Reprint
Ribosome Inactivating Toxins
Edited by
January 2019
329 pages
- ISBN978-3-03897-248-8 (Paperback)
- ISBN978-3-03897-249-5 (PDF)
This book is a reprint of the Special Issue Ribosome Inactivating Toxins that was published in
Biology & Life Sciences
Medicine & Pharmacology
Public Health & Healthcare
Summary
Ribosome inactivating proteins (RIPs) form a vast family of hundreds of toxins from plants, fungi, algae and bacteria. RIP activities have also been detected in animal tissues. They target a single adenine of a ribosomal RNA, thereby blocking protein synthesis and leading intoxicated cells to apoptosis. The role of plant RIPs may be related to plant defense against predators and viruses, plant senescence or bacterial pathogenesis. Most RIPs are no threat to human or animal health. However, several bacterial RIPs are major virulence factors involved in severe epidemic diseases such as dysentery or the hemolytic uremic syndrome that may occur in patients suffering from Shiga toxin-producing entero-hemorrhagic Escherichia coli infection. Several plant RIPs such as ricin toxin, abrin or sarcin have been, or may be involved in accidental or criminal poisonings, political intimidation or bio-suicides. Health crisis, biosafety and biosecurity issues became a major concern and many efforts are made to develop treatments. Finally, RIPs can be engineered into immunotoxins to destroy cancer cells or cells chronically infected by viruses.This book presents the most recent data on all aspects of RIPs including function, diversity and evolution, mechanism, pathophysiology, medical countermeasures and engineering into anticancer drugs.
Format
- Paperback
License
© 2019 by the authors; CC BY-NC-ND license
Keywords
Ricin; ribosome-inactivating protein; ribosomal P stalk protein; ribosome; MOD; PEGylation; antigenicity; pharmacokinetics study; circulation half-life; antibody induction; S. cerevisiae; ricin toxin A chain (RTA); ribosome inactivating protein (RIP); retrograde protein transport; trans-Golgi network (TGN); endoplasmic reticulum (ER); b-32; cereals; JIP60; Ribosome-inactivating proteins; RIP; Shiga toxin 1; Shiga toxin 2; Stx1; Stx2; ricin; ribosome binding; depurination activity; B-lymphoma; CD20; CD22; immunotherapy; immunotoxin; ribosome-inactivating proteins; saporin-S6; ricin; total body irradiation; leukopenia; neutropenia; inflammation; Shiga toxin; Shiga-like toxins; STX1; STX2; Shiga toxin-producing E. coli; STEC; hemolytic uremic syndrome; unfolded protein response; ribotoxic stress response; ribotoxin; ricin; pulmonary intoxication; countermeasures; antitoxins; disease-modifying agents; anti-ricin small molecules; plant ribosome inactivating proteins; ER-stress; saporin; targeted drug delivery; nanovectors; Shiga toxins; Shiga toxin type 1 and 2; Shiga toxin-producing Escherichia coli; hemolytic uremic syndrome; signaling pathways; apoptosis; retinal pigment epithelial cells; abrin; Abrus precatorius; mouse bioassay; food safety; temperature stability; pH stability; ricin; antibody; antitoxin; efficacy; intracellular trafficking; abrin; abrus precatorius; ELISA; monoclonal antibodies; ribosome-inactivating protein; glycosphingolipid; globotriaosylceramide; Gb3; raft; galectin; integrin; CD44; cholera toxin; thermal Casimir-like force; spontaneous curvature; ribosome inactivating proteins; immunotoxins; therapeutic applications; Shiga toxin; hemolytic uremic syndrome; enterohemorrhagic Escherichia coli; microvesicles; kidney; ricin; antibody; neutralizing; epitope; n/a; n/a