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Jean Dunez - One of the best experts on this subject based on the ideXlab platform.
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Characterization of a New Nepovirus Infecting Apricot in Southeastern France: Apricot Latent Ringspot Virus
European Journal of Plant Pathology, 2001Co-Authors: Pascal Gentit, Thierry Candresse, René-pierre Delbos, Jean DunezAbstract:A pathogen was transmitted from apricot trees showing symptoms of viral infection to GF305 peach seedlings which reacted by stunting, shortened internodes and chlorotic mottling. The agent was transmitted to cherry, apricot, peach and plum by grafting and to several herbaceous hosts by mechanical inoculation. Isometric nepovirus-like particles of 30–31 nm diameter extracted from infected Chenopodium quinoa sedimented as two peaks in sucrose gradients. These particles contained two single stranded RNAs of approximately 5.9 and 7.9 kb, and a single coat protein subunit of 53.7 kDa. No cross-reactions were observed with a number of Nepoviruses infecting fruit trees. Inoculation of purified particles to herbaceous or woody hosts reproduced the same symptoms caused by the original isolate. Sequencing of a 2.2 kbp cDNA clone covering the 3′ end of the small genomic RNA identified an open reading frame encoding a 317 aa N-truncated protein exhibiting significant similarities with the coat protein of Nepoviruses. The 1257 nt long 3′ non-coding region showed up to about 65% homology to the equivalent region of members of the subgroup C of Nepoviruses. The properties of this pathogen do not match those of any previously described nepovirus. It should therefore be considered as a new member of the subgroup C of Nepoviruses, for which the name of Apricot latent ringspot virus (ALRSV) is proposed. The nucleotide sequence reported in this work has been deposited in the EMBL databank under the accession number AJ278875.
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Characterization of a New Nepovirus Infecting Apricot in Southeastern France: Apricot Latent Ringspot Virus
European Journal of Plant Pathology, 2001Co-Authors: Pascal Gentit, Thierry Candresse, René-pierre Delbos, Jean DunezAbstract:A pathogen was transmitted from apricot trees showing symptoms of viral infection to GF305 peach seedlings which reacted by stunting, shortened internodes and chlorotic mottling. The agent was transmitted to cherry, apricot, peach and plum by grafting and to several herbaceous hosts by mechanical inoculation. Isometric nepovirus-like particles of 30–31 nm diameter extracted from infected Chenopodium quinoa sedimented as two peaks in sucrose gradients. These particles contained two single stranded RNAs of approximately 5.9 and 7.9 kb, and a single coat protein subunit of 53.7 kDa. No cross-reactions were observed with a number of Nepoviruses infecting fruit trees. Inoculation of purified particles to herbaceous or woody hosts reproduced the same symptoms caused by the original isolate. Sequencing of a 2.2 kbp cDNA clone covering the 3′ end of the small genomic RNA identified an open reading frame encoding a 317 aa N-truncated protein exhibiting significant similarities with the coat protein of Nepoviruses. The 1257 nt long 3′ non-coding region showed up to about 65% homology to the equivalent region of members of the subgroup C of Nepoviruses. The properties of this pathogen do not match those of any previously described nepovirus. It should therefore be considered as a new member of the subgroup C of Nepoviruses, for which the name of Apricot latent ringspot virus (ALRSV) is proposed. The nucleotide sequence reported in this work has been deposited in the EMBL databank under the accession number AJ278875.
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Transgenic tobaccos transformed with a gene encoding a truncated form of the coat protein of tomato black ring nepovirus are resistant to viral infection.
Plant cell reports, 1999Co-Authors: C Pacot-hiriart, O. Gall, Thierry Candresse, R. P. Delbos, Jean DunezAbstract:Tomato black ring virus (TBRV) belongs to the Nepoviruses, an important genus of phytoviruses characterized by isometric particles and by their transmission by longidorid nematodes. As for all other Nepoviruses, the coat protein (CP) of TBRV is encoded by the 3′ terminal part of the viral RNA2 (positions 2801–4334). A hybrid gene driving the expression of a truncated form of the TBRV CP was constructed. It contains a frameshift deletion at position T4065 so that in the encoded protein the last 90 amino acids of the wild-type CP are replaced by 52 amino acids encoded by a different reading frame of the viral RNA. This hybrid gene was introduced into the genome of Nicotiana tabacum cv 'Xanthi' plants. When compared to control plants, progeny of some transformants expressing the mutated CP gene (CPm+ plants) showed resistance against TBRV infection. This resistance is characterized by a delay in the appearance of symptoms, a reduction in the number of infected plants and a reduction in virus accumulation.
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An RNA-dependent-RNA-polymerase activity associated with grapevine chrome mosaic nepovirus infection
Archives of Virology, 1997Co-Authors: Olivier Gall, Thierry Candresse, Jean DunezAbstract:A virus-induced, viral RNA-specific, RNA-dependent-RNA-poly-merase activity has been observed in vitro associated with membrane extracts of plants of three different species after infection with grapevine chrome mosaic nepovirus (GCMV). The products of this activity are full-length, positive sense GCMV RNAs present in double-stranded structures. As has been demonstrated for a relative to Nepoviruses, cowpea mosaic comovirus, this activity probably corresponds to the nepoviral replication complex.
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A multiple alignment of the capsid protein sequences of Nepoviruses and comoviruses suggests a common structure
Archives of Virology, 1995Co-Authors: O. Gall, Thierry Candresse, Jean DunezAbstract:The amino acid sequences of the regions encoding the structural proteins of eleven Nepoviruses and five comoviruses, two genera of the family Comoviridae , have been aligned. The properties predicted by computer analysis (three-dimensional-3D-structure, hydrophobicity) are also correlated along this alignment, and aligned to the experimentally determined 3D structure of two comoviruses. It can thus be assumed that the 3D structure of the unique nepovirus coat protein matches that of the bipartite protomer found in the comovirus particles. In this model, the spatial locations of two amino-acid motifs characteristic of Nepoviruses are in close vicinity, at the external surface of the virion. The coat proteins of Nepoviruses and comoviruses may thus share a common evolutionary origin. A phylogenetic analysis was made using the multiple alignment, allowing a better understanding of the molecular relationships between these two groups of viruses.
Hélène Sanfaçon - One of the best experts on this subject based on the ideXlab platform.
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A Renaissance in Nepovirus Research Provides New Insights Into Their Molecular Interface With Hosts and Vectors.
Advances in virus research, 2016Co-Authors: Marc Fuchs, Corinne Schmitt-keichinger, Hélène SanfaçonAbstract:Nepoviruses supplied seminal landmarks to the historical trail of plant virology. Among the first agriculturally relevant viruses recognized in the late 1920s and among the first plant viruses officially classified in the early 1970s, Nepoviruses also comprise the first species for which a soil-borne ectoparasitic nematode vector was identified. Early research on Nepoviruses shed light on the genome structure and expression, biological properties of the two genomic RNAs, and mode of transmission. In recent years, research on Nepoviruses enjoyed an extraordinary renaissance. This resurgence provided new insights into the molecular interface between viruses and their plant hosts, and between viruses and dagger nematode vectors to advance our understanding of some of the major steps of the infectious cycle. Here we examine these recent findings, highlight ongoing work, and offer some perspectives for future research.
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Insertion of large amino acid repeats and point mutations contribute to a high degree of sequence diversity in the X4 protein of tomato ringspot virus (genus Nepovirus)
Archives of Virology, 2009Co-Authors: Bita Jafarpour, Hélène SanfaçonAbstract:Tomato ringspot virus (ToRSV) is a serious pathogen of small fruits and fruit trees in North America [14]. Several ToRSV isolates have been described that differ in natural host range and intensity of symptoms in herbaceous hosts [3, 17]. Tomato ringspot virus is a species of the genus Nepovirus [15], which has recently been reassigned to the proposed new family ‘‘Secoviridae’’ (subfamily ‘‘Comovirinae’’) within the order Picornavirales [16]. Nepoviruses have a bipartite positive-strand RNA genome. Each RNA encodes a polyprotein that is cleaved by the viral proteinase (Pro) at specific cleavage sites. RNA1 encodes replication proteins, while RNA2 codes for the coat protein (CP), movement protein (MP) and other protein(s) of less defined function. Using in vitro processing assays, three proteinase cleavage sites have been identified in the RNA2encoded polyprotein of ToRSV (a subgroup C nepovirus), allowing the definition of four protein domains (X3, X4, MP and CP) [4, 5]. In contrast, only three protein domains are present in the polyprotein of subgroup A and B Nepoviruses (2a, MP and CP; see Fig. 1a). The ToRSV X3 protein shares conserved sequence motifs with the 2a protein of subgroup A and B Nepoviruses [12]. The 2a protein of grapevine fanleaf virus has been shown to play a role in the replication of RNA2 [7]. The ToRSV X4 protein does not have significant sequence identity with proteins available in the database and does not have a functional equivalent in the genome of Nepoviruses of subgroups A and B (Fig. 1a). The only other nepovirus of subgroup C for which the entire nucleotide sequence is available is blackcurrant reversion virus (BRV). The extent of sequence identity between ToRSV and BRV is very low in the deduced amino acid (a.a.) sequence of the X4 protein (8%) but higher in the deduced a.a. sequence of the CP (29%), VPg (viral protein linked to the genome), Pro and polymerase (Pol) (36%). In this study, we examined the extent of sequence diversity in the X4 protein among closely related ToRSV isolates. We show that there is a high degree of sequence diversity in the X4 protein, which is due in part to the insertion of multiple copies of two types of large amino acid repeats.
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Characterization of proteinase cleavage sites in the N-terminal region of the RNA1-encoded polyprotein from Arabis mosaic virus (subgroup A nepovirus)
Virology, 2008Co-Authors: Thierry Wetzel, Joan Chisholm, Alexandra Bassler, Hélène SanfaçonAbstract:Arabis mosaic virus is a subgroup A nepovirus. The RNA1-encoded polyprotein (P1) contains the domains for the NTP-binding protein (NTB), VPg, proteinase (Pro) and polymerase at its C-terminus. Putative cleavage sites delineating these domains have been proposed. However, the number and location of cleavage sites upstream of the NTB domain are not known. Using in vitro processing assays, we have confirmed proteolytic cleavage at the NTB-VPg and VPg-Pro sites. In addition, we have identified two cleavage sites in the N-terminal region of P1. Site-directed mutagenesis and immunoprecipitation experiments using inserted peptide tags confirmed that the position of these cleavage sites corresponds to that of cleavage sites delineating the X1 and X2 domains in Tomato ringspot virus (subgroup C nepovirus). Amino acid alignments implied the presence of similar cleavage sites in the P1 polyprotein of other Nepoviruses. Our results suggest that the presence of two protein domains upstream of NTB is a common feature of Nepoviruses.
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Cheravirus and Sadwavirus: two unassigned genera of plant positive-sense single-stranded RNA viruses formerly considered atypical members of the genus Nepovirus (family Comoviridae)
Archives of Virology, 2007Co-Authors: O. Gall, Alexander Karasev, Joan Wellink, K Lehto, Hélène Sanfaçon, M. Ikegami, T. Iwanami, T. Jones, T. Wetzel, N. YoshikawaAbstract:The genus Nepovirus (family Comoviridae ) was known both for a good level of homogeneity and for the presence of atypical members. In particular, the atypical members of the genus differed by the number of capsid protein (CP) subunits. While typical Nepoviruses have a single CP subunit with three structural domains, atypical Nepoviruses have either three small CP subunits, probably corresponding to the three individual domains, or a large and a small subunit, probably containing two and one structural domains, respectively. These differences are corroborated by hierarchical clustering based on sequences derived from both genomic RNAs. Therefore, these atypical viruses are now classified in two distinct genera, Cheravirus (three CP subunits; type species Cherry rasp leaf virus ) and Sadwavirus (two CP subunits; type species Satsuma dwarf virus ).
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Proteolytic processing at a novel cleavage site in the N-terminal region of the tomato ringspot nepovirus RNA-1-encoded polyprotein in vitro.
Journal of General Virology, 2000Co-Authors: Aiming Wang, Hélène SanfaçonAbstract:Tomato ringspot nepovirus RNA-1-encoded polyprotein (P1) contains the domains for the putative NTP-binding protein, VPg, 3C-like protease and a putative RNA-dependent RNA polymerase in its C-terminal region. The N-terminal region of P1, with a coding capacity for a protein (or a precursor) of 67 kDa, has not been characterized. Using partial cDNA clones, it is shown that the 3C-like protease can process the N-terminal region of P1 at a novel cleavage site in vitro, allowing the release of two proteins, X1 (located at the N terminus of P1) and X2 (located immediately upstream of the NTB domain). P1 precursors in which the protease was inactive or absent were not cleaved by exogenously added protease, suggesting that P1 processing was predominantly in cis. Results from site-directed mutagenesis of putative cleavage sites suggest that dipeptides Q423/G and Q620/G are the X1-X2 and X2-NTB cleavage sites, respectively. The putative X1 protein contains a previously identified alanine-rich sequence which is present in Nepoviruses but not in the related comoviruses. The putative X2 protein contains a region with similarity to the comovirus 32 kDa protease co-factor (the only mature protein released from the N terminus of comovirus P1 polyproteins) and to the corresponding region of other nepovirus P1 polyproteins. These results raise the possibility that the presence of two distinct protein domains in the N-terminal part of the P1 polyprotein may be a common feature of Nepoviruses.
Thierry Candresse - One of the best experts on this subject based on the ideXlab platform.
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Characterization of a New Nepovirus Infecting Apricot in Southeastern France: Apricot Latent Ringspot Virus
European Journal of Plant Pathology, 2001Co-Authors: Pascal Gentit, Thierry Candresse, René-pierre Delbos, Jean DunezAbstract:A pathogen was transmitted from apricot trees showing symptoms of viral infection to GF305 peach seedlings which reacted by stunting, shortened internodes and chlorotic mottling. The agent was transmitted to cherry, apricot, peach and plum by grafting and to several herbaceous hosts by mechanical inoculation. Isometric nepovirus-like particles of 30–31 nm diameter extracted from infected Chenopodium quinoa sedimented as two peaks in sucrose gradients. These particles contained two single stranded RNAs of approximately 5.9 and 7.9 kb, and a single coat protein subunit of 53.7 kDa. No cross-reactions were observed with a number of Nepoviruses infecting fruit trees. Inoculation of purified particles to herbaceous or woody hosts reproduced the same symptoms caused by the original isolate. Sequencing of a 2.2 kbp cDNA clone covering the 3′ end of the small genomic RNA identified an open reading frame encoding a 317 aa N-truncated protein exhibiting significant similarities with the coat protein of Nepoviruses. The 1257 nt long 3′ non-coding region showed up to about 65% homology to the equivalent region of members of the subgroup C of Nepoviruses. The properties of this pathogen do not match those of any previously described nepovirus. It should therefore be considered as a new member of the subgroup C of Nepoviruses, for which the name of Apricot latent ringspot virus (ALRSV) is proposed. The nucleotide sequence reported in this work has been deposited in the EMBL databank under the accession number AJ278875.
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Characterization of a New Nepovirus Infecting Apricot in Southeastern France: Apricot Latent Ringspot Virus
European Journal of Plant Pathology, 2001Co-Authors: Pascal Gentit, Thierry Candresse, René-pierre Delbos, Jean DunezAbstract:A pathogen was transmitted from apricot trees showing symptoms of viral infection to GF305 peach seedlings which reacted by stunting, shortened internodes and chlorotic mottling. The agent was transmitted to cherry, apricot, peach and plum by grafting and to several herbaceous hosts by mechanical inoculation. Isometric nepovirus-like particles of 30–31 nm diameter extracted from infected Chenopodium quinoa sedimented as two peaks in sucrose gradients. These particles contained two single stranded RNAs of approximately 5.9 and 7.9 kb, and a single coat protein subunit of 53.7 kDa. No cross-reactions were observed with a number of Nepoviruses infecting fruit trees. Inoculation of purified particles to herbaceous or woody hosts reproduced the same symptoms caused by the original isolate. Sequencing of a 2.2 kbp cDNA clone covering the 3′ end of the small genomic RNA identified an open reading frame encoding a 317 aa N-truncated protein exhibiting significant similarities with the coat protein of Nepoviruses. The 1257 nt long 3′ non-coding region showed up to about 65% homology to the equivalent region of members of the subgroup C of Nepoviruses. The properties of this pathogen do not match those of any previously described nepovirus. It should therefore be considered as a new member of the subgroup C of Nepoviruses, for which the name of Apricot latent ringspot virus (ALRSV) is proposed. The nucleotide sequence reported in this work has been deposited in the EMBL databank under the accession number AJ278875.
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Transgenic tobaccos transformed with a gene encoding a truncated form of the coat protein of tomato black ring nepovirus are resistant to viral infection.
Plant cell reports, 1999Co-Authors: C Pacot-hiriart, O. Gall, Thierry Candresse, R. P. Delbos, Jean DunezAbstract:Tomato black ring virus (TBRV) belongs to the Nepoviruses, an important genus of phytoviruses characterized by isometric particles and by their transmission by longidorid nematodes. As for all other Nepoviruses, the coat protein (CP) of TBRV is encoded by the 3′ terminal part of the viral RNA2 (positions 2801–4334). A hybrid gene driving the expression of a truncated form of the TBRV CP was constructed. It contains a frameshift deletion at position T4065 so that in the encoded protein the last 90 amino acids of the wild-type CP are replaced by 52 amino acids encoded by a different reading frame of the viral RNA. This hybrid gene was introduced into the genome of Nicotiana tabacum cv 'Xanthi' plants. When compared to control plants, progeny of some transformants expressing the mutated CP gene (CPm+ plants) showed resistance against TBRV infection. This resistance is characterized by a delay in the appearance of symptoms, a reduction in the number of infected plants and a reduction in virus accumulation.
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An RNA-dependent-RNA-polymerase activity associated with grapevine chrome mosaic nepovirus infection
Archives of Virology, 1997Co-Authors: Olivier Gall, Thierry Candresse, Jean DunezAbstract:A virus-induced, viral RNA-specific, RNA-dependent-RNA-poly-merase activity has been observed in vitro associated with membrane extracts of plants of three different species after infection with grapevine chrome mosaic nepovirus (GCMV). The products of this activity are full-length, positive sense GCMV RNAs present in double-stranded structures. As has been demonstrated for a relative to Nepoviruses, cowpea mosaic comovirus, this activity probably corresponds to the nepoviral replication complex.
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A multiple alignment of the capsid protein sequences of Nepoviruses and comoviruses suggests a common structure
Archives of Virology, 1995Co-Authors: O. Gall, Thierry Candresse, Jean DunezAbstract:The amino acid sequences of the regions encoding the structural proteins of eleven Nepoviruses and five comoviruses, two genera of the family Comoviridae , have been aligned. The properties predicted by computer analysis (three-dimensional-3D-structure, hydrophobicity) are also correlated along this alignment, and aligned to the experimentally determined 3D structure of two comoviruses. It can thus be assumed that the 3D structure of the unique nepovirus coat protein matches that of the bipartite protomer found in the comovirus particles. In this model, the spatial locations of two amino-acid motifs characteristic of Nepoviruses are in close vicinity, at the external surface of the virion. The coat proteins of Nepoviruses and comoviruses may thus share a common evolutionary origin. A phylogenetic analysis was made using the multiple alignment, allowing a better understanding of the molecular relationships between these two groups of viruses.
John E. Johnson - One of the best experts on this subject based on the ideXlab platform.
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Structures of Picorna-Like Plant Viruses: Implications and Applications
Advances in virus research, 2003Co-Authors: Tianwei Lin, John E. JohnsonAbstract:Publisher Summary Picorna-like plant viruses that include Como and Nepo genera of the Comoviridae, share similarities in structure, genome organization, and replication strategy with mammalian picornaviruses. Structural studies of comoviruses and a nepovirus contribute to the understanding of icosahedral virus structures, the development of novel methods for investigating macromolecular assemblies, and the infrastructure for virus-based bio- and nanotechnology. It is found that bean pod mottle virus (BPMV) shares similar overall genome organization, replication strategy, and capsid structure with the type member cowpea mosaic virus (CPMV). Structural studies of BPMV provided the first observation of a portion of a viral genome in association with its capsid, and the structural comparison of a nucleoprotein particle with an empty capsid that demonstrated ordering of elements of the capsid. Red clover mottle virus (RCMV) is another member of the comovirus family that was investigated biochemically and genetically and its structure was determined for comparative studies. There are significant structural differences between comoviruses and some Nepoviruses in that the capsids of comoviruses are composed of two polypeptides whereas those of Nepoviruses are composed of a single polypeptide. The structure of a nepovirus, tobacco ringspot virus (TRSV), was determined. Structural comparison showed that TRSV was likely to be an evolutionary intermediate of development of comoviruses.
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The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily
Structure, 1998Co-Authors: Veda Chandrasekar, John E. JohnsonAbstract:BACKGROUND: Tobacco ringspot virus (TRSV) is a member of the nepovirus genus of icosahedral RNA plant viruses that cause disease in fruit crops. Nepoviruses, comoviruses and picornaviruses are classified in the picornavirus superfamily. Crystal structures of comoviruses and picornaviruses and the molecular mass of the TRSV subunit (sufficient to accommodate three beta-barrel domains) suggested that Nepoviruses may represent a link in the evolution of the picornavirus capsids from a T = 3 icosahedral virus. This evolutionary process is thought to involve triplication of the capsid protein gene, to encode a three-domain polyprotein, followed by development of cleavage sites in the interdomain linking regions. Structural studies on TRSV were initiated to determine if the TRSV subunit corresponds to the proposed uncleaved three-domain polyprotein. RESULTS: The 3.5 A resolution structure of TRSV shows that the capsid protein consists of three beta-barrel domains covalently linked by extended polypeptides. The order of connectivity of the domains in TRSV confirms the proposed connectivity for the precleaved comovirus and picornavirus capsid polyprotein. Structural differences between equivalent domains in TRSV and comoviruses are confined to the external surface loops, interdomain connecting polypeptides and N termini. The three different domains within TRSV and comoviruses are more closely related at the structural level than the three individual domains within picornaviruses. CONCLUSIONS: The structural results confirm the notion of divergent evolution of the capsid polyproteins of Nepoviruses, comoviruses and picornaviruses from a common ancestor. A number of residues were found to be conserved among various Nepoviruses, some of which stabilize the quaternary structure of the three domains in the TRSV capsid protein subunit. Two conserved regions were identified on the external surface of TRSV, however, mutational studies will be needed to understand their functional significance. Nepoviruses transmitted by the same nematode species do not share regions with similar amino acid composition on the viral surface.
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The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily
Structure (London England : 1993), 1998Co-Authors: Veda Chandrasekar, John E. JohnsonAbstract:Abstract Background: Tobacco ringspot virus (TRSV) is a member of the nepovirus genus of icosahedral RNA plant viruses that cause disease in fruit crops. Nepoviruses, comoviruses and picornaviruses are classified in the picornavirus superfamily. Crystal structures of comoviruses and picornaviruses and the molecular mass of the TRSV subunit (sufficient to accommodate three β -barrel domains) suggested that Nepoviruses may represent a link in the evolution of the picornavirus capsids from a T=3 icosahedral virus. This evolutionary process is thought to involve triplication of the capsid protein gene, to encode a three-domain polyprotein, followed by development of cleavage sites in the interdomain linking regions. Structural studies on TRSV were initiated to determine if the TRSV subunit corresponds to the proposed uncleaved three domain polyprotein. Results: The 3.5 a resolution structure of TRSV shows that the capsid protein consists of three β -barrel domains covalently linked by extended polypeptides. The order of connectivity of the domains in TRSV confirms the proposed connectivity for the precleaved comovirus and picornavirus capsid polyprotein. Structural differences between equivalent domains in TRSV and comoviruses are confined to the external surface loops, interdomain connecting polypeptides and N termini. The three different domains within TRSV and comoviruses are more closely related at the structural level than the three individual domains within picornaviruses. Conclusions: The structural results confirm the notion of divergent evolution of the capsid polyproteins of Nepoviruses, comoviruses and picornaviruses from a common ancestor. A number of residues were found to be conserved among various Nepoviruses, some of which stabilize the quaternary structure of the three domains in the TRSV capsid protein subunit. Two conserved regions were identified on the external surface of TRSV, however, mutational studies will be needed to understand their functional significance. Nepoviruses transmitted by the same nematode species do not share regions with similar amino acid composition on the viral surface.
B. Javornik - One of the best experts on this subject based on the ideXlab platform.
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Xiphinema rivesi from Slovania Transmit Tobacco ringspot virus and Tomato ringspot virus to Cucumber Bait Plants
Plant disease, 2007Co-Authors: Simon Širca, Gregor Urek, B. Gerič Stare, I. Mavrič Pleško, M. Viršček Marn, B. JavornikAbstract:The dagger nematode, Xiphinema rivesi Dalmasso, a member of the X. americanum group, was detected in 2002 for the first time in Slovenia and for the fourth time in Europe (4). X. rivesi is a vector of at least four North American Nepoviruses including Cherry rasp leaf virus (CRLV), Tobacco ringspot virus (TRSV), Tomato ringspot virus (ToRSV), and Peach rosette mosaic virus (PRMV) (1,2). All of these viruses are included on the EPPO and EU lists of quarantine organisms, but none of the Xiphinema species found in Europe have been reported to transmit these Nepoviruses. Three virus isolates, including TRSV (from Lobelia spp.; virus collection of the Plant Protection Service, Wageningen, The Netherlands), ToRSV (grapevine isolate PV-0381; DSMZ, Braunschweig, Germany), and Arabis mosaic virus (ArMV) (from Vinca spp.; virus collection of the Plant Protection Service), were used in transmission tests with a population of X. rivesi found in Slovenia. X. rivesi is not known to transmit ArMV and this virus was incl...