Ricin is a plant derived biological toxin produced by the castor bean plant, Ricinus communis L., often referred to as the castor oil plant. The plant itself and the toxin extracted from it are well-known for its toxicity. The plant is widely distributed throughout the world and is native to the Mediterranean, northeast Africa and the Middle East (plant hardiness zones 6-9), growing up to 40ft (12 m) tall in the wild. Global cultivation of the plant, the ease of toxin extraction from castor beans and isolation of the toxin itself, make ricin a very appealing agent, with a strong potential to be employed as a biological weapon [1,2]. The Ricin Toxin (RT) has been known and used as a homicidal poison since antiquity [3]. To date, over seven hundred human intoxications have been reported, dating as far back as the late 1800s [4,5].Ricin belongs to a family of phytotoxins known as Ribosome Inactivating Proteins (RIPs), specifically type 2 RIPs. RIPs are RNA N-glycosidases that target and deactivate ribosomes required for protein synthesis [6,7]. The holotoxin is comprised of two separate and distinct polypeptide chains, connected by a disulfide bond [8]. The Ricin A chain (RTA) bears the catalytic properties, selectively recognizing and cleaving a distinct adenine from large ribosomal 28s RNA (A4324 for the rat liver ribosome) [9]. This specific purine base is located inside a universally conserved Sarcin/Ricin Loop (SRL) within the large rRNA [10], depurination of which leads to the inhibition of protein synthesis and cellular death. The Ricin B chain (RTB) is divergent and structurally distinct from RTA, with lectin properties (carbohydrate binding domain) [11][12][13]. The lectin chain is able to bind galactosyl moieties of glycoproteins and/or glycolipids, located on the exterior of eukaryotic cells and promote reverse transport of the RTA to the cytosol [14][15][16]. The RT accesses translational machinery and depurinates ribosomes after it enters the cytosol. Ricin and other type 2 RIPs owe their toxicity and cytotoxicity to the binding affinity of the B chain to sugar-containing receptors on the cell surfaces. Ricin is an acutely toxic protein, known to induce 50% apoptosis in cells at concentrations below 1 ng/mL. Recent reviews provide excellent summaries of ricin trafficking, host cell signal transduction, ribosomal binding and induction of apoptosis [17][18][19][20][21].