Pathophysiology: Scorpions use their pincers to grasp their prey; then, they arch their tail over their body to drive their stinger into the prey to inject their venom, sometimes more than once. The scorpion can voluntarily regulate how much venom to inject with each sting. The striated muscles in the stinger allow regulation of the amount of venom ejected, which is usually 0.1-0.6 mg. If the entire supply of venom is used, several days must elapse before the supply is replenished. Furthermore, scorpions with large venom sacs, such as the Parabuthus species, can even squirt their venom.
The venom glands are located on the tail lateral to the tip of the stinger and are composed of 2 types of tall columnar cells. One type produces the toxins, while the other produces mucus. The potency of the venom varies with the species, with some producing only a mild flu and others producing death within an hour. Generally, the venom is distributed rapidly into the tissue if it is deposited into a venous structure. Venom deposited via the intravenous route can cause symptoms only 4-7 minutes after the injection, with a peak tissue concentration in 30 minutes and an overall toxin elimination half-life of 4.2-13.4 hours through the urine. The more rapidly the venom enters the bloodstream, the higher the venom concentration in the blood and the more rapid the onset of systemic symptoms.
Scorpion venom is a water-soluble, antigenic, heterogenous mixture, as demonstrated on electrophoresis studies. This heterogeneity accounts for the variable patient reactions to the scorpion sting. However, the closer the phylogenetic relationship between the scorpions, the more similar the immunological properties. Furthermore, the various constituents of the venom may act directly or indirectly and individually or synergistically to manifest their effects. In addition, differences in the amino acid sequence of each toxin account for their differences in the function and immunology. Thus, any modifications of the amino acid sequence result in modification of the function and immunology of the toxin.
The venom is composed of varying concentrations of neurotoxin, cardiotoxin, nephrotoxin, hemolytic toxin, phosphodiesterases, phospholipases, hyaluronidases, glycosaminoglycans, histamine, serotonin, tryptophan, and cytokine releasers.*
The most potent toxin is the neurotoxin, of which 2 classes exist. Both of these classes are heat-stable, have low molecular weight, and are responsible for causing cell impairment in nerves, muscles, and the heart by altering ion channel permeability.
The long-chain polypeptide neurotoxin causes stabilization of voltage-dependent sodium channels in the open position, leading to continuous, prolonged, repetitive firing of the somatic, sympathetic, and parasympathetic neurons. This repetitive firing results in autonomic and neuromuscular overexcitation symptoms, and it prevents normal nerve impulse transmissions. Furthermore, it results in release of excessive neurotransmitters such as epinephrine, norepinephrine, acetylcholine, glutamate, and aspartate.*
Meanwhile, the short polypeptide neurotoxin blocks the potassium channels.
The binding of these neurotoxins to the host is reversible, but different neurotoxins have different affinities. The stability of the neurotoxin is due to the 4 disulfide bridges that fold the neurotoxin into a very compact 3-dimensional structure, thus making it resistant to pH and temperature changes. However, reagents that can break the disulfide bridges can inactivate this toxin by causing it to unfold. Also, the antigenicity of this toxin is dependent on the length and number of exposed regions that are sticking out of the 3-dimensional structure.