Partial Proteome of the Corynetoxin‐Producing Gram‐Positive Bacterium, <i>Rathayibacter toxicus</i>

Fennessey, Christine M.; McMahon, Michael B.; Sechler, A.; Kaiser, Jaclyn A.; Garrett, Wesley M.; Tancos, Matthew A.; Luster, Douglas G.; Rogers, Elizabeth E.; Schneider, William L.

doi:10.1002/pmic.201700350

Cited by 2 publications

(2 citation statements)

References 16 publications

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“…Antigen targets were identified from a previously published R. toxicus proteome study (Fennessey et al, 2018). Output from the study was searched in the SCAFFOLD software package (Proteome Software, Inc.) for hypothetical proteins containing a minimum of 5 unique peptides in their amino acid sequences.…”

Section: Identification Of Antigen Targetsmentioning

confidence: 99%

“…In a previous study, we applied LC/MSMS to R. toxicus cell extracts to identify, catalogue and categorize proteins (Fennessey et al, 2018) using an annotated R. toxicus genome (Sechler et al, 2017; NCBI BioProject PRJNA312185) as a database. In this study, we used the resulting proteome to focus on the subset of secreted proteins, searching for proteins with characteristics suitable for antibody production and diagnostic immunoassay development.…”

Section: Candidate Protein Antigen Selectionmentioning

confidence: 99%

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Immunoreagents for development of a diagnostic assay specific for Rathayibacter toxicus

Luster

McMahon

Carter

et al. 2020

Food and Agricultural Immunology

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Rathayibacter toxicus is Gram-positive bacterium causing gummosis of forage grasses, and it produces a corynetoxin responsible for livestock poisonings in Australia. R. toxicus is a USDA APHIS-listed Select Agent, threatening seed and livestock production areas in the U.S. We therefore are developing diagnostic assays to prepare for the introduction of the pathogen into the U.S. Using proteomic data, we identified proteins expressed in R. toxicus but not in other Rathayibacter spp. Recombinant proteins corresponding to extracellular domains of candidate proteins were used to raise polyclonal and monoclonal antibodies. Antibodies were evaluated for sensitivity and specificity in immunoassays against a panel of Rathayibacter spp. and near-neighbours. Polyclonal and monoclonal antibodies exhibited high sensitivity and specificity for R. toxicus in assays with cultured bacteria. The highest-performing immunoreagents were identified for further testing with field samples collected in Australia and for eventual development of an immunoassay for bacterial detection in grass samples.

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Section: Identification Of Antigen Targetsmentioning

confidence: 99%

Section: Candidate Protein Antigen Selectionmentioning

confidence: 99%

Immunoreagents for development of a diagnostic assay specific for Rathayibacter toxicus

Luster

McMahon

Carter

et al. 2020

Food and Agricultural Immunology

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Comparative Secretome Analyses of Toxigenic and AtoxigenicRathayibacterSpecies

et al. 2021

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Phytopathogenic Rathayibacter species are unique bacterial plant pathogens as they are obligately vectored by plant parasitic Anguinid nematodes to the developing seedheads of forage grasses and cereals. This understudied group of plant-associated Actinomycetes includes the neurotoxigenic plant pathogen, R. toxicus, which causes annual ryegrass toxicity in grazing livestock. Rathayibacter toxicus is currently endemic to Australia and is listed as a plant pathogen select agent by the U.S. Department of Agriculture – Animal and Plant Health Inspection Service. The complex Rathayibacter disease cycle requires intimate interactions with the nematode vector and plant hosts, which warrants an increased understanding of the secretory and surface-associated proteins that mediate these diverse eukaryotic interactions. Here we present the first comparative secretome analysis for this complex, nematode-vectored Rathayibacter genera that compares the three agronomically-damaging toxigenic and atoxigenic Rathayibacter species, R. toxicus, R. iranicus, and R. tritici. The exoproteomic comparison identified 1,423 unique proteins between the three species using LC-MS/MS, leading to the identification of putative pathogenicity-related proteins and proteins that may mediate nematode attachment. Of the uniquely identified proteins, 94 homologous proteins were conserved between the three Rathayibacter exoproteomes and comprised between 43.4 – 58.6% of total protein abundance. Comparative analyses revealed both conserved and uniquely expressed extracellular proteins, which, interestingly, had more similarities to extracellular proteins commonly associated with bacterial animal pathogens than classical plant pathogens. This comparative exoproteome analysis will facilitate the characterization of proteins essential for vector attachment and host colonization and assist in the development of serological diagnostic assays.

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Partial Proteome of the Corynetoxin‐Producing Gram‐Positive Bacterium, Rathayibacter toxicus

Cited by 2 publications

References 16 publications

Immunoreagents for development of a diagnostic assay specific for Rathayibacter toxicus

Immunoreagents for development of a diagnostic assay specific for Rathayibacter toxicus

Comparative Secretome Analyses of Toxigenic and AtoxigenicRathayibacterSpecies

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