Phallolysin

Due to this, the death cap mushroom has gained the nickname the ‘killer of kings.’ The beginning of this research into the hemolytic properties of the Amanita phalloides, or the Death Cap Mushroom, began with Eduard Rudolf Kobert in 1891, who originally denoted it ‘phallin,’ and was continued by John Jacob Abel and William Webber Ford in 1908.

However, in addition to the non-specificity of the toxin, these trials resulted in the development of an increased potassium concentration in the bloodstream due to the extreme intravascular hemolysis and cytolysis of multiple cell types.

Two of the three proteins have been found to be composed of amino acids with high solubility in water, and each containing one tryptophan residue.

Although they are inactivated by temperatures above 65 °C and acidic environments, they are able to remain stable when coming in contact with proteases or glycosidic enzymes.

Such proteases range from pepsin, trypsin, alpha-chymotrypsin, subtilisin, pronase E, bromelin, proteinase K, alpha-amylase, and pancreatin.[9],.

[1],[9] These properties are believed to be instigated by ion permeable membrane channels that form as a result of the hemolytic capabilities of phallolysin.

In addition to hemolysis, phallolysin in high concentrations are also thought to cause damage to bovine phospholipids with a negative net charge, phosphatidylcholine, and sphingomyelin containing liposomes.

This interaction further backs up the claim in which phallolysin does not target the cell's plasma membrane, but rather the glycoprotein receptors.

This has been discovered in the specific cellular phospholipase A2 in 3T3 Swiss mouse fibroblasts, which are key components in the structural formation of connective tissues.

[17],[13] Phallolysin has additionally been discovered to interact mostly with D-galactose and the 𝛽-derivatives, with no glycosylation preferences between O-glycosylation and N-glycosylation.