Anti-Clostridium botulinum Toxin A Antibody

[Botulinum neurotoxin A light chain]: Secreted, Host cytoplasm, host cytosol, Host cell junction, host synapse, host presynaptic cell membrane, Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane, Multi-pass membrane protein

Synthetic peptide corresponding to aa 1280-1292 (Cys-Ser-Trp-Glu-Phe-Ile-Pro-Val- Asp-Asp-Gly-Trp-Gly-COOH) at the C-terminus of Clostridium botulinum Toxin A.

[Botulinum neurotoxin type A]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:8103915). Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles (By similarity). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:19476346). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway (By similarity). When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol (By similarity). Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). {UniProtKB:P0DPI0, PubMed:19476346, PubMed:8103915}.; [Botulinum neurotoxin A light chain]: Has proteolytic activity (PubMed:8103915, PubMed:8294407). In vitro the whole toxin is reduced to release LC (PubMed:8103915, PubMed:8294407). After translocation into the eukaryotic host cytosol, LC hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP25, blocking neurotransmitter release (PubMed:8103915, PubMed:8294407). {PubMed:8103915, PubMed:8294407, PubMed:19476346}.; [Botulinum neurotoxin A heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD) (PubMed:9783750, PubMed:17173035). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously rUniProtKB:P0DPI0, PubMed:17173035, PubMed:19476346, PubMed:21849494, PubMed:9783750}.

Clostridium botulinum, an anaerobic, gram-positive, spore-forming rod commonly found on plants, in soil, water, and the intestinal tracts of animals, produces eight antigenically distinguishable exotoxins (A, B, C1, C2, D, E, F and G). Type A is the most potent toxin, followed by types B and F. All botulinum neurotoxins are produced as single polypeptide chains of ~150 kDa comprised of a heavy (H) chain and a light (L) chain of roughly 100 and 50 kDa, respectively, linked by a disulfide bond. The heavy (H) chain of the toxin binds selectively and irreversibly to high affinity receptors at the presynaptic surface of cholinergic neurones, and the toxin-receptor complex is taken up into the cell by endocytosis where the disulfide bond between the two chains is cleaved. The light (L) chain interacts with different proteins in the nerve terminals to prevent fusion of acetylcholine vesicles with the cell membrane.