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1. Abstracts of presentations on plant protection issues at the xth international congress of virology: August 11-16, 1996 Binyanei haOoma, Jerusalem Iarael part 3(final part)

Author

O. Faktor, G. P. Lomonossoff, S. Souche, B. Levine, C. Ford, D. Schumann, Sh. Abo-El-Saad, Fuh-Jyh Jan, F. Revere, J. Zalewski, M. Ravelonandro, M. Zaitlin, K. Lento, V. Hardi, V. Gaba, A. Romero, M. A. El-Saied, Michael J. Adams, O. N. Denisenko, M. Pilowsky, B. Böddi, W. Zagórski, M. Kikkert, J. Nahring, J. Peterka, U. Oertel, S. Seal, Kristin D. Kasschau, Susan Phillips, David C. Baulcombe, Michael G. K. Jones, S. A. MacFarlane, David M. Tricoli, Phil Larkin, M. A. Mayo, Maja Ravnikar, Patricio Arce-Johnson, H. Uchino, P. Bodegom, T. J. Higgins, Aiming Wang, Roger N. Beachy, T. Lin, M. I. Boulton, T. Natsuaki, S. Astier, A. de Kochko, E. Meiri, Marc G. Fortin, Orit Edelbaum, K. H. Hellwald, B. Falk, M. Ikegami, R. S. Zemetra, D. E. Purcifull, Rafael Rivera-Bustamante, X. W. Xiao, W. K. Kaniewski, M. M. Maugeri, Silvy Zeituny, N. H. Soliman, A. A. Brunt, S. Zimmermann, Hector D. Quemada, J. A. Daròs, I. Sela, I. Oukropec, Ab van Kammen, E. Dagless, R. Carson, P. de Haan, D. D. Shukla, P. J. Shiel, T. Ruiz-Perez, Darja Barlič Maganja, S. C. Taylor, Kristina Gruden, G. Salem, Varsha Wesley, D. L. Gellatly, V. Thole, H. Kawashima, E. Pehu, Erwin Cardol, P. Kominek, L. Mehlo, J. van Lent, K. Graichen, Frank Rabenstein, D. Robinson, J. Walter, M. Kelve, C. Porta, L. Tabe, M. El-Hariry, Johannes Fütterer, Stephen J. Wylie, A. Merits, Roger Hull, R. Goldbach, R. Arroyo, D. K. Becker, A. Ragozzino, H. Chatel, Velitchka Nikolaeva, J. F. Bol, N. Paltridge, G. I. Atiri, K. M. Taylor, A. N. Chiang, Andrew Wieczorek, K. H. Ryu, J. Polák, Y. Chupeau, J. C. Thouvenel, Daniel Plante, Na-Sheng Lin, J. Angel-Diaz, J. Porter, D. Gahakwa, A. Mooney, M. J. Frenkel, S. D. Wyatt, P. Chu, Brandt G. Cassidy, A. Van Schepen, G. R. Smith, A. R. De Rover, L. Sela, Y. Stram, Margarita Yankulova, T. Otsubo, O. Livneh, S. Tsuda, M. R. Hajimorad, J. E. Johnson, G. D. May, L. Levy, T. Candresse, Yan Yitang, Marilyn J. Roossinck, D. J. Hwang, C. M. Fauquet, J. J. L. Gielen, S. Lock, David Charles Baulcombe, B. J. Shi, M. Bitoova, Duk-Ju Hwang, E. Ham, V. M. Ursin, M. Barba, B. L. Barrón, Y. Kageyama, P. Palukaitis, Yau-Heiu Hsu, E. Aliskevicius, O. Le Gall, J. Antoniw, C. J. Arntzen, J. A. Sanchez-Navarro, T. Tamm, W. Chaleeprom, S. Dinant, S. Yu. Morozov, Biing-Yuan Lin, J. L. Badge, S. S. Bishnoi, J. L. Dale, R. Kormelink, N. E. Turner, J. P. T. Valkonen, A. E. Aboul-Ata, S. W. Ding, C. W. A. Pleij, Chu-Hui Chiang, Thomas Hohn, S. Kashiwazaki, F. Ponz, A. M. Chachulska, A. Almási, E. Vardi, J. M. Martínez-Zapater, E. Hiebert, P. Roy, Sheldon Cohen, J. Kunhara, M. Saarma, E. Truve, M. Taliansky, Marcel Prins, Joze Brzin, R. H. Symons, M. Leech, Sheng-Zhi Pang, D. A. Zelenina, M. Storms, M. Saito, M. Kinta, K. Tomaru, Peter de Haan, F. E. Christensen, J. Rathjen, S. J. Yang, E. Fuchs, A. Zelcer, I. B. Kaplan, E. C. Lawson, Hélène Sanfaçon, B. C. Rodoni, G. Mazithulela, Ching-Hsien Wang, M. Ekes, S. Wittmann, S. Schillberg, T. Maki-Valkama, E. Sivamani, M. Shams-Bakhsh, R. Turner, E. Mueller, Borut Štrukelj, M. Karamagioli, V. Somsap, A. Hernádez, A. Golshani, H. P. Loo, E. Ramirez, P. W. G. Chu, Colin W. Ward, T. B. Clifford, N. Collins, K. M. Makkouk, Amis Druka, G. D. Foster, T. Mitsky, M. F. Bateson, Igor Kregar, A. Mathews, Maria-Rosa Marano, L. Rasochova, James C. Carrington, C. A. Powell, K. Makinen, P. H. Berger, Mounir G. AbouHaidar, Nilgun Turner, J. J. English, F. Blaise, M. Q. J. M. Van Grinsven, Helen Rothnie, Frank Ratcliff, Rahat Makhdoom, Kim Carney, Y. M. Hou, R. L. Gilbertson, I. García-Luque, M. T. Serra, G. I. Dwyer, A. Murayama, Rob W. Goldbach, F. DiSerio, C. Jacquet, N. Banerjee, Stanislaw Flasinski, D. Twell, C. Kusiak, M. Chrzanowska, J. Feldman, Lidia Ivanova, Karma Carrier, John F. Bol, W. A. Miller, B. Raccah, J. A. Handley, J. Bachelier, T. Tamada, L. Nigul, R. N. Beachy, T. Kuittinen, R. Floras, A. K. Koenen, S. Guelemerov, Dennis Gonsalves, Joan Wellink, P. Gilardi, Monique M. van Oers, T. Kiguchi, L. Chen, Moshe Lapidot, G. Adam, D. H. L. Bishop, Ivan Ivanov, Shyi-Dong Yeh, G. Rodriguez-Alvarado, A. Callahan, G. Davenport, R. Stratford, B. Passmore, J. E. Faure, R. Gaborianvi, Gang Chen, Richard Kormelink, H. Huet, P. L. McCarthy, J. Drossard, Titia Sijen, R. Fischer, Z. Szigeti, P. Christou, D. Wolf, J. F. Laliberté, J. G. Atabekov, L. López, L. Tomassoli, B. A. L. M. Deiman, L. Kuznetsova, M. A. Wurscher, C. Robaglia, Q. Li, R. B. Sangwan, J. Dunez, R. M. Harding, Amit Gal-On, V. E. Spall, M. J. Soto, J. Hansen, N. Sugimura, C. A. Ong, G. P. Lodhi, Huub J. M. Linthorst, D. Li, R. Scorza, W. X. Li, Narayan Rishi, J. Schubert, M. Aulik, H. Lot, T. Kusume, R. Sanders, J. W. Davies, M. Satour, O. N. Fedorkin, G. A. Prody, M. V. Mikhailov, G. J. Hafner, Sandra Corsten, T. Pehu, Claire Huguenot, F. Garcia-Arenal, Y. P. Duan, D. Marshall, V. Pallas, A. Atanassov, P. Sithisarn-Burns, J. C. Bachelier, and J. Albouy

Subjects
0106 biological sciences, 010602 entomology, Insect Science, Ecology (disciplines), International congress, Physiology, Library science, Plant Science, Biology, 01 natural sciences, 010606 plant biology & botany
Published
2018

2. Genomic organization of RNA2 of Tomato ringspot virus: processing at a third cleavage site in the N-terminal region of the polyprotein in vitro

Author

Karma Carrier, Yu Xiang, and Hélène Sanfaçon

Subjects
Cleavage factor, Cleavage stimulation factor, Binding Sites, Nepovirus, Protein domain, Cleavage and polyadenylation specificity factor, Biology, Cleavage (embryo), biology.organism_classification, Virology, Molecular biology, Viral Proteins, Solanum lycopersicum, Endopeptidases, Tomato ringspot virus, Mutagenesis, Site-Directed, RNA, Viral, Movement protein, Protein Processing, Post-Translational
Abstract

The proteinase ofTomato ringspot virus(genusNepovirus) is responsible for proteolytic cleavage of the RNA2-encoded polyprotein (P2) at two cleavage sites, allowing definition of the domains for the movement protein (MP) and coat protein. In this study, we have characterized a third cleavage site in the N-terminal region of P2 using anin vitroprocessing assay and partial cDNA clones. Results from site-directed mutagenesis of putative cleavage sites suggest that cleavage occurs at dipeptide Q301/G. Cleavage at this site is predicted to result in the release of two proteins from the N-terminal region of P2: a 34 kDa protein located at the N terminus of P2 (assuming translation initiation at the first AUG codon) and a 71 kDa protein located immediately upstream of the MP domain. In contrast, only one protein domain is present in the equivalent region of the P2 polyprotein of other characterized nepoviruses.

Published
2001
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3. Mutagenesis of amino acids at two tomato ringspot nepovirus cleavage sites: effect on proteolytic processing in cis and in trans by the 3C-like protease

Author

Fabienne Hans, Karma Carrier, and Hélène Sanfaçon

Subjects
Cleavage factor, Proteases, medicine.medical_treatment, Nepovirus, Cleavage and polyadenylation specificity factor, Cleavage (embryo), 03 medical and health sciences, chemistry.chemical_compound, Viral Proteins, Solanum lycopersicum, Virology, RNA polymerase, medicine, Amino Acids, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Protease, Binding Sites, biology, 030302 biochemistry & molecular biology, 3C Viral Proteases, biology.organism_classification, RNA-Dependent RNA Polymerase, Amino acid, Plant Viral Movement Proteins, Cysteine Endopeptidases, chemistry, Biochemistry, Mutagenesis, Site-Directed, Protein Processing, Post-Translational
Abstract

Tomato ringspot nepovirus (ToRSV) encodes two polyproteins that are processed by a 3C-like protease at specific cleavage sites. Analysis of ToRSV cleavage sites identified previously and in this study revealed that cleavage occurs at conserved Q/(G or S) dipeptides. In addition, a Cys or Val is found in the −2 position. Amino acid substitutions were introduced in the −6 to +1 positions of two ToRSV cleavage sites: the cleavage site between the protease and putative RNA-dependent RNA polymerase, which is processed in cis , and the cleavage site at the N-terminus of the movement protein, which is cleaved in trans . The effect of the mutations on proteolytic processing at these sites was tested using in vitro translation systems. Substitution of conserved amino acids at the −2, −1, and +1 positions resulted in a significant reduction in proteolytic processing at both cleavage sites. The effects of individual substitutions were stronger on the cleavage site processed in trans than on the one processed in cis . The cleavage site specificity of the ToRSV protease is discussed in comparison to that of related proteases.

Published
1999

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