Abutilon Mosaic Virus

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Holger Jeske - One of the best experts on this subject based on the ideXlab platform.

  • the induction of stromule formation by a plant dna Virus in epidermal leaf tissues suggests a novel intra and intercellular macromolecular trafficking route
    Frontiers in Plant Science, 2012
    Co-Authors: Björn Krenz, Holger Jeske, Tatjana Kleinow
    Abstract:

    Stromules are dynamic thin protrusions of membrane envelope from plant cell plastids. Despite considerable progress in understanding the importance of certain cytoskeleton elements and motor proteins for stromule maintenance, their function within the cell has yet to be unraveled. Several Viruses cause a remodulation of plastid structures and stromule biogenesis within their host plants. For RNA-Viruses these interactions were demonstrated to be relevant to the infection process. An involvement of plastids and stromules is assumed in the DNA-Virus life cycle as well, but their functional role needs to be determined. Recent findings support a participation of heat shock cognate 70 kDa protein (cpHSC70-1)-containing stromules induced by a DNA-Virus infection (Abutilon Mosaic Virus, AbMV, Geminiviridae) in intra- and intercellular molecule exchange. The chaperone cpHSC70-1 was shown to interact with the AbMV movement protein (MP). Bimolecular fluorescence complementation confirmed the interaction of cpHSC70-1 and MP, and showed a homo-oligomerization of either protein in planta. The complexes were detected at the cellular margin and co-localized with plastids. In healthy plant tissues cpHSC70-1-oligomers occurred in distinct spots at chloroplasts and in small filaments extending from plastids to the cell periphery. AbMV-infection induced a cpHSC70-1-containing stromule network that exhibits elliptical dilations and transverses whole cells. Silencing of the cpHSC70-gene revealed an impact of cpHSC70 on chloroplast stability and restricted AbMV movement, but not viral DNA accumulation. Based on these data, a model is suggested in which these stromules function in molecule exchange between plastids and other organelles and perhaps other cells. AbMV may utilize cpHSC70-1 for trafficking along plastids and stromules into a neighboring cell or from plastids into the nucleus. Experimental approaches to investigate this hypothesis are discussed.

  • a plastid targeted heat shock cognate 70 kda protein interacts with the Abutilon Mosaic Virus movement protein
    Virology, 2010
    Co-Authors: Björn Krenz, Holger Jeske, Christina Wege, Volker Windeisen, Tatjana Kleinow
    Abstract:

    The movement protein (MP) of bipartite geminiViruses facilitates cell-to-cell as well as long-distance transport within plants and influences viral pathogenicity. Yeast two-hybrid assays identified a chaperone, the nuclear-encoded and plastid-targeted heat shock cognate 70kDa protein (cpHSC70-1) of Arabidopsis thaliana, as a potential binding partner for the Abutilon Mosaic Virus (AbMV) MP. In planta, bimolecular fluorescence complementation (BiFC) analysis showed cpHSC70-1/MP complexes and MP homooligomers at the cell periphery and co-localized with chloroplasts. BiFC revealed cpHSC70-1 oligomers associated with chloroplasts, but also distributed at the cellular margin and in filaments arising from plastids reminiscent of stromules. Silencing the cpHSC70 gene of Nicotiana benthamiana using an AbMV DNA A-derived gene silencing vector induced minute white leaf areas, which indicate an effect on chloroplast stability. Although AbMV DNA accumulated within chlorotic spots, a spatial restriction of these occurred, suggesting a functional relevance of the MP-chaperone interaction for viral transport and symptom induction.

  • expression dynamics and ultrastructural localization of epitope tagged Abutilon Mosaic Virus nuclear shuttle and movement proteins in nicotiana benthamiana cells
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Björn Krenz, Christina Wege, Fariha Tanwir, Cornelia Kocher, Holger Jeske
    Abstract:

    The geminiVirus Abutilon Mosaic Virus (AbMV) encodes two proteins which are essential for viral spread within plants. The nuclear shuttle protein (NSP) transfers viral DNA between the nucleus and cytoplasm, whereas the movement protein (MP) facilitates transport between cells through plasmodesmata and long-distance via phloem. An inducible overexpression system for epitope-tagged NSP and MP in plants yielded unprecedented amounts of both proteins. Western blots revealed extensive posttranslational modification and truncation for MP, but not for NSP. Ultrastructural examination of Nicotiana benthamiana tissues showed characteristic nucleopathic alterations, including fibrillar rings, when epitope-tagged NSP and MP were simultaneously expressed in leaves locally infected with an AbMV DNA A in which the coat protein gene was replaced by a green fluorescent protein encoding gene. Immunogold labelling localized NSP in the nucleoplasm and in the fibrillar rings. MP appeared at the cell periphery, probably the plasma membrane, and plasmodesmata.

  • three c terminal phosphorylation sites in the Abutilon Mosaic Virus movement protein affect symptom development and viral dna accumulation
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Fariha Tanwir, Marc Nischang, Alexander Beck, Ulrich Kratzer, Werner Preiss, Gabi Kepp, Holger Jeske
    Abstract:

    The Abutilon Mosaic Virus (AbMV, Geminiviridae) DNA B component encodes a movement protein (MP), which facilitates viral transport within plants and affects pathogenicity. The presence of phosphorylated serine and threonine residues was confirmed for MP expressed in yeast and Nicotiana benthamiana by comparative Western blot analysis using phospho-amino acid- and MP-specific immunodetection. Mass spectrometry of yeast-derived MP identified three phosphorylation sites located in the C-terminal domain (Thr-221, Ser-223 and Ser-250). To assess their functional relevance in plants, several point mutations were generated in the MP gene of DNA B, which replace Thr-221, Ser-223 and Ser-250, either singly or in combinations, with either an uncharged alanine or a phosphorylation-mimicking aspartate residue. When co-inoculated with DNA A, all mutants were infectious. In systemically infected plants the symptoms and/or viral DNA accumulation were significantly altered for several of the mutants.

  • Interaction of DNA with the movement proteins of geminiViruses revisited.
    Journal of virology, 2004
    Co-Authors: Stefan Hehnle, Christina Wege, Holger Jeske
    Abstract:

    GeminiViruses manage the transport of their DNA within plants with the help of three proteins, the coat protein (CP), the nuclear shuttle protein (NSP), and the movement protein (MP). The DNA-binding capabilities of CP, NSP, and MP of Abutilon Mosaic Virus (AbMV; family Geminiviridae; genus BegomoVirus) were scrutinized using gel mobility shift assays and electron microscopy. CP and NSP revealed a sequence-independent affinity for both double-stranded and single-stranded DNA, as has been previously reported for other begomoViruses. MP interacted selectively with dimeric supercoiled plasmid DNA in the electrophoretic assay. Further apparent size- and form-selective binding capacities of MP have been previously reported for another geminiVirus (Bean dwarf Mosaic Virus), but in the case of AbMV, they have been identified as the result of electrophoretic interference rather than of complex formation. Without these complications, electron microscopy confirmed the assembly of double-stranded supercoiled DNA with NSP and MP into conspicuous structures and provided the first direct evidence for cooperative interaction of MP, NSP, and DNA. Based on these results and previous ones, a transport model of geminiViruses is discussed in which NSP packages DNA and MP anchors this complex to the protoplasmic leaflets of plasma membranes and microsomes for cell-to-cell movement.

Christina Wege - One of the best experts on this subject based on the ideXlab platform.

  • a plastid targeted heat shock cognate 70 kda protein interacts with the Abutilon Mosaic Virus movement protein
    Virology, 2010
    Co-Authors: Björn Krenz, Holger Jeske, Christina Wege, Volker Windeisen, Tatjana Kleinow
    Abstract:

    The movement protein (MP) of bipartite geminiViruses facilitates cell-to-cell as well as long-distance transport within plants and influences viral pathogenicity. Yeast two-hybrid assays identified a chaperone, the nuclear-encoded and plastid-targeted heat shock cognate 70kDa protein (cpHSC70-1) of Arabidopsis thaliana, as a potential binding partner for the Abutilon Mosaic Virus (AbMV) MP. In planta, bimolecular fluorescence complementation (BiFC) analysis showed cpHSC70-1/MP complexes and MP homooligomers at the cell periphery and co-localized with chloroplasts. BiFC revealed cpHSC70-1 oligomers associated with chloroplasts, but also distributed at the cellular margin and in filaments arising from plastids reminiscent of stromules. Silencing the cpHSC70 gene of Nicotiana benthamiana using an AbMV DNA A-derived gene silencing vector induced minute white leaf areas, which indicate an effect on chloroplast stability. Although AbMV DNA accumulated within chlorotic spots, a spatial restriction of these occurred, suggesting a functional relevance of the MP-chaperone interaction for viral transport and symptom induction.

  • expression dynamics and ultrastructural localization of epitope tagged Abutilon Mosaic Virus nuclear shuttle and movement proteins in nicotiana benthamiana cells
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Björn Krenz, Christina Wege, Fariha Tanwir, Cornelia Kocher, Holger Jeske
    Abstract:

    The geminiVirus Abutilon Mosaic Virus (AbMV) encodes two proteins which are essential for viral spread within plants. The nuclear shuttle protein (NSP) transfers viral DNA between the nucleus and cytoplasm, whereas the movement protein (MP) facilitates transport between cells through plasmodesmata and long-distance via phloem. An inducible overexpression system for epitope-tagged NSP and MP in plants yielded unprecedented amounts of both proteins. Western blots revealed extensive posttranslational modification and truncation for MP, but not for NSP. Ultrastructural examination of Nicotiana benthamiana tissues showed characteristic nucleopathic alterations, including fibrillar rings, when epitope-tagged NSP and MP were simultaneously expressed in leaves locally infected with an AbMV DNA A in which the coat protein gene was replaced by a green fluorescent protein encoding gene. Immunogold labelling localized NSP in the nucleoplasm and in the fibrillar rings. MP appeared at the cell periphery, probably the plasma membrane, and plasmodesmata.

  • Abutilon Mosaic Virus DNA B component supports mechanical Virus transmission, but does not counteract begomoviral phloem limitation in transgenic plants.
    Virology, 2007
    Co-Authors: Christina Wege, Diana Pohl
    Abstract:

    Different Nicotiana benthamiana lines stably transformed with Abutilon Mosaic Virus (AbMV) dimeric DNA B were capable of systemically spreading complete bipartite AbMV genomes, following agroinoculation of DNA A alone. Constitutively expressed viral movement protein (BC1) did not induce any persistent disease phenotype, but plants developed transient morphological abnormalities such as radially symmetric leaves after kanamycin withdrawal. Systemic AbMV infection produced symptoms and Virus titers indistinguishable from those in non-transgenic plants. In systemically invaded leaves, the begomoVirus remained phloem-limited, whereas the plants' susceptibility to mechanical transmission of AbMV was enhanced by a factor of three to five, as compared to non-transgenic controls. Hence, DNA B-encoded movement functions can complement local movement to the phloem after mechanical transmission, but fail to support viral invasion of non-phloem cells in systemically infected organs, indicating that the phloem restriction of AbMV does not result predominantly from a lack of transport competence in mesophyll tissues.

  • synergism of a dna and an rna Virus enhanced tissue infiltration of the begomoVirus Abutilon Mosaic Virus abmv mediated by cucumber Mosaic Virus cmv
    Virology, 2007
    Co-Authors: Christina Wege, Daniela Siegmund
    Abstract:

    Replication of the begomoVirus Abutilon Mosaic Virus (AbMV) is restricted to phloem nuclei, generating moderate levels of Virus DNA. Co-infection with Cucumber Mosaic Virus (CMV) evidently increased AbMV titers in Nicotiana benthamiana, tobacco, and tomato, resulting in synergistic symptom enhancement. In situ hybridization revealed that in double-infected leaves an increased number of nuclei contained elevated amounts of AbMV. Additionally, the begomoviral phloem-limitation was broken. Whereas CMV 3a movement protein-expressing tobacco plants did not exert any similar influence, the presence of CMV 2b silencing suppressor protein lead to enhanced AbMV titers and numbers of infected vascular cells. The findings prove that AbMV can replicate in nonvascular cells and represent the first report on a true synergism of an RNA/ssDNA Virus combination in plants, in which CMV 2b protein plays a role. They indicate considerable consequences of mixed infections between begomo- and cucumoViruses on Virus epidemiology and agriculture.

  • Interaction of DNA with the movement proteins of geminiViruses revisited.
    Journal of virology, 2004
    Co-Authors: Stefan Hehnle, Christina Wege, Holger Jeske
    Abstract:

    GeminiViruses manage the transport of their DNA within plants with the help of three proteins, the coat protein (CP), the nuclear shuttle protein (NSP), and the movement protein (MP). The DNA-binding capabilities of CP, NSP, and MP of Abutilon Mosaic Virus (AbMV; family Geminiviridae; genus BegomoVirus) were scrutinized using gel mobility shift assays and electron microscopy. CP and NSP revealed a sequence-independent affinity for both double-stranded and single-stranded DNA, as has been previously reported for other begomoViruses. MP interacted selectively with dimeric supercoiled plasmid DNA in the electrophoretic assay. Further apparent size- and form-selective binding capacities of MP have been previously reported for another geminiVirus (Bean dwarf Mosaic Virus), but in the case of AbMV, they have been identified as the result of electrophoretic interference rather than of complex formation. Without these complications, electron microscopy confirmed the assembly of double-stranded supercoiled DNA with NSP and MP into conspicuous structures and provided the first direct evidence for cooperative interaction of MP, NSP, and DNA. Based on these results and previous ones, a transport model of geminiViruses is discussed in which NSP packages DNA and MP anchors this complex to the protoplasmic leaflets of plasma membranes and microsomes for cell-to-cell movement.

Tatjana Kleinow - One of the best experts on this subject based on the ideXlab platform.

  • the induction of stromule formation by a plant dna Virus in epidermal leaf tissues suggests a novel intra and intercellular macromolecular trafficking route
    Frontiers in Plant Science, 2012
    Co-Authors: Björn Krenz, Holger Jeske, Tatjana Kleinow
    Abstract:

    Stromules are dynamic thin protrusions of membrane envelope from plant cell plastids. Despite considerable progress in understanding the importance of certain cytoskeleton elements and motor proteins for stromule maintenance, their function within the cell has yet to be unraveled. Several Viruses cause a remodulation of plastid structures and stromule biogenesis within their host plants. For RNA-Viruses these interactions were demonstrated to be relevant to the infection process. An involvement of plastids and stromules is assumed in the DNA-Virus life cycle as well, but their functional role needs to be determined. Recent findings support a participation of heat shock cognate 70 kDa protein (cpHSC70-1)-containing stromules induced by a DNA-Virus infection (Abutilon Mosaic Virus, AbMV, Geminiviridae) in intra- and intercellular molecule exchange. The chaperone cpHSC70-1 was shown to interact with the AbMV movement protein (MP). Bimolecular fluorescence complementation confirmed the interaction of cpHSC70-1 and MP, and showed a homo-oligomerization of either protein in planta. The complexes were detected at the cellular margin and co-localized with plastids. In healthy plant tissues cpHSC70-1-oligomers occurred in distinct spots at chloroplasts and in small filaments extending from plastids to the cell periphery. AbMV-infection induced a cpHSC70-1-containing stromule network that exhibits elliptical dilations and transverses whole cells. Silencing of the cpHSC70-gene revealed an impact of cpHSC70 on chloroplast stability and restricted AbMV movement, but not viral DNA accumulation. Based on these data, a model is suggested in which these stromules function in molecule exchange between plastids and other organelles and perhaps other cells. AbMV may utilize cpHSC70-1 for trafficking along plastids and stromules into a neighboring cell or from plastids into the nucleus. Experimental approaches to investigate this hypothesis are discussed.

  • a plastid targeted heat shock cognate 70 kda protein interacts with the Abutilon Mosaic Virus movement protein
    Virology, 2010
    Co-Authors: Björn Krenz, Holger Jeske, Christina Wege, Volker Windeisen, Tatjana Kleinow
    Abstract:

    The movement protein (MP) of bipartite geminiViruses facilitates cell-to-cell as well as long-distance transport within plants and influences viral pathogenicity. Yeast two-hybrid assays identified a chaperone, the nuclear-encoded and plastid-targeted heat shock cognate 70kDa protein (cpHSC70-1) of Arabidopsis thaliana, as a potential binding partner for the Abutilon Mosaic Virus (AbMV) MP. In planta, bimolecular fluorescence complementation (BiFC) analysis showed cpHSC70-1/MP complexes and MP homooligomers at the cell periphery and co-localized with chloroplasts. BiFC revealed cpHSC70-1 oligomers associated with chloroplasts, but also distributed at the cellular margin and in filaments arising from plastids reminiscent of stromules. Silencing the cpHSC70 gene of Nicotiana benthamiana using an AbMV DNA A-derived gene silencing vector induced minute white leaf areas, which indicate an effect on chloroplast stability. Although AbMV DNA accumulated within chlorotic spots, a spatial restriction of these occurred, suggesting a functional relevance of the MP-chaperone interaction for viral transport and symptom induction.

  • expression dynamics and ultrastructural localization of epitope tagged Abutilon Mosaic Virus nuclear shuttle and movement proteins in nicotiana benthamiana cells
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Björn Krenz, Christina Wege, Fariha Tanwir, Cornelia Kocher, Holger Jeske
    Abstract:

    The geminiVirus Abutilon Mosaic Virus (AbMV) encodes two proteins which are essential for viral spread within plants. The nuclear shuttle protein (NSP) transfers viral DNA between the nucleus and cytoplasm, whereas the movement protein (MP) facilitates transport between cells through plasmodesmata and long-distance via phloem. An inducible overexpression system for epitope-tagged NSP and MP in plants yielded unprecedented amounts of both proteins. Western blots revealed extensive posttranslational modification and truncation for MP, but not for NSP. Ultrastructural examination of Nicotiana benthamiana tissues showed characteristic nucleopathic alterations, including fibrillar rings, when epitope-tagged NSP and MP were simultaneously expressed in leaves locally infected with an AbMV DNA A in which the coat protein gene was replaced by a green fluorescent protein encoding gene. Immunogold labelling localized NSP in the nucleoplasm and in the fibrillar rings. MP appeared at the cell periphery, probably the plasma membrane, and plasmodesmata.

  • three c terminal phosphorylation sites in the Abutilon Mosaic Virus movement protein affect symptom development and viral dna accumulation
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Fariha Tanwir, Marc Nischang, Alexander Beck, Ulrich Kratzer, Werner Preiss, Gabi Kepp, Holger Jeske
    Abstract:

    The Abutilon Mosaic Virus (AbMV, Geminiviridae) DNA B component encodes a movement protein (MP), which facilitates viral transport within plants and affects pathogenicity. The presence of phosphorylated serine and threonine residues was confirmed for MP expressed in yeast and Nicotiana benthamiana by comparative Western blot analysis using phospho-amino acid- and MP-specific immunodetection. Mass spectrometry of yeast-derived MP identified three phosphorylation sites located in the C-terminal domain (Thr-221, Ser-223 and Ser-250). To assess their functional relevance in plants, several point mutations were generated in the MP gene of DNA B, which replace Thr-221, Ser-223 and Ser-250, either singly or in combinations, with either an uncharged alanine or a phosphorylation-mimicking aspartate residue. When co-inoculated with DNA A, all mutants were infectious. In systemically infected plants the symptoms and/or viral DNA accumulation were significantly altered for several of the mutants.

Björn Krenz - One of the best experts on this subject based on the ideXlab platform.

  • The stress granule component G3BP is a novel interaction partner for the nuclear shuttle proteins of the nanoVirus pea necrotic yellow dwarf Virus and geminiVirus Abutilon Mosaic Virus
    Virus research, 2016
    Co-Authors: Susanna Krapp, Eva Greiner, Bushra Amin, Uwe Sonnewald, Björn Krenz
    Abstract:

    Stress granules (SGs) are structures within cells that regulate gene expression during stress response, e.g. viral infection. In mammalian cells assembly of SGs is dependent on the Ras-GAP SH3-domain-binding protein (G3BP). The C-terminal domain of the viral nonstructural protein 3 (nsP3) of Semliki Forest Virus (SFV) forms a complex with mammalian G3BP and sequesters it into viral RNA replication complexes in a manner that inhibits the formation of SGs. The binding domain of nsP3 to HsG3BP was mapped to two tandem 'FGDF' repeat motifs close to the C-terminus of the viral proteins. It was speculated that plant Viruses employ a similar strategy to inhibit SG function. This study identifies an Arabidopsis thaliana NTF2-RRM domain-containing protein as a G3BP-like protein (AtG3BP), which localizes to plant SGs. Moreover, the nuclear shuttle protein (NSP) of the begomoVirus Abutilon Mosaic Virus (AbMV), which harbors a 'FVSF'-motif at its C-terminal end, interacts with the AtG3BP-like protein, as does the 'FNGSF'-motif containing NSP of pea necrotic yellow dwarf Virus (PNYDV), a member of the Nanoviridae family. We therefore propose that SG formation upon stress is conserved between mammalian and plant cells and that plant Viruses may follow a similar strategy to inhibit plant SG function as it has been shown for their mammalian counterparts.

  • the induction of stromule formation by a plant dna Virus in epidermal leaf tissues suggests a novel intra and intercellular macromolecular trafficking route
    Frontiers in Plant Science, 2012
    Co-Authors: Björn Krenz, Holger Jeske, Tatjana Kleinow
    Abstract:

    Stromules are dynamic thin protrusions of membrane envelope from plant cell plastids. Despite considerable progress in understanding the importance of certain cytoskeleton elements and motor proteins for stromule maintenance, their function within the cell has yet to be unraveled. Several Viruses cause a remodulation of plastid structures and stromule biogenesis within their host plants. For RNA-Viruses these interactions were demonstrated to be relevant to the infection process. An involvement of plastids and stromules is assumed in the DNA-Virus life cycle as well, but their functional role needs to be determined. Recent findings support a participation of heat shock cognate 70 kDa protein (cpHSC70-1)-containing stromules induced by a DNA-Virus infection (Abutilon Mosaic Virus, AbMV, Geminiviridae) in intra- and intercellular molecule exchange. The chaperone cpHSC70-1 was shown to interact with the AbMV movement protein (MP). Bimolecular fluorescence complementation confirmed the interaction of cpHSC70-1 and MP, and showed a homo-oligomerization of either protein in planta. The complexes were detected at the cellular margin and co-localized with plastids. In healthy plant tissues cpHSC70-1-oligomers occurred in distinct spots at chloroplasts and in small filaments extending from plastids to the cell periphery. AbMV-infection induced a cpHSC70-1-containing stromule network that exhibits elliptical dilations and transverses whole cells. Silencing of the cpHSC70-gene revealed an impact of cpHSC70 on chloroplast stability and restricted AbMV movement, but not viral DNA accumulation. Based on these data, a model is suggested in which these stromules function in molecule exchange between plastids and other organelles and perhaps other cells. AbMV may utilize cpHSC70-1 for trafficking along plastids and stromules into a neighboring cell or from plastids into the nucleus. Experimental approaches to investigate this hypothesis are discussed.

  • a plastid targeted heat shock cognate 70 kda protein interacts with the Abutilon Mosaic Virus movement protein
    Virology, 2010
    Co-Authors: Björn Krenz, Holger Jeske, Christina Wege, Volker Windeisen, Tatjana Kleinow
    Abstract:

    The movement protein (MP) of bipartite geminiViruses facilitates cell-to-cell as well as long-distance transport within plants and influences viral pathogenicity. Yeast two-hybrid assays identified a chaperone, the nuclear-encoded and plastid-targeted heat shock cognate 70kDa protein (cpHSC70-1) of Arabidopsis thaliana, as a potential binding partner for the Abutilon Mosaic Virus (AbMV) MP. In planta, bimolecular fluorescence complementation (BiFC) analysis showed cpHSC70-1/MP complexes and MP homooligomers at the cell periphery and co-localized with chloroplasts. BiFC revealed cpHSC70-1 oligomers associated with chloroplasts, but also distributed at the cellular margin and in filaments arising from plastids reminiscent of stromules. Silencing the cpHSC70 gene of Nicotiana benthamiana using an AbMV DNA A-derived gene silencing vector induced minute white leaf areas, which indicate an effect on chloroplast stability. Although AbMV DNA accumulated within chlorotic spots, a spatial restriction of these occurred, suggesting a functional relevance of the MP-chaperone interaction for viral transport and symptom induction.

  • expression dynamics and ultrastructural localization of epitope tagged Abutilon Mosaic Virus nuclear shuttle and movement proteins in nicotiana benthamiana cells
    Virology, 2009
    Co-Authors: Tatjana Kleinow, Björn Krenz, Christina Wege, Fariha Tanwir, Cornelia Kocher, Holger Jeske
    Abstract:

    The geminiVirus Abutilon Mosaic Virus (AbMV) encodes two proteins which are essential for viral spread within plants. The nuclear shuttle protein (NSP) transfers viral DNA between the nucleus and cytoplasm, whereas the movement protein (MP) facilitates transport between cells through plasmodesmata and long-distance via phloem. An inducible overexpression system for epitope-tagged NSP and MP in plants yielded unprecedented amounts of both proteins. Western blots revealed extensive posttranslational modification and truncation for MP, but not for NSP. Ultrastructural examination of Nicotiana benthamiana tissues showed characteristic nucleopathic alterations, including fibrillar rings, when epitope-tagged NSP and MP were simultaneously expressed in leaves locally infected with an AbMV DNA A in which the coat protein gene was replaced by a green fluorescent protein encoding gene. Immunogold labelling localized NSP in the nucleoplasm and in the fibrillar rings. MP appeared at the cell periphery, probably the plasma membrane, and plasmodesmata.

Thomas Frischmuth - One of the best experts on this subject based on the ideXlab platform.

  • sida micrantha Mosaic is associated with a complex infection of begomoViruses different from Abutilon Mosaic Virus
    Archives of Virology, 2004
    Co-Authors: Juan Jovel, Thomas Frischmuth, G Reski, Dirk Rothenstein, Margit Ringel, Holger Jeske
    Abstract:

    We report on the nucleotide sequences of geminiViruses of the genus BemogoVirus infecting Sida micrantha Schr., a common weed in Brazil. For decades, the Mosaic frequently associated with Sida plants was considered to be caused by a Brazilian strain of Abutilon Mosaic Virus (AbMV). By infection studies and sequence comparisons, we demonstrate that it is associated with a complex of at least two begomoViruses as different from AbMV as most South American geminiViruses. Two molecules of DNA A (A1, A2) and three of DNA B (B1, B2, B3) were cloned and sequenced. According to the high homology in their common regions, DNA A1 and DNA B3, as well as DNA A2 and DNA B2, are cognate components of two begomoViruses, which were infectious in Nicotiana benthamiana plants. No trans-replication was found for any other A/B combination. The intergenic region of DNA B2 appears to be the product of the recombination between DNA B1 and DNA A2. These results show that a coinfection of begomoViruses can persist over decades, producing a reservoir of partially recombined but distinct geminiViruses.

  • exchange of three amino acids in the coat protein results in efficient whitefly transmission of a nontransmissible Abutilon Mosaic Virus isolate
    Virology, 2001
    Co-Authors: Martin Hohnle, Petra Hofer, Ian D Bedford, Rob W Briddon, P G Markham, Thomas Frischmuth
    Abstract:

    GeminiViruses are transmitted in a circulative manner by whiteflies, leafhoppers, or treehoppers. The whitefly species Bemisia tabaci (Genn.) is the vector for members of the genus BegomoVirus. The closely related bipartite Central American begomoViruses Abutilon Mosaic Virus (AbMV), Sida golden Mosaic Virus originating from Costa Rica (SiGMV-CR), and Sida golden Mosaic Virus originating from Honduras (SiGMV-Hoyv) were used to study transmission by their insect vector. The AbMV isolate is defective in transmission, whereas the two Sida-infecting Viruses are readily transmitted by B. tabaci. These three Viruses are able to form pseudorecombinant Viruses by exchange of genomic components. The pseudorecombinant Virus SiGMV-Hoyv A/AbMV B was transmissible, whereas the reciprocal pseudorecombinant Virus AbMV A/SiGMV-Hoyv B was not transmitted, indicating that DNA B is not involved in the transmission defect. However, the uptake of the pseudorecombinant Virus AbMV A/SiGMV-Hoyv B was much better than AbMV itself, indicating that DNA B or DNA B gene products enhance uptake of viral DNA. Exchange of AbMV coat protein with that of SiGMV-CR resulted in a transmissible chimeric AbMV. Mutagenesis of the AbMV coat protein showed that the exchange of two amino acids, at positions 124 and 149, was sufficient to obtain a whitefly-transmissible AbMV mutant. However, when amino acid 174 was altered in addition to amino acids 124 and 149 AbMV was readily transmitted by B. tabaci. From this we conclude that it is not a concise motif, such as the amino acid triplet, aspartate-alanine-glycine (DAG), involved in aphid transmission of potyViruses, that determines transmissibility of begomoViruses by B. tabaci. Instead it is the composition of the coat protein domain from amino acid 123 to 149, as a minimal transmission domain, with the contribution of amino acids 149 to 174 for efficient transmission.

  • fulfilling koch s postulates for Abutilon Mosaic Virus
    Archives of Virology, 2000
    Co-Authors: Christina Wege, R D Gotthardt, Thomas Frischmuth, Holger Jeske
    Abstract:

    Cloned Abutilon Mosaic geminiVirus (AbMV) has been re-transmitted to Abutilon sellovianum (syn. striatum) plants by a two-step combined agroinfection/grafting method. The symptoms induced were indistinguishable from the characteristic Mosaic of ornamental Abutilon plants. Therefore, we can exclude that a mixture of different AbMV variants is responsible for the striking variety of Abutilon leaf pattern elements. Analysis of the symptoms on consecutively infected leaves suggests that Mosaic formation depends on routing and timing of super-imposed Virus waves.