| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Laboratory of Phytopathology and Plant Protection, Katholieke Universiteit Leuven, 3001 Leuven, Belgium
1Correspondence: Laboratory of Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium. E-mail: Els.VanDamme{at}agr.kuleuven.ac.be
Many plants contain proteins that are capable of inactivating ribosomes and accordingly are called ribosome-inactivating proteins or RIPs. These typical plant proteins receive a lot of attention in biological and biomedical research because of their unique biological activities toward animal and human cells. In addition, evidence is accumulating that some RIPs play a role in plant defense and hence can be exploited in plant protection. To understand the mode of action of RIPs and to optimize their medical and therapeutical applications and their use as antiviral compounds in plant protection, intensive efforts have been made to unravel the enzymatic activities of RIPs and provide a structural basis for these activities. Though marked progress has been made during the last decade, the enzymatic activity of RIPs has become a controversial issue because of the concept that RIPs possess, in addition to their classical RNA N-glycosidase and polynucleotide:adenosine glycosidase activity, other unrelated enzymatic activities. Moreover, the presumed novel enzymatic activities, especially those related to diverse nuclease activities, are believed to play an important role in various biological activities of RIPs. However, both the novel enzymatic activities and their presumed involvement in the biological activities of RIPs have been questioned because there is evidence that the activities observed are due to contaminating enzymes. We offer a critical review of the pros and cons of the putative novel enzymatic activities of RIPs. Based on the available data, it is suggested that there is little conclusive evidence in support of the presumed activities and that in the past too little attention has been given to the purity of the RIP preparation. The antiviral activity and mode of action of RIPs in plants are discussed in view of their classical and presumed novel enzymatic activities.—Peumans, W. J., Hao, Q., Van Damme, E. J. M. Ribosome-inactivating proteins from plants: more than RNA N-glycosidases?
Key Words: antiviral activity • DNA glycosylase/AP lyase • polynucleotide:adenosine glycosidase
This article has been cited by other articles:
|
|
 |
|
  H. Kaku, H. Kaneko, N. Minamihara, K. Iwata, E. T. Jordan, M. A. Rojo, N. Minami-Ishii, E. Minami, S. Hisajima, and N. Shibuya Elderberry Bark Lectins Evolved to Recognize Neu5Ac{alpha}2,6Gal/GalNAc Sequence from a Gal/GalNAc Binding Lectin Through the Substitution of Amino-Acid Residues Critical for the Binding to Sialic Acid J. Biochem., September 1, 2007; 142(3): 393 - 401. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Sato, S. Okuyama, and K. Hori Primary Structure and Carbohydrate Binding Specificity of a Potent Anti-HIV Lectin Isolated from the Filamentous Cyanobacterium Oscillatoria agardhii J. Biol. Chem., April 13, 2007; 282(15): 11021 - 11029. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Mishra, S. Bilgrami, R. S. Sharma, P. Kaur, S. Yadav, R. Krauspenhaar, C. Betzel, W. Voelter, C. R. Babu, and T. P. Singh Crystal Structure of Himalayan Mistletoe Ribosome-inactivating Protein Reveals the Presence of a Natural Inhibitor and a New Functionally Active Sugar-binding Site J. Biol. Chem., May 27, 2005; 280(21): 20712 - 20721. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S.-W. Park, R. Vepachedu, R. A. Owens, and J. M. Vivanco The N-Glycosidase Activity of the Ribosome-inactivating Protein ME1 Targets Single-stranded Regions of Nucleic Acids Independent of Sequence or Structural Motifs J. Biol. Chem., August 13, 2004; 279(33): 34165 - 34174. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. A. Rojo, H. Kaku, N. Ishii-Minami, E. Minami, M. Yato, S. Hisajima, T. Yamaguchi, and N. Shibuya Characterization and cDNA Cloning of Monomeric Lectins That Correspond to the B-Chain of a Type 2 Ribosome-Inactivating Protein from the Bark of Japanese Elderberry (Sambucus sieboldiana) J. Biochem., April 1, 2004; 135(4): 509 - 516. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Veronese, M. T. Ruiz, M. A. Coca, A. Hernandez-Lopez, H. Lee, J. I. Ibeas, B. Damsz, J. M. Pardo, P. M. Hasegawa, R. A. Bressan, et al. In Defense against Pathogens. Both Plant Sentinels and Foot Soldiers Need to Know the Enemy Plant Physiology, April 1, 2003; 131(4): 1580 - 1590. [Full Text] [PDF]
|
|
|
|
|
|
S. Bagga, D. Seth, and J. K. Batra The Cytotoxic Activity of Ribosome-inactivating Protein Saporin-6 Is Attributed to Its rRNA N-Glycosidase and Internucleosomal DNA Fragmentation Activities J. Biol. Chem., February 7, 2003; 278(7): 4813 - 4820. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. P. Pistillo, P. L. Tazzari, G. L. Palmisano, I. Pierri, A. Bolognesi, F. Ferlito, P. Capanni, L. Polito, M. Ratta, S. Pileri, et al. CTLA-4 is not restricted to the lymphoid cell lineage and can function as a target molecule for apoptosis induction of leukemic cells Blood, January 1, 2003; 101(1): 202 - 209. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Bolognesi, L. Polito, C. Lubelli, L. Barbieri, A. Parente, and F. Stirpe Ribosome-inactivating and Adenine Polynucleotide Glycosylase Activities in Mirabilis jalapa L. Tissues J. Biol. Chem., April 12, 2002; 277(16): 13709 - 13716. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. BRIGOTTI, R. ALFIERI, P. SESTILI, M. BONELLI, P. G. PETRONINI, A. GUIDARELLI, L. BARBIERI, F. STIRPE, and S. SPERTI Damage to nuclear DNA induced by Shiga toxin 1 and ricin in human endothelial cells FASEB J, March 1, 2002; 16(3): 365 - 372. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
