Toxic Plant Proteins

1. Front Matter

   Pages i-x

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2. Evolution of Plant Ribosome-Inactivating Proteins

   • Willy J. Peumans, Els J. M. Van Damme

   Pages 1-26

3. RNA N-Glycosidase Activity of Ribosome-Inactivating Proteins

   • Kazuyuki Takai, Tatsuya Sawasaki, Yaeta Endo

   Pages 27-39

4. Enzymatic Activities of Ribosome-Inactivating Proteins

   • Martin R. Hartley

   Pages 41-54

5. Type I Ribosome-Inactivating Proteins from Saponaria officinalis

   • Alessio Lombardi, Richard S. Marshall, Carmelinda Savino, Maria Serena Fabbrini, Aldo Ceriotti

   Pages 55-78

6. Type 1 Ribosome-Inactivating Proteins from the Ombú Tree (Phytolacca dioica L.)

   • Augusto Parente, Rita Berisio, Angela Chambery, Antimo Di Maro

   Pages 79-106

7. Sambucus Ribosome-Inactivating Proteins and Lectins

   • José Miguel Ferreras, Lucía Citores, Rosario Iglesias, Pilar Jiménez, Tomás Girbés

   Pages 107-131

8. Ribosome-Inactivating Proteins from Abrus pulchellus

   • Ana Paula Ulian Araújo, Priscila Vasques Castilho, Leandro Seiji Goto

   Pages 133-147

9. Ribosome-Inactivating Proteins in Cereals

   • Carlotta Balconi, Chiara Lanzanova, Mario Motto

   Pages 149-166

10. Ribosome Inactivating Proteins and Apoptosis

    • Deepa Sikriwal, Janendra K. Batra

    Pages 167-189

11. The Synthesis of Ricinus communis Lectins

    • Lorenzo Frigerio, Lynne M. Roberts

    Pages 191-205

12. How Ricin Reaches its Target in the Cytosol of Mammalian Cells

    • Robert A. Spooner, Jonathan P. Cook, Shuyu Li, Paula Pietroni, J. Michael Lord

    Pages 207-224

13. Ribosome-Inactivating Protein-Containing Conjugates for Therapeutic Use

    • Giulio Fracasso, Fiorenzo Stirpe, Marco Colombatti

    Pages 225-263

14. Back Matter

    Pages 265-270

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Many plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.

• Cytosol
• Polypeptide
• Protein
• RNA
• Ribosome-inactivating proteins
• Tree
• enzymes
• plant lectins
• proteins
• ricinus communis

• Dept. Biological Sciences, University of Warwick, Coventry, United Kingdom

  J. Michael Lord, Martin R. Hartley

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