Snake venom

Snake Venoms – How Evolved Snake Do They Really Work?

Snake venom is a specialized saliva containing anti-venom that helps the quick immobilization and digestive processes of prey, as well as an effective defense against potential threats. Normally, it is injected directly into the vivarium through a strike from a preying snake, although some species can also spit venom at the target. The saliva is extremely potent, which makes it important to use an anti-venom gel when handling snakes.

There are two basic types of snake venom: hemotoxic and toxic. Hemotoxic venom has a greater composition of protein and amino acids, while the toxic composition contains various chemical constituents. Generally, the amount of protein and amino acid varies between species. The most common protein composition is identified as canine albuminoid protein, which is found in all known species, but is not present in all snakes. However, there are still some undiscovered species (such as the black rat snake) that have a protein composition that is significantly higher than canine albuminoid protein.

One of the major functions of venom-induced toxins is to provide the body with a compensatory mechanism, enabling it to remove foreign particles that are detrimental to organisms. This is usually done by disrupting the functions of the enzymes involved in the proteolytic cycle of the cells. Some snake venoms are capable of generating enzymes within the cell that interfere with the synthesis of neurotransmitters such as acetylcholine. Other toxins can affect specific cell functions by damaging ribosomes. In either case, the disrupted functioning of the cell leads to malfunctioning or death.

The major toxin components are usually peptides, which are manufactured to create a molecular structure that is dissolvable in water. Commonly, these toxins consist of a chain of amino acids linked together through various Gly residues. Some of the known Snake Vomiting peptides are mentioned below:

Peptide I: This peptide triggers an immunological response and releases gamma-interferon, interleukin-6, and interleukin-3. These proteins destroy the membranes of the lower intestine and promote inflammation in the digestive tract. It further causes damage to other cells in the digestive tract, resulting in diarrhea, vomiting, or even necrosis of tissue. The pancreatic islet cells of the pancreas are sometimes affected, which can cause pancreatic cancer. A rare neglected tropical disease, leptospirosis, can result from this toxin.

Peptide II: It is responsible for producing the neurotoxic amino acid voripranin. In fact, this is the most studied and potent snake bite toxin. Its symptoms include muscle weakness, paralysis, convulsions, respiratory failure, and extreme pain. The injected voripranin breaks down nerves, prevents cell regeneration, paralyzes muscles and leads to death. A relatively new toxic compound, it was only discovered in the 1970s and has been responsible for a very few snakebites. However, this protein is highly toxic to humans.

Snake venom proteomes are also found in other reptiles such as iguanas and frogs. While it is hard to say if these toxins have any evolutionary advantage over the prey’s genes, studies on non-venomous snakes may shed some light on this. For instance, the egg-laying glands of certain iguanas appear to have evolved independently from venom glands. If this is true, it supports the theory of gene transcription, whereby pre-existing genetic structures act as templates for new ones.

Gene transcription in the case of toxins may serve to provide an extra route of protection for the weaker venomous species. Alternatively, these evolved peptides act to disrupt prey by disrupting the prey’s nervous system or possibly the brain. These disruptions may allow them to escape from the scene of the crime or at least slow down the effects of death. Further research is needed to support whether these toxins have any real benefits or if they are all just noise inside the animal’s body.

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