New Insight into Ricin Toxicity

Dear Colleague,

Ricin, one of the most potent protein-based toxins in nature, belongs to the Type II group of ribosome-inactivating proteins (RIPs). Ricin is composed of two subunits: RTA and RTB. The binding subunit RTB is a galactose-specific lectin which promotes toxin attachment to the cell and retrograde trafficking from the plasma membrane to the trans-Golgi network. The enzymatic subunit RTA, an RNA N-glycosidase, mediates the depurination of a single adenine residue within the sarcin–ricin loop of eukaryotic ribosomal RNA and activates multiple stress-activated protein kinase networks and programmed cell death pathways. Although it is well documented that the ribosome represents the primary target for ricin, the underlying molecular basis of cytotoxicity and cellular malfunctions that lead to clinical symptoms remain poorly understood. The cytotoxicity of ricin is clearly related to a combination of effects, including ribotoxic stress, intracellular trafficking, ROS production, ER stress, JNK- and p38-dependent cascades, and activation of apoptosis, but their interdependence and relationship with depurination and translation inhibition has yet to be elucidated. The scope of this Special Issue will be centered on broad aspects of ricin toxicity and other RIP proteins, including the biology of ricin/RIPs, molecular action of the toxins, cell signaling in connection to toxicokinetics, pathophysiology, medical treatment, and all consequences of ricin/RIPs intoxication.

Prof. Dr. Marek Tchórzewski
Prof. Dr. Nicholas Mantis
Guest Editors

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• ribosome-inactivating protein
• RIP
• ricin
• sarcin–ricin loop