The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform

Michal Przydacz - One of the best experts on this subject based on the ideXlab platform.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • The fungal ribonuclease-like effector Protein CSEP0064/BEC1054 represses plant immunity and interferes with degradation of host ribosomal RNA.
    Public Library of Science (PLoS), 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz, Tolga Bozkurt
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus

Rhian Jones - One of the best experts on this subject based on the ideXlab platform.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • The fungal ribonuclease-like effector Protein CSEP0064/BEC1054 represses plant immunity and interferes with degradation of host ribosomal RNA.
    Public Library of Science (PLoS), 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz, Tolga Bozkurt
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus

Helen G Pennington - One of the best experts on this subject based on the ideXlab platform.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • the fungal ribonuclease like effector Protein csep0064 bec1054 represses plant immunity and interferes with degradation of host ribosomal rna
    PLOS Pathogens, 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus.

  • The fungal ribonuclease-like effector Protein CSEP0064/BEC1054 represses plant immunity and interferes with degradation of host ribosomal RNA.
    Public Library of Science (PLoS), 2019
    Co-Authors: Helen G Pennington, Rhian Jones, Seomun Kwon, Giulia Bonciani, Hannah Thieron, Thomas Chandler, Peggy Luong, Sian Natasha Morgan, Michal Przydacz, Tolga Bozkurt
    Abstract:

    The biotrophic fungal pathogen Blumeria graminis causes the powdery mildew disease of cereals and grasses. We present the first crystal structure of a B. graminis effector of pathogenicity (CSEP0064/BEC1054), demonstrating it has a ribonuclease (RNase)-like fold. This effector is part of a group of RNase-like Proteins (termed RALPHs) which comprise the largest set of secreted effector candidates within the B. graminis genomes. Their exceptional abundance suggests they play crucial functions during pathogenesis. We show that transgenic expression of RALPH CSEP0064/BEC1054 increases susceptibility to infection in both monocotyledonous and dicotyledonous plants. CSEP0064/BEC1054 interacts in planta with the Pathogenesis-Related Protein PR10. The effector Protein associates with total RNA and weakly with DNA. Methyl jasmonate (MeJA) levels modulate susceptibility to aniline-induced host RNA fragmentation. In planta expression of CSEP0064/BEC1054 reduces the formation of this RNA fragment. We propose CSEP0064/BEC1054 is a pseudoenzyme that binds to host ribosomes, thereby inhibiting the action of plant ribosome-inactivating Proteins (RIPs) that would otherwise lead to host cell death, an unviable interaction and demise of the fungus

Ralph L. Nicholson - One of the best experts on this subject based on the ideXlab platform.

  • cdna cloning of a sorghum pathogenesis related Protein pr 10 and differential expression of defense related genes following inoculation with cochliobolus heterostrophus or colletotrichum sublineolum
    Molecular Plant-microbe Interactions, 1999
    Co-Authors: John Hipskind, Ralph L. Nicholson
    Abstract:

    A sorghum cDNA clone was isolated by differential screening of a cDNA library prepared from mesocotyls (cultivar DK18) inoculated with fungal pathogenes. The deduced translation product shows sequence similarity to a family of intracellular Pathogenesis-Related Proteins (PR-10) with a potential ribonuclease function. We studied the accumulation of PR-10 and chalcone synthase (CHS) transcripts in mesocotyls following inoculation with Cochliobolus heterostrophus or Colletotrichum sublineolum. CHS is involved in phytoalexin synthesis in sorghum. Coordinate expression of PR-10 and CHS genes was localized in the area of inoculation along with the accumulation of phytoalexins. C. heterostrophus is a nonpathogen of sorghum and cytological studies indicated that cultivar DK18 is resistant to C. sublineolum, a sorghum pathogen. We demonstrated that the two fungi triggered different time courses of plant defense reactions. Inoculation with C. heterostrophus resulted in rapid accumulation of PR-10 and CHS transcripts after appressoria had become mature. Accumulation of these transcripts was delayed in plants inoculated with C. sublineolum until penetration of host tissue had been completed and infection vesicles had formed. Results suggest that different recognition events are involved in the expression of resistance to the two fungi used or that C. sublineolum suppresses the nonspecific induction of defense responses.

  • cdna cloning of a sorghum pathogenesis related Protein pr 10 and differential expression of defense related genes following inoculation with cochliobolus heterostrophus or colletotrichum sublineolum
    Molecular Plant-microbe Interactions, 1999
    Co-Authors: Szechung Clive Lo, John Hipskind, Ralph L. Nicholson
    Abstract:

    A sorghum cDNA clone was isolated by differential screening of a cDNA library prepared from mesocotyls (cultivar DK18) inoculated with fungal pathogens. The deduced translation product shows sequence similarity to a family of intracellular Pathogenesis-Related Proteins (PR-10) with a potential ribonuclease function. We studied the accumulation of PR-10 and chalcone synthase (CHS) transcripts in mesocotyls following inoculation with Cochliobolus heterostrophus or Colletotrichum sublineolum. CHS is involved in phytoalexin synthesis in sorghum. Coordinate expression of PR-10 and CHS genes was localized in the area of inoculation along with the accumulation of phytoalexins. C. heterostrophus is a nonpathogen of sorghum and cytological studies indicated that cultivar DK18 is resistant to C. sublineolum, a sorghum pathogen. We demonstrated that the two fungi triggered different time courses of plant defense reactions. Inoculation with C. heterostrophus resulted in rapid accumulation of PR-10 and CHS transcripts...

  • Accumulation of 3-deoxyanthocyanidin phytoalexins and resistance to Colletotrichum sublineolum in sorghum
    Physiological and Molecular Plant Pathology, 1999
    Co-Authors: Katarina De Verdier, Ralph L. Nicholson
    Abstract:

    Abstract 3-Deoxyanthocyanidins are the principal phytoalexins that accumulate in sorghum in response to fungal infection. Two cultivars which differed in their reaction to Colletotrichum sublineolum , the pathogen causing the anthracnose disease in sorghum, were examined for their phytoalexin response and expression of defense-related genes. In the incompatible interaction, fungal development in the host was contained during early stages of pathogenesis. When compared to the susceptible cultivar, defense responses in the resistant cultivar were characterized by a greater and faster accumulation of phytoalexins and an earlier induction of defense-related genes encoding chalcone synthase and Pathogenesis-Related Protein PR-10. In the compatible interaction, the pathogen was able to colonize the host with the proliferation of primary and secondary hyphae. In addition to the quantitative and timing differences, there were qualitative differences between the cultivars in their phytoalexin response. Thus, the resistant cultivar accumulated a complex phytoalexin mixture, including luteolinidin and 5-methoxyluteolinidin, neither of which was produced by the susceptible cultivar following fungal inoculation. These compounds were shown previously to exhibit higher fungitoxicity than other phytoalexin components in sorghum. Our results demonstrate that 3-deoxyanthocyanidin phytoalexins represent major components of resistance to C. sublineolum in sorghum.

John P Carr - One of the best experts on this subject based on the ideXlab platform.

  • chemically induced virus resistance in arabidopsis thaliana is independent of pathogenesis related Protein expression and the npr1 gene
    Molecular Plant-microbe Interactions, 2002
    Co-Authors: Chui E Wong, Rachael A J Carson, John P Carr
    Abstract:

    Salicylic acid (SA) treatment triggers inhibition of replication or movement of several positive-sense RNA plant viruses in tobacco. This resistance can also be stimulated by nonlethal concentrations of cyanide and antimycin A (AA) without triggering induction of Pathogenesis-Related PR-1 Protein genes. In two ecotypes of Arabidopsis thaliana (Columbia and Nossen), SA-induced resistance to a tobamovirus, Turnip vein clearing virus (TVCV), was also induced by nonlethal concentrations of cyanide and AA without concomitant induction of PR-1 gene expression. Furthermore, chemically induced resistance to TVCV, as well as the induction of the plant mitochondrial alternative oxidase (a potential target for the chemicals), was independent of NPR1, a gene that plays a key role downstream of SA in the induction of PR Proteins. The chemically induced resistance to TVCV appeared to be due to inhibition of replication at the site of inoculation. Taken together, these results show that in Arabidopsis, as in tobacco, resistance to viruses can be induced via a distinct branch of the defensive signal transduction pathway. This suggests that the existence of this virus-specific branch may be widespread among plants.

  • salicylic acid interferes with tobacco mosaic virus replication via a novel salicylhydroxamic acid sensitive mechanism
    The Plant Cell, 1997
    Co-Authors: Stephen Chivasa, Alex M Murphy, M Naylor, John P Carr
    Abstract:

    Salicylic acid (SA) induces resistance to all plant pathogens, including bacteria, fungi, and viruses, but the mechanism by which SA engenders resistance to viruses is not known. Pretreatment of tobacco mosaic virus (TMV)-susceptible (nn genotype) tobacco tissue with SA reduced the levels of viral RNAs and viral coat Protein accumulating after inoculation with TMV. Viral RNAs were not affected equally, suggesting that SA treatment interferes with TMV replication. Salicylhydroxamic acid (SHAM), an inhibitor of the mitochondrial alternative oxidase, antagonized both SA-induced resistance to TMV in nn genotype plants and SA-induced acquired resistance in resistant (NN genotype) tobacco. SHAM did not inhibit induction of the PR-1 Pathogenesis-Related Protein or induction of resistance to Erwinia carotovora or Botrytis cinerea by SA. This indicates that SA induces resistance to TMV via a novel SHAM-sensitive signal transduction pathway (potentially involving alternative oxidase), which is distinct from that leading to resistance to bacteria and fungi.