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Function
Clostridium botulinum is a rod-shaped, spore-forming bacteria that is highly pathogenic. These bacteria are prevalent in soils, sediments, and aquatic environments. The botulinum toxins decrease or prevent nerve function which leads to respiratory and muscular paralysis.
The spores within the C. botulinum grow an abundance of active bacteria and transform into neurotoxins to produce Botulinum Neurotoxin or Botulinum Toxin- one of the most toxic proteins known to exist.
There are four types of botulism that are associated with the bacteria, Clostridium botulinum.
These include food, wound, infant botulism, and inhalation botulism.
Disease
Relevance
Structural highlights
Consists of a heavy chain (100 kDa) and light chain (50 kDa) which are linked together by a single disulfide bond. It is a 150- kDa molecular weight protein that inhibits the release of acetylcholine by blocking the neuromuscular communications and transmissions on motor and sympathetic nerve terminals. The heavy chain binds at the pre-synaptic surface of cholinergic neurons. They bind one way and are irreversible. Endocytosis allows for the toxin receptor- complex to be sent into the cell after binding. The botulism toxin enters the cytoplasm after the disulfide bond between the two chains is broken. The light chain interacts with SNAP-25 (needed for binding/ attachment and release of ACH from vesicles) specifically at the nerve terminal to prevent binding of acetylcholine vesicles with the cell membrane.
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