Ribosome-inactivating proteins with an emphasis on bacterial RIPs and their potential medical applications.
Ribosome-inactivating proteins (RIPs) are toxic due to their N-glycosidase activity catalyzing depurination at the universally conserved α-sarcin loop of the 60S ribosomal subunit. In addition, RIPs have been shown to also have other enzymatic activities, including polynucleotide:adenosine glycosidase activity. RIPs are mainly produced by different plant species, but are additionally found in a number of bacteria, fungi, algae and some mammalian tissues. This review describes the occurrence of RIPs, with special emphasis on bacterial RIPs, including the Shiga toxin and RIP in Streptomyces coelicolor recently identified in S. coelicolor. The properties of RIPs, such as enzymatic activity and targeting specificity, and how their unique biological activity could be potentially turned into medical or agricultural tools to combat tumors, viruses and fungi, are highlighted.
Departamento de Biotecnología, División de Ciencias Biológicas & de la Salud, Universidad Autónoma Metropolitana, Mexico City, Mexico.
Ana G
AG
Reyes
Jozef
J
Anné
Armando
A
Mejía
D020418:Algal Proteins / Q000633:toxicity; D001426:Bacterial Proteins / Q000627:therapeutic use* / Q000633:toxicity*; D005656:Fungal Proteins / Q000633:toxicity; D006801:Humans; D010940:Plant Proteins / Q000633:toxicity; D054788:Ribosome Inactivating Proteins / Q000627:therapeutic use* / Q000633:toxicity*; D012760:Shigella / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000378:metabolism
D020418:Algal Proteins; D001426:Bacterial Proteins; D005656:Fungal Proteins; D010940:Plant Proteins; D054788:Ribosome Inactivating Proteins