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Erratum published on 22 March 2021, see Toxins 2021, 13(3), 229.
Article

Several New Putative Bacterial ADP-Ribosyltransferase Toxins Are Revealed from In Silico Data Mining, Including the Novel Toxin Vorin, Encoded by the Fire Blight Pathogen Erwinia amylovora

Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada
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Author to whom correspondence should be addressed.
Toxins 2020, 12(12), 792; https://doi.org/10.3390/toxins12120792
Received: 10 November 2020 / Revised: 28 November 2020 / Accepted: 10 December 2020 / Published: 11 December 2020
(This article belongs to the Special Issue Structure and Function of Bacterial ADP-Ribosylation Toxins)
Mono-ADP-ribosyltransferase (mART) toxins are secreted by several pathogenic bacteria that disrupt vital host cell processes in deadly diseases like cholera and whooping cough. In the last two decades, the discovery of mART toxins has helped uncover the mechanisms of disease employed by pathogens impacting agriculture, aquaculture, and human health. Due to the current abundance of mARTs in bacterial genomes, and an unprecedented availability of genomic sequence data, mART toxins are amenable to discovery using an in silico strategy involving a series of sequence pattern filters and structural predictions. In this work, a bioinformatics approach was used to discover six bacterial mART sequences, one of which was a functional mART toxin encoded by the plant pathogen, Erwinia amylovora, called Vorin. Using a yeast growth-deficiency assay, we show that wild-type Vorin inhibited yeast cell growth, while catalytic variants reversed the growth-defective phenotype. Quantitative mass spectrometry analysis revealed that Vorin may cause eukaryotic host cell death by suppressing the initiation of autophagic processes. The genomic neighbourhood of Vorin indicated that it is a Type-VI-secreted effector, and co-expression experiments showed that Vorin is neutralized by binding of a cognate immunity protein, VorinI. We demonstrate that Vorin may also act as an antibacterial effector, since bacterial expression of Vorin was not achieved in the absence of VorinI. Vorin is the newest member of the mART family; further characterization of the Vorin/VorinI complex may help refine inhibitor design for mART toxins from other deadly pathogens. View Full-Text
Keywords: mono-ADP-ribosyltransferase toxins; Erwinia amylovora; toxin-antitoxin; bacterial toxins; agriculture diseases mono-ADP-ribosyltransferase toxins; Erwinia amylovora; toxin-antitoxin; bacterial toxins; agriculture diseases
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MDPI and ACS Style

Tremblay, O.; Thow, Z.; Geddes-McAlister, J.; Merrill, A.R. Several New Putative Bacterial ADP-Ribosyltransferase Toxins Are Revealed from In Silico Data Mining, Including the Novel Toxin Vorin, Encoded by the Fire Blight Pathogen Erwinia amylovora. Toxins 2020, 12, 792. https://doi.org/10.3390/toxins12120792

AMA Style

Tremblay O, Thow Z, Geddes-McAlister J, Merrill AR. Several New Putative Bacterial ADP-Ribosyltransferase Toxins Are Revealed from In Silico Data Mining, Including the Novel Toxin Vorin, Encoded by the Fire Blight Pathogen Erwinia amylovora. Toxins. 2020; 12(12):792. https://doi.org/10.3390/toxins12120792

Chicago/Turabian Style

Tremblay, Olivier, Zachary Thow, Jennifer Geddes-McAlister, and A. Rod Merrill. 2020. "Several New Putative Bacterial ADP-Ribosyltransferase Toxins Are Revealed from In Silico Data Mining, Including the Novel Toxin Vorin, Encoded by the Fire Blight Pathogen Erwinia amylovora" Toxins 12, no. 12: 792. https://doi.org/10.3390/toxins12120792

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