DOCSLIB.ORG

Umbravirus-Encoded Proteins Both Stabilize Heterologous Viral RNA and Mediate Its Systemic Movement in Some Plant Species

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Umbravirus-Encoded Proteins Both Stabilize Heterologous Viral RNA and Mediate Its Systemic Movement in Some Plant Species Virology 288, 391–400 (2001) doi:10.1006/viro.2001.1078, available online at http://www.idealibrary.com on View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Umbravirus-Encoded Proteins both Stabilize Heterologous Viral RNA and Mediate Its Systemic Movement in Some Plant Species Eugene V. Ryabov,1 David J. Robinson, and Michael Taliansky2 Unit of Virology, Scottish Crop Research Institute, Invergowrie, Dundee, DD2 5DA, United Kingdom Received June 1, 2001; returned to author for revision June 25, 2001; accepted July 5, 2001 The proteins encoded by open reading frame 3 (ORF3) of the umbraviruses pea enation mosaic virus-2 and tobacco mottle virus, like that of groundnut rosette virus, mediated the movement of viral RNA through the phloem of infected Nicotiana benthamiana or N. clevelandii plants when they were expressed from chimeric tobacco mosaic virus in place of the coat protein. However, these chimeras did not move systemically in N. tabacum. In lysates of N. benthamiana or N. tabacum protoplasts, the chimeric RNAs were more stable than was RNA of tobacco mosaic virus lacking the coat protein gene. The chimeric viruses also protected the latter in trans, suggesting that the ORF3 proteins can increase the stability of heterologous viral RNA. Umbraviral ORF3 proteins contain a conserved arginine-rich domain, and the possible roles of this motif in the functions of the proteins are discussed. © 2001 Academic Press Key Words: plant virus; umbraviruses; virus movement; stabilization of viral RNA. INTRODUCTION spread of the umbraviruses (Demler et al., 1994). More- over, unlike most single-stranded viral RNAs, umbraviral The coat protein (CP) encoded by most plant viruses fulfills various biological functions, primarily the protec- RNA remains infective in crude sap extracts for several tion of viral RNA by encapsidating it to form virus nucleo- hours (Murant et al., 1969; Reddy et al., 1985). These protein particles. The CP is also usually involved in the observations suggest that umbraviruses can exploit one transmission of viruses by their biological vectors and in or more alternative mechanisms for RNA protection and the systemic spread of viruses in infected plants (see for systemic spread, different from those provided by a CP. reviews, Carrington et al., 1996; Harrison and Murant, The RNA genomes of umbraviruses contain four open Ј 1984). Some plant viruses, such as potato virus X (PVX; reading frames (ORFs) (Fig. 1A). The two ORFs at the 5 Chapman et al., 1992), cucumber mosaic virus (CMV; end of the RNA are expressed by a Ϫ1 frameshift to yield Canto et al., 1997), and cowpea mosaic virus (Wellink a single protein that appears to be an RNA-dependent and van Kammen, 1989), require the CP for both cell-to- RNA polymerase (Demler et al., 1993; Taliansky et al., cell and long-distance movement. Others, such as to- 1996; Gibbs et al., 1996). The other two ORFs overlap bacco mosaic virus (TMV), do not depend on CP for each other in different reading frames. ORF4 encodes a cell-to-cell movement but do require it for long-distance 27- to 29-kDa protein, which contains stretches of simi- movement (Siegel et al., 1962; Takamatsu et al., 1987; larity with several plant virus-encoded movement pro- Saito et al., 1990; Osbourn et al., 1990; Holt and Beachy, teins (MPs) that control virus movement from cell-to-cell 1991; Hilf and Dawson, 1993; Spitsin et al., 1999). The (Taliansky et al., 1996; Gibbs et al., 1996). In gene re- genomes of umbraviruses (genus Umbravirus) differ from placement experiments, the ORF4 protein encoded by those of all other plant viruses in that they do not encode one of the umbraviruses, groundnut rosette virus (GRV), a CP, and thus no virus particles are formed in infected was shown to be able to functionally replace the MPs of plants (see for review, Robinson and Murant, 1999). Nev- PVX or CMV (Ryabov et al., 1998, 1999a), confirming that ertheless, umbraviruses can accumulate and spread the GRV ORF4 protein is a cell-to-cell MP. The ORF4 very efficiently within plants. Although umbraviruses de- protein enabled cell-to-cell movement of PVX and CMV pend on the assistance of a luteovirus for aphid trans- regardless of the presence or absence of their CPs, but mission, the presence or absence of the luteovirus and the CPs were still required for long-distance movement. its CP does not affect the accumulation and systemic Database searches with the sequence of the umbra- viral 26- to 29-kDa ORF3 proteins revealed no significant 1 similarity with any other viral or nonviral proteins, except Present address: Horticulture Research International-East Malling, the corresponding proteins encoded by different umbra- West Malling, Kent, ME19 6BJ, UK. 2 To whom correspondence and reprint requests should be ad- viruses (Taliansky et al., 1996). In epidermal and meso- dressed. Fax: 44-1382-562426. E-mail: [email protected]. phyll cells, the GRV ORF3 protein is located in small 0042-6822/01 $35.00 391 Copyright © 2001 by Academic Press All rights of reproduction in any form reserved. 392 RYABOV, ROBINSON, AND TALIANSKY amino acid sequence identity to the corresponding parts of the polypeptides encoded by ORF 2 of GRV (Taliansky et al., 1996), carrot mottle mimic virus (CMoMV; Gibbs et al., 1996), and PEMV-2 (Demler et al., 1993). At the 3Ј end of the partial sequence are two overlapping ORFs, which are arranged in the same way as ORF3 and ORF4 of other umbraviruses (Fig. 1A) and which will be referred to as ORF3 and ORF4 of TMoV. ORF4 encompasses 765 nucleotides and codes for a protein of 254 amino acid residues and a molecular mass of 28 kDa, with 46 to 63% amino acid sequence identity to the ORF4 proteins en- coded by other umbraviruses. The sequence of TMoV ORF3 contains only one po- tential AUG translation start codon and comprises 705 nucleotides. The polypeptide it encodes consists of 234 amino acid residues, with a molecular mass of 26 kDa and with 29 to 35% amino acid sequence identity to the ORF3 proteins of other umbraviruses (Fig. 2). The ORF3 proteins are rich in arginine, proline, serine, and glycine FIG. 1. Schematic representation of the genome of umbraviruses (A) residues. Measurement of local compositional complex- and of the TMV-based vector TMV(30B) and its derivatives expressing ity, using the SEG program (Wootton and Federhen, 1996) umbraviral ORF3s or the GFP gene (B). Boxes represent ORFs, lines represent untranslated sequences. MP, TMV movement protein; CP, indicates that 85–95% of residues in each protein fall TMV coat protein; (•) subgenomic promoter. Deleted sequences are within predicted low-complexity, nonglobular regions. indicated. The part of the umbraviral genome corresponding to the The amino terminal halves of the sequences (positions nucleotide sequences of TMoV RNA that were determined is high- 25–145 of the alignment; Fig. 2) are the most hydrophilic lighted in A. and include a highly basic arginine-rich domain (posi- tions 109–123; Fig. 2) with four conserved arginine resi- dues. The ORF3 protein sequences also contain a hy- membrane-associated cytoplasmic vesicles and in the drophobic element (positions 146–169 of the alignment, nuclei, preferentially targeting nucleoli (Ryabov et al., Fig. 2) which includes three invariant leucine residues. 1998). Recently, we showed that the GRV ORF3 protein Plants infected with the pea enation mosaic virus facilitated the long-distance movement of TMV RNA in complex consisting of pea enation mosaic virus-1 cis and in trans, replacing the TMV CP, which is normally (PEMV-1), a luteovirus, and PEMV-2, an umbravirus, pro- essential for the long-distance movement of TMV RNA duce virus particles containing both PEMV-1 RNA and (Ryabov et al., 1999b). In this work, we show that the PEMV-2 RNA encapsidated by the PEMV-1 CP. Thus, to ORF3 proteins encoded by two other umbraviruses, pea generate cDNA clones corresponding to the PEMV-2 enation mosaic virus-2 (PEMV-2) and tobacco mottle ORF3, viral RNA isolated from such particles was used virus (TMoV), are also able to mediate long-distance for reverse transcription–PCR. The primers were de- movement of heterologous TMV RNA. However, the fa- signed according to the PEMV-2 sequence published by cilitation of long-distance movement of RNA by the um- Demler et al. (1993, 1994). The sequence of the PEMV-2 braviral ORF3 proteins is host-specific. We also show ORF3 fragment generated (GeneBank Accession No. that the ORF3 proteins can stabilize TMV RNA in lysates AY007257; Fig. 2) was essentially similar to that pub- of infected protoplasts. lished by Demler et al. (1993, 1994) and encoded a protein with only six amino acid differences, all in non- RESULTS conserved regions. Like GRV ORF3 and in contrast to TMoV ORF3 and CMoMV ORF3, PEMV-2 ORF3 contains PEMV-2 and TMoV ORF3 and generation of chimeric at the 5Ј end two in-frame AUG codons. However, muta- TMV tional analysis (Demler et al., 1994) has shown that the cDNA clones corresponding to TMoV RNA were gen- upstream AUG initiation codon is essential for PEMV-2 erated from virus specific dsRNA isolated from TMoV- infectivity. infected Nicotiana benthamiana plants. The partial ge- The CP gene of TMV was deleted and replaced by nome sequence obtained (GeneBank Accession No. ORF3 of either PEMV-2 or TMoV in a TMV-based vector, AY007231; see also Fig. 1A) is similar to the genome TMV(30B) (Shivprasad et al., 1999), to give the hybrids sequences of other umbraviruses. At the 5Ј end is an TMV(ORF3P) and TMV(ORF3T), respectively, as de- incomplete ORF capable of coding for a polypeptide scribed previously for the hybrid containing GRV ORF3 consisting of 361 amino acid residues, with 66.5 to 67.5% (Ryabov et al., 1999b; Fig.
Load more

Recommended publications
  • Groundnut Rosette Disease and Their Diagnosis a F Murant, D J Robinson, and M E Taliansky 5
    Citation: Reddy, D.V.R., Delfosse, P., Lenne, J.M., and Subrahmanyam, P. (eds.) 1997. Groundnut virus diseases in Africa: summary and recommendations of the Sixth Meeting of the International Working Group, 18-19 Mar 1996, Agricultural Research Council, Plant Protection Research Institute, Pretoria, South Africa. (In En. Summaries in En, Fr, Pt) Patancheru 502 324, Andhra Pradesh, India: International Crops Research Institute for the Semi-Arid Tropics; and 1000 Brussels, Belgium: Belgian Administration for Development Cooperation. 64 pp. ISBN 92-9066-358-8. Order code: CPE 109. Abstract The International Working Group Meeting on groundnut viruses in Africa reviewed progress made on the detection, identification, characterization, and management of groundnut viruses in Africa, with special emphasis on rosette and clump viruses. Country representatives summarized the status of research on groundnut viruses in their countries. In order to accomplish integrated management of rosette and clump virus diseases, it was agreed that consolidated efforts should be made to understand their epidemiology. Among the important aspects discussed were the provision of diagnostic aids and training in the identifi­ cation and detection of viruses for the national agricultural research systems in Africa, and strengthening of laboratory facilities. Scientists from Burkina Faso, Kenya, Malawi, Nigeria, South Africa, and Zimbabwe, and from Bel­ gium, Germany, India, UK, and USA attended the meeting, which was the first gathering of so many plant virologists in
    [Show full text]
  • Interaction of a Plant Virus-Encoded Protein with the Major Nucleolar Protein Fibrillarin Is Required for Systemic Virus Infection
    Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection Sang Hyon Kim†, Stuart MacFarlane†, Natalia O. Kalinina†‡, Daria V. Rakitina†‡, Eugene V. Ryabov§, Trudi Gillespie†, Sophie Haupt†, John W. S. Brown†, and Michael Taliansky†¶ †Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom; ‡A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia; and §Horticulture Research International, University of Warwick, Wellesbourne, Warwick CV35 9EF, United Kingdom Communicated by Bryan D. Harrison, Scottish Crop Research Institute, Dundee, United Kingdom, May 17, 2007 (received for review April 4, 2007) The nucleolus and specific nucleolar proteins are involved in the life Umbraviruses have RNA genomes and differ from most other cycles of some plant and animal viruses, but the functions of these viruses in that they do not encode a coat protein (CP) and so do not proteins and of nucleolar trafficking in virus infections are largely produce conventional virus particles in infected plants (15, 16). unknown. The ORF3 protein of the plant virus, groundnut rosette Nevertheless, they accumulate and spread efficiently within the virus (an umbravirus), has been shown to cycle through the infected plant; their lack of a CP is compensated for by the ORF3 nucleus, passing through Cajal bodies to the nucleolus and then protein. This protein fulfils umbraviral functions that are normally exiting back into the cytoplasm. This journey is absolutely required provided by the CPs of other plant viruses, such as long-distance for the formation of viral ribonucleoprotein particles (RNPs) that, movement of viral RNA through the phloem (17, 18).
    [Show full text]
  • Sequence Diversity Within the Three Agents of Groundnut Rosette Disease
    Virology Sequence Diversity Within the Three Agents of Groundnut Rosette Disease C. M. Deom, R. A. Naidu, A. J. Chiyembekeza, B. R. Ntare, and P. Subrahmanyam First author: Department of Plant Pathology, Plant Sciences Building, The University of Georgia, Athens 30602-7274; second and fifth authors: Genetic Resources and Enhancement Program (GREP), International Crops Research Institute for the Semi-Arid Tropics (ICRISAT), P.O. Box 1096, Lilongwe, Malawi; third author: Department of Agricultural Research and Technical Services, Chitedze Agricultural Research Station, Lilongwe, Malawi; fourth author: GREP, ICRISAT, P.O. Box 320, Bamako, Mali. Current address of R. A. Naidu: Department of Plant Pathology, The University of Georgia, Athens 30602-7274. Accepted for publication 5 December 1999. ABSTRACT Deom, C. M., Naidu, R. A., Chiyembekeza, A. J., Ntare, B. R., and isolates within a geographic region but less conserved (88 to 89%) be- Subrahmanyam, P. 2000. Sequence diversity within the three agents of tween isolates from the two distinct geographic regions. Phylogenetic groundnut rosette disease. Phytopathology 90:214-219. analysis of the overlapping ORFs 3 and 4 show that the GRV isolates cluster according to the geographic region from which they were iso- Sequence diversity was examined in the coat protein (CP) gene of lated, indicating that Malawian GRV isolates are distinct from Nigerian Groundnut rosette assistor virus (GRAV), the overlapping open reading GRV isolates. Similarity within the sat-RNA sequences analyzed ranged frames (ORFs) 3 and 4 of Groundnut rosette virus (GRV), and the satel- from 88 to 99%. Phylogenetic analysis also showed clustering within the lite RNA (sat-RNA) of GRV obtained from field isolates from Malawi sat-RNA isolates according to country of origin, as well as within isolates and Nigeria.
    [Show full text]
  • The Ins and Outs of Nondestructive Cell-To-Cell and Systemic Movement of Plant Viruses
    Critical Reviews in Plant Sciences, 23(3):195–250 (2004) Copyright C Taylor and Francis Inc. ISSN: 0735-2689 print / 1549-7836 online DOI: 10.1080/07352680490452807 The Ins and Outs of Nondestructive Cell-to-Cell and Systemic Movement of Plant Viruses Elisabeth Waigmann Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Institute of Medical Biochemistry, Medical University of Vienna, Dr. Bohrgasse 9 A-1030, Vienna, Austria Shoko Ueki Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794-5215 Kateryna Trutnyeva Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Institute of Medical Biochemistry, Medical University of Vienna, Dr. Bohrgasse 9 A-1030, Vienna, Austria Vitaly Citovsky∗ Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794-5215 Referee: Dr. Ernest Hiebert, Professor, Department of Plant Pathology, University of Florida/IFAS, P.O. Box 110680, 1541 Fifield Hall, Gainesville, FL 32611-0680, USA. Table of Contents 1. Introduction ..........................................................................................................................................................196 2. Structure and Composition of Plasmodesmata, the Intercellular Conduits for Viral Movement ..............................198 3. Cell-to-Cell Transport of Plant Viruses: Have Movement Protein, Will Travel ........................................................200 3.1. MP Structure: Are Common Functions Supported by
    [Show full text]
  • Virus World As an Evolutionary Network of Viruses and Capsidless Selfish Elements
    Virus World as an Evolutionary Network of Viruses and Capsidless Selfish Elements Koonin, E. V., & Dolja, V. V. (2014). Virus World as an Evolutionary Network of Viruses and Capsidless Selfish Elements. Microbiology and Molecular Biology Reviews, 78(2), 278-303. doi:10.1128/MMBR.00049-13 10.1128/MMBR.00049-13 American Society for Microbiology Version of Record http://cdss.library.oregonstate.edu/sa-termsofuse Virus World as an Evolutionary Network of Viruses and Capsidless Selfish Elements Eugene V. Koonin,a Valerian V. Doljab National Center for Biotechnology Information, National Library of Medicine, Bethesda, Maryland, USAa; Department of Botany and Plant Pathology and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, Oregon, USAb Downloaded from SUMMARY ..................................................................................................................................................278 INTRODUCTION ............................................................................................................................................278 PREVALENCE OF REPLICATION SYSTEM COMPONENTS COMPARED TO CAPSID PROTEINS AMONG VIRUS HALLMARK GENES.......................279 CLASSIFICATION OF VIRUSES BY REPLICATION-EXPRESSION STRATEGY: TYPICAL VIRUSES AND CAPSIDLESS FORMS ................................279 EVOLUTIONARY RELATIONSHIPS BETWEEN VIRUSES AND CAPSIDLESS VIRUS-LIKE GENETIC ELEMENTS ..............................................280 Capsidless Derivatives of Positive-Strand RNA Viruses....................................................................................................280
    [Show full text]
  • Jiang J, Kuo YW, Salem N, Erickson A, Falk BW. 2021. Carrot Mottle
    Research Carrot mottle virus ORF4 movement protein targets plasmodesmata by interacting with the host cell SUMOylation system Jun Jiang1 , Yen-Wen Kuo1 , Nida Salem2 , Anna Erickson1 and Bryce W. Falk1 1Department of Plant Pathology, University of California, Davis, CA 95616, USA; 2Department of Plant Protection, School of Agriculture, The University of Jordan, Amman 11942, Jordan Summary Author for correspondence: Plant virus movement proteins (MPs) facilitate virus spread in their plant hosts, and some of Bryce W. Falk them are known to target plasmodesmata (PD). However, how the MPs target PD is still Email: [email protected] largely unknown. Carrot mottle virus (CMoV) encodes the ORF3 and ORF4 proteins, which are involved in Received: 8 February 2021 CMoV movement. In this study, we used CMoV as a model to study the PD targeting of a plant virus MP. We showed that the CMoV ORF4 protein, but not the ORF3 protein, modified PD and led New Phytologist (2021) to the virus movement. We found that the CMoV ORF4 protein interacts with the host cell doi: 10.1111/nph.17370 small ubiquitin-like modifier (SUMO) 1, 2 and the SUMO-conjugating enzyme SCE1, result- ing in the ORF4 protein SUMOylation. Downregulation of mRNAs for NbSCE1 and NbSUMO Key words: Carrot mottle virus (CMoV), impaired CMoV infection. The SUMO-interacting motifs (SIMs) LVIVF, VIWV, and a lysine movement proteins (MPs), plasmodesmata residue at position 78 (K78) are required for the ORF4 protein SUMOylation. The mutation of (PD), small ubiquitin-like modifier (SUMO), these motifs prevented the protein to efficiently target PD, and further slowed or completely Umbravirus.
    [Show full text]
  • This Lists All Proposals Ratified at Glasgow Congress on the 10Th August 1993
    New taxa ratified in 1993 [from Pringle (1993) Arch Virol 133:491-495] This lists all proposals ratified at Glasgow Congress on the 10th August 1993. These appear to be all the proposals since the 1990 Congress and are to be incorporated into the 6th Report so should contain all changes between the 5th and 6th Reports. Informal codes in red have been assigned by MJA for convenient reference but are not used in any minutes or other formal records. Bacterial viruses The Chlamydia phages [1993.01B] 1. To establish a new genus within the family Microviridae 2. To name the new genus Chlamydiamicrovirus 3. To designate Chlamydia phage Chp 1 as type virus of the genus The Mac-1 type phages [1993.02B] l. To establish a new genus within the family Microviridae 2. To name the genus containing Mac-1 and related phages Bdellomicrovirus 3. To establish Mac-1 as the type species of the genus The SSV-1 type phages [1993.03B] 1. To name the family containing SSV-1 type phages Fuselloviridae 2. To name the SSV-1 group genus Fusellovirus Protozoal and fungal viruses Totiviruses [1993.01F] 1. To revise the classification of the Giardiavirus genus of dsDNA protozoal viruses from a possible genus in the family Totiviridae to a legitimate genus 2. To establish a new genus of isometric dsRNA viruses of the parasitic protozoan Leishmania braziliensis within the family Totiviridae 3. To name the genus Leishmaniavirus 4. To designate Leishmania RNA Virus 1-1 (LRV1-1) as the type species of the genus Bacilliform viruses of fungi [1993.02F] 1.
    [Show full text]
  • Satellite RNA Is Essential for Encapsidation of Groundnut Rosette Umbravirus RNA by Groundnut Rosette Assistor Luteovirus Coat Protein
    Virology 254, 105–114 (1999) Article ID viro.1998.9527, available online at http://www.idealibrary.com on View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Satellite RNA Is Essential for Encapsidation of Groundnut Rosette Umbravirus RNA by Groundnut Rosette Assistor Luteovirus Coat Protein D. J. Robinson, E. V. Ryabov, S. K. Raj,1 I. M. Roberts, and M. E. Taliansky2 Virology Department, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom Received September 11, 1998; returned to author for revision September 28, 1998; accepted November 17, 1998 Groundnut rosette disease is caused by a complex of agents comprising groundnut rosette umbravirus (GRV), GRV satellite RNA (sat-RNA) and groundnut rosette assistor luteovirus (GRAV). Both GRAV and GRV sat-RNA are needed for GRV to be aphid transmissible. To understand the role of GRAV and GRV sat-RNA in the aphid transmission of GRV, encapsidation of GRV genomic and satellite RNAs has been studied using transgenic Nicotiana benthamiana plants expressing GRAV coat protein (CP). GRAV CP expressed from a transgene was shown to package GRV genomic and satellite RNAs efficiently, giving a high yield of transcap- sidated virus particles. GRV sat-RNA was absolutely essential for this process. GRV genomic RNA was not encapsidated by GRAV CP in the absence of the sat-RNA. Using different mutants of GRV sat-RNA, it was found that some property of full-length satellite RNA molecules, such as size or specific conformation rather than potential open reading frames, was required for the production of virus particles.
    [Show full text]
  • Controlling Epidemics of Emerging and Established Plant Virus Diseases - the Way Forward
    10th International Plant Virus Epidemiology Symposium Controlling Epidemics of Emerging and Established Plant Virus Diseases - The Way Forward 15-19 October 2007, ICRISAT Patancheru 502324, AP, India Program and Abstracts ® Organized and Hosted by the International Crops Research Institute for the Semi-Arid Tropics Program 10th International Plant Virus Epidemiology Symposium Controlling Epidemics of Emerging and Established Plant Virus Diseases - The Way Forward 15 - 19 October 2007 International Crops Research Institute for the Semi-Arid Tropics Patancheru 502 324, Hyderabad, Andhra Pradesh, India Program and Abstracts Compiled by 1 2 3 P Lava Kumar , RAC Jones and F Waliyar 1International Institute of Tropical Agriculture, Nigeria 2Agriculture Research Western Australia, Australia 3International Crops Research Institute for the Semi-Arid Tropics, India 10th Plant Virus Epidemiology Symposium, 15 – 19 Oct 07, ICRISAT, India i Program About ICRISAT The International Crops Research Institute for the Semi-Arid Tropics (ICRISAT) is a non-profit, non-political international for science based agricultural development. ICRISAT conducts research on sorghum, pearl millet, chickpea, groundnut and pigeonpea – crops that support the livelihoods of the poorest of the poor in the semi- arid tropics encompassing 48 countries. ICRISAT also shares information and knowledge through capacity building, publications, and information and communication technologies. Established in 1972, ICRISAT belongs to the Alliance of Centers supported by the Consultative Group on International Agricultural Research (CGIAR) [www.icrisat.org; www.cgiar.org]. About IPVE International Plant Virus Epidemiology (IPVE) Group is a coordinated by the IPVE Committee of the International Society of Plant Pathology (ISPP). The ISPP was founded in 1968 in the United Kingdom to sponsor the development of plant pathology worldwide.
    [Show full text]
  • Interaction of a Plant Virus-Encoded Protein with the Major Nucleolar Protein Fibrillarin Is Required for Systemic Virus Infection
    Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection Sang Hyon Kim†, Stuart MacFarlane†, Natalia O. Kalinina†‡, Daria V. Rakitina†‡, Eugene V. Ryabov§, Trudi Gillespie†, Sophie Haupt†, John W. S. Brown†, and Michael Taliansky†¶ †Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom; ‡A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia; and §Horticulture Research International, University of Warwick, Wellesbourne, Warwick CV35 9EF, United Kingdom Communicated by Bryan D. Harrison, Scottish Crop Research Institute, Dundee, United Kingdom, May 17, 2007 (received for review April 4, 2007) The nucleolus and specific nucleolar proteins are involved in the life Umbraviruses have RNA genomes and differ from most other cycles of some plant and animal viruses, but the functions of these viruses in that they do not encode a coat protein (CP) and so do not proteins and of nucleolar trafficking in virus infections are largely produce conventional virus particles in infected plants (15, 16). unknown. The ORF3 protein of the plant virus, groundnut rosette Nevertheless, they accumulate and spread efficiently within the virus (an umbravirus), has been shown to cycle through the infected plant; their lack of a CP is compensated for by the ORF3 nucleus, passing through Cajal bodies to the nucleolus and then protein. This protein fulfils umbraviral functions that are normally exiting back into the cytoplasm. This journey is absolutely required provided by the CPs of other plant viruses, such as long-distance for the formation of viral ribonucleoprotein particles (RNPs) that, movement of viral RNA through the phloem (17, 18).
    [Show full text]
  • Encyclopedia of Plant Viruses and Viroids K
    Encyclopedia of Plant Viruses and Viroids K. Subramanya Sastry • Bikash Mandal John Hammond • S. W. Scott R. W. Briddon Encyclopedia of Plant Viruses and Viroids K. Subramanya Sastry Bikash Mandal Indian Council of Agricultural Indian Agricultural Research Institute Research, IIHR New Delhi, India Bengaluru, India Indian Council of Agricultural Research, IIOR and IIMR Hyderabad, India John Hammond S. W. Scott USDA, Agricultural Research Service Clemson University Beltsville, MD, USA Clemson, SC, USA R. W. Briddon John Innes Centre Norwich, UK ISBN 978-81-322-3911-6 ISBN 978-81-322-3912-3 (eBook) ISBN 978-81-322-3913-0 (print and electronic bundle) https://doi.org/10.1007/978-81-322-3912-3 # Springer Nature India Private Limited 2019 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors, and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, expressed or implied, with respect to the material contained herein or for any errors or omissions that may have been made.
    [Show full text]
  • Genetic Diversity of Groundnut Rosette Disease Causal Agents Towards Its Management: a Review
    International Journal of Genetics and Genomics 2019; 7(1): 12-17 http://www.sciencepublishinggroup.com/j/ijgg doi: 10.11648/j.ijgg.20190701.12 ISSN: 2376-7340 (Print); ISSN: 2376-7359 (Online) Review Article Genetic Diversity of Groundnut Rosette Disease Causal Agents Towards Its Management: A Review Benard Mukoye *, Anthony Simiyu Mabele Department of Biological Sciences, School of Natural Sciences (SONAS), Masinde Muliro University of Science and Technology (MMUST), Kakamega, Kenya Email address: *Corresponding author To cite this article: Benard Mukoye, Anthony Simiyu Mabele. Genetic Diversity of Groundnut Rosette Disease Causal Agents Towards Its Management: A Review. International Journal of Genetics and Genomics. Vol. 7, No. 1, 2019, pp. 12-17. doi: 10.11648/j.ijgg.20190701.12 Received : March 7, 2019; Accepted : April 16, 2019; Published : June 3, 2019 Abstract: In this review, the genetic diversity of the three causal agents of Groundnut Rosette Disease (GRD) in Sub-Saharan Africa (SSA) are discussed. Epidemics of GRD viruses in SSA, often reduce groundnut productivity. The etiology of GRD is a complex, involving three agents; Groundnut rosette assistor luteovirus (GRAV), Groundnut rosette umbravirus (GRV) and a Satellite-RNA (Sat-RNA) of GRV. The complex etiology and lack of sensitive and specific diagnostic tools, are major limitations in understanding the epidemiology of GRD viruses, and developing appropriate management strategies for the disease. Nucleotide identity of 97 to 100% among GRAV isolates from different regions in Kenya have been reported. Sat-RNA sequences from Kenya shared nucleotide identity of 95% with Malawian isolate (M24S) and 89% with Nigerian isolate (NG3a). GRAV CP gene was highly conserved (97-99%) regardless of the geographical distance.
    [Show full text]