B and E translocate at different rates and exhibit divergent responses to GT1b and low pH.''; PubMed Europe PMC Scholia
  28. Kroken AR, Karalewitz AP, Fu Z, Kim JJ, Barbieri JT.; ''Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into neurons.''; PubMed Europe PMC Scholia
  29. Lee K, Gu S, Jin L, Le TT, Cheng LW, Strotmeier J, Kruel AM, Yao G, Perry K, Rummel A, Jin R.; ''Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity.''; PubMed Europe PMC Scholia
  30. Amatsu S, Sugawara Y, Matsumura T, Kitadokoro K, Fujinaga Y.; ''Crystal structure of Clostridium botulinum whole hemagglutinin reveals a huge triskelion-shaped molecular complex.''; PubMed Europe PMC Scholia
  31. Fu Z, Chen C, Barbieri JT, Kim JJ, Baldwin MR.; ''Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype F.''; PubMed Europe PMC Scholia
  32. Südhof TC, De Camilli P, Niemann H, Jahn R.; ''Membrane fusion machinery: insights from synaptic proteins.''; PubMed Europe PMC Scholia
  33. Mochida S, Poulain B, Weller U, Habermann E, Tauc L.; ''Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro-neuronal synapses, and its internalization is mediated by heavy chain.''; PubMed Europe PMC Scholia
  34. Sakaguchi G.; ''Clostridium botulinum toxins.''; PubMed Europe PMC Scholia
  35. Swaminathan S, Eswaramoorthy S.; ''Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.''; PubMed Europe PMC Scholia
  36. Arndt JW, Chai Q, Christian T, Stevens RC.; ''Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity.''; PubMed Europe PMC Scholia
  37. Willjes G, Mahrhold S, Strotmeier J, Eichner T, Rummel A, Binz T.; ''Botulinum neurotoxin G binds synaptotagmin-II in a mode similar to that of serotype B: tyrosine 1186 and lysine 1191 cause its lower affinity.''; PubMed Europe PMC Scholia
  38. Blasi J, Chapman ER, Yamasaki S, Binz T, Niemann H, Jahn R.; ''Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin.''; PubMed Europe PMC Scholia
  39. Kozaki S, Kamata Y, Watarai S, Nishiki T, Mochida S.; ''Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins.''; PubMed Europe PMC Scholia
  40. Peng L, Berntsson RP, Tepp WH, Pitkin RM, Johnson EA, Stenmark P, Dong M.; ''Botulinum neurotoxin D-C uses synaptotagmin I and II as receptors, and human synaptotagmin II is not an effective receptor for type B, D-C and G toxins.''; PubMed Europe PMC Scholia
  41. Deinhardt K, Berninghausen O, Willison HJ, Hopkins CR, Schiavo G.; ''Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1.''; PubMed Europe PMC Scholia
  42. Schiavo G, Malizio C, Trimble WS, Polverino de Laureto P, Milan G, Sugiyama H, Johnson EA, Montecucco C.; ''Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond.''; PubMed Europe PMC Scholia
  43. Dong M, Liu H, Tepp WH, Johnson EA, Janz R, Chapman ER.; ''Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons.''; PubMed Europe PMC Scholia
  44. Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S.; ''Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway.''; PubMed Europe PMC Scholia
  45. Schmidt JJ, Sathyamoorthy V, DasGupta BR.; ''Partial amino acid sequence of the heavy and light chains of botulinum neurotoxin type A.''; PubMed Europe PMC Scholia
  46. Turton K, Chaddock JA, Acharya KR.; ''Botulinum and tetanus neurotoxins: structure, function and therapeutic utility.''; PubMed Europe PMC Scholia
  47. Koriazova LK, Montal M.; ''Translocation of botulinum neurotoxin light chain protease through the heavy chain channel.''; PubMed Europe PMC Scholia
  48. Vaidyanathan VV, Yoshino K, Jahnz M, Dörries C, Bade S, Nauenburg S, Niemann H, Binz T.; ''Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage.''; PubMed Europe PMC Scholia
  49. Benefield DA, Dessain SK, Shine N, Ohi MD, Lacy DB.; ''Molecular assembly of botulinum neurotoxin progenitor complexes.''; PubMed Europe PMC Scholia
  50. Fujinaga Y, Sugawara Y, Matsumura T.; ''Uptake of botulinum neurotoxin in the intestine.''; PubMed Europe PMC Scholia
  51. Yamasaki S, Baumeister A, Binz T, Blasi J, Link E, Cornille F, Roques B, Fykse EM, Südhof TC, Jahn R.; ''Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin.''; PubMed Europe PMC Scholia
  52. Sathyamoorthy V, Dasgupta BR, Foley J, Niece RL.; ''Botulinum neurotoxin type A: cleavage of the heavy chain into two halves and their partial sequences.''; PubMed Europe PMC Scholia
  53. Henderson I, Whelan SM, Davis TO, Minton NP.; ''Genetic characterisation of the botulinum toxin complex of Clostridium botulinum strain NCTC 2916.''; PubMed Europe PMC Scholia
  54. Foran P, Lawrence GW, Shone CC, Foster KA, Dolly JO.; ''Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release.''; PubMed Europe PMC Scholia
  55. Sudhof TC.; ''The synaptic vesicle cycle.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
113137view11:20, 2 November 2020ReactomeTeamReactome version 74
112368view15:30, 9 October 2020ReactomeTeamReactome version 73
101270view11:16, 1 November 2018ReactomeTeamreactome version 66
100808view20:44, 31 October 2018ReactomeTeamreactome version 65
100349view19:21, 31 October 2018ReactomeTeamreactome version 64
99894view16:04, 31 October 2018ReactomeTeamreactome version 63
99451view14:38, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99115view12:40, 31 October 2018ReactomeTeamreactome version 62
93784view13:36, 16 August 2017ReactomeTeamreactome version 61
93317view11:20, 9 August 2017ReactomeTeamreactome version 61
87757view09:56, 25 July 2016RyanmillerOntology Term : 'disease pathway' added !
87755view09:56, 25 July 2016RyanmillerOntology Term : 'infectious disease pathway' added !
87752view09:53, 25 July 2016RyanmillerOntology Term : 'bacterial infectious disease' added !
86402view09:17, 11 July 2016ReactomeTeamreactome version 56
83321view10:46, 18 November 2015ReactomeTeamVersion54
81748view09:47, 26 August 2015ReactomeTeamVersion53
76848view08:07, 17 July 2014ReactomeTeamFixed remaining interactions
76552view11:53, 16 July 2014ReactomeTeamFixed remaining interactions
75885view09:54, 11 June 2014ReactomeTeamRe-fixing comment source
75585view10:42, 10 June 2014ReactomeTeamReactome 48 Update
74940view13:46, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74584view08:37, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
BoNT/A HC disulfide bonded ProteinP10845 (Uniprot-TrEMBL)
BoNT/A HC:LC dimerComplexR-CBO-5228590 (Reactome)
BoNT/A HCProteinP10845 (Uniprot-TrEMBL)
BoNT/A LC ProteinP10845 (Uniprot-TrEMBL)
BoNT/A LC disulfide bonded ProteinP10845 (Uniprot-TrEMBL)
BoNT/A LC:Zn2+ComplexR-CBO-190017 (Reactome)
BoNT/A:NTNHA:HAComplexR-CBO-5228604 (Reactome)
BoNT/A:SV2:GT1bComplexR-NUL-5244411 (Reactome)
BoNT/A:SV2:GT1bComplexR-NUL-5244507 (Reactome)
BoNT/B HC disulfide bonded ProteinP10844 (Uniprot-TrEMBL)
BoNT/B HC:LC dimerComplexR-CBO-5228599 (Reactome)
BoNT/B HCProteinP10844 (Uniprot-TrEMBL)
BoNT/B LC ProteinP10844 (Uniprot-TrEMBL)
BoNT/B LC disulfide bonded ProteinP10844 (Uniprot-TrEMBL)
BoNT/B LC:Zn2+ComplexR-CBO-190016 (Reactome)
BoNT/B:NTNHA:HAComplexR-CBO-5228681 (Reactome)
BoNT/B:SYT:GT1bComplexR-NUL-5244408 (Reactome)
BoNT/B:SYT:GT1bComplexR-NUL-5244502 (Reactome)
BoNT/C HC disulfide bonded ProteinP18640 (Uniprot-TrEMBL)
BoNT/C HC:LC dimerComplexR-CBO-5246516 (Reactome)
BoNT/C HCProteinP18640 (Uniprot-TrEMBL)
BoNT/C LC ProteinP18640 (Uniprot-TrEMBL)
BoNT/C LC disulfide bonded ProteinP18640 (Uniprot-TrEMBL)
BoNT/C LC:Zn2+ComplexR-CBO-190018 (Reactome)
BoNT/C:GT1bComplexR-CBO-5246508 (Reactome)
BoNT/C:GT1bComplexR-CBO-5246513 (Reactome)
BoNT/D HC disulfide bonded ProteinP19321 (Uniprot-TrEMBL)
BoNT/D HC:LC dimerComplexR-CBO-5250523 (Reactome)
BoNT/D HCProteinP19321 (Uniprot-TrEMBL)
BoNT/D LC ProteinP19321 (Uniprot-TrEMBL)
BoNT/D LC disulfide bonded ProteinP19321 (Uniprot-TrEMBL)
BoNT/D LC:Zn2+ComplexR-CBO-190038 (Reactome)
BoNT/D:SV2:GD2ComplexR-NUL-5250603 (Reactome)
BoNT/D:SV2:GD2ComplexR-NUL-5250612 (Reactome)
BoNT/E HC disulfide bonded ProteinQ00496 (Uniprot-TrEMBL)
BoNT/E HC:LC dimerComplexR-CBO-5228686 (Reactome)
BoNT/E HCProteinQ00496 (Uniprot-TrEMBL)
BoNT/E LC ProteinQ00496 (Uniprot-TrEMBL)
BoNT/E LC disulfide bonded ProteinQ00496 (Uniprot-TrEMBL)
BoNT/E LC:Zn2+ComplexR-CBO-190047 (Reactome)
BoNT/E:NTNHAComplexR-CBO-5228688 (Reactome)
BoNT/E:SV2:GT1bComplexR-NUL-5244509 (Reactome)
BoNT/E:SV2:GT1bComplexR-NUL-5244512 (Reactome)
BoNT/F HC disulfide bonded ProteinP30996 (Uniprot-TrEMBL)
BoNT/F HC:LC dimerComplexR-CBO-5250693 (Reactome)
BoNT/F HCProteinP30996 (Uniprot-TrEMBL)
BoNT/F LC ProteinP30996 (Uniprot-TrEMBL)
BoNT/F LC disulfide bonded ProteinP30996 (Uniprot-TrEMBL)
BoNT/F LC:Zn2+ComplexR-CBO-190042 (Reactome)
BoNT/F:SV2:GT1bComplexR-NUL-5250879 (Reactome)
BoNT/F:SV2:GT1bComplexR-NUL-5250883 (Reactome)
BoNT/G HC disulfide bonded ProteinQ60393 (Uniprot-TrEMBL)
BoNT/G HC:LC dimerComplexR-CBO-5250691 (Reactome)
BoNT/G HCProteinQ60393 (Uniprot-TrEMBL)
BoNT/G LC ProteinQ60393 (Uniprot-TrEMBL)
BoNT/G LC disulfide bonded ProteinQ60393 (Uniprot-TrEMBL)
BoNT/G LC:Zn2+ComplexR-CBO-190032 (Reactome)
BoNT/G:SYT1:GT1bComplexR-NUL-5250975 (Reactome)
BoNT/G:SYT1:GT1bComplexR-NUL-5250976 (Reactome)
GD2 MetaboliteCHEBI:28648 (ChEBI)
GD2MetaboliteCHEBI:28648 (ChEBI)
GD3 MetaboliteCHEBI:28424 (ChEBI)
GD3MetaboliteCHEBI:28424 (ChEBI)
GM1a MetaboliteCHEBI:18216 (ChEBI)
GM1aMetaboliteCHEBI:18216 (ChEBI)
GT1b MetaboliteCHEBI:60913 (ChEBI)
GT1bMetaboliteCHEBI:60913 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
NTNHA ProteinQ9LBS8 (Uniprot-TrEMBL)
NTNHAProteinQ9LBS8 (Uniprot-TrEMBL)
SNAP25(1-197)ProteinP60880 (Uniprot-TrEMBL)
SNAP25(1-198)ProteinP60880 (Uniprot-TrEMBL)
SNAP25(198-206)ProteinP60880 (Uniprot-TrEMBL)
SNAP25(199-206)ProteinP60880 (Uniprot-TrEMBL)
SNAP25ProteinP60880 (Uniprot-TrEMBL)
STX1(1-?)R-HSA-5250515 (Reactome)
STX1(?-288)R-HSA-5250513 (Reactome)
STX1R-HSA-5250514 (Reactome)
SV2A ProteinQ7L0J3 (Uniprot-TrEMBL)
SV2A,B,CR-HSA-5324682 (Reactome)
SV2A,B,CR-HSA-5324684 (Reactome)
SV2A,BR-HSA-5324689 (Reactome)
SV2A,BR-HSA-5324690 (Reactome)
SV2B ProteinQ7L1I2 (Uniprot-TrEMBL)
SV2C ProteinQ496J9 (Uniprot-TrEMBL)
SYT1 ProteinP21579 (Uniprot-TrEMBL)
SYT1,2R-HSA-5324683 (Reactome)
SYT1,2R-HSA-5324686 (Reactome)
SYT1ProteinP21579 (Uniprot-TrEMBL)
SYT2 ProteinQ8N9I0 (Uniprot-TrEMBL)
TeNT HC disulfide bonded ProteinP04958 (Uniprot-TrEMBL)
TeNT HC:LC dimerComplexR-CTE-5228372 (Reactome)
TeNT HCProteinP04958 (Uniprot-TrEMBL)
TeNT LC ProteinP04958 (Uniprot-TrEMBL)
TeNT LC disulfide bonded ProteinP04958 (Uniprot-TrEMBL)
TeNT LC:Zn2+ComplexR-CTE-5228371 (Reactome)
TeNT:gangliosidesComplexR-CTE-5228368 (Reactome)
TeNT:gangliosidesComplexR-CTE-5228374 (Reactome)
TeNT:gangliosidesComplexR-CTE-5228403 (Reactome)
VAMP1(1-60)ProteinP23763 (Uniprot-TrEMBL)
VAMP1(1-61)ProteinP23763 (Uniprot-TrEMBL)
VAMP1(1-83)ProteinP23763 (Uniprot-TrEMBL)
VAMP1(61-118)ProteinP23763 (Uniprot-TrEMBL)
VAMP1(62-118)ProteinP23763 (Uniprot-TrEMBL)
VAMP1(84-118)ProteinP23763 (Uniprot-TrEMBL)
VAMP1ProteinP23763 (Uniprot-TrEMBL)
VAMP2(2-58)ProteinP63027 (Uniprot-TrEMBL)
VAMP2(2-59)ProteinP63027 (Uniprot-TrEMBL)
VAMP2(2-76)ProteinP63027 (Uniprot-TrEMBL)