Plant ribosome-inactivating proteins (RIPs) are N-glycosidases which cleave the N-glycosidic bond of adenine in a specific ribosomal RNA sequence. Most commonly RIPs are single-chain proteins (type 1 RIPs), but some (type 2 RIPs) possess a galactose-specific lectin domain that binds to cell surfaces. The latter RIPs are potent toxins, the best known of which is ricin. RIPs have antiviral and abortifacient activities, and, in a widespread application, can also be linked to antibodies or ligands to form immunotoxins or conjugates specifically toxic to a given type of cell.