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Heterologous Production and Functional Characterization of Ageritin, a Novel Type of Ribotoxin Highly Expressed during Fruiting of the Edible Mushroom Agrocybe aegerita

Tayyrov, Annageldi and Azevedo, Sophie and Herzog, Robert and Vogt, Eva and Arzt, Simon and Lüthy, Peter and Müller, Pie and Rühl, Martin and Hennicke, Florian and Künzler, Markus. (2019) Heterologous Production and Functional Characterization of Ageritin, a Novel Type of Ribotoxin Highly Expressed during Fruiting of the Edible Mushroom Agrocybe aegerita. Applied and Environmental Microbiology, 85 (21). e01549-19.

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Official URL: https://edoc.unibas.ch/72983/

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Abstract

Fungi produce various defense proteins against antagonists, including ribotoxins. These toxins cleave a single phosphodiester bond within the universally conserved sarcin-ricin loop of ribosomes and inhibit protein biosynthesis. Here, we report on the structure and function of ageritin, a previously reported ribotoxin from the edible mushroom; Agrocybe aegerita; The amino acid sequence of ageritin was derived from cDNA isolated from the dikaryon; A. aegerita; AAE-3 and lacks, according to; in silico; prediction, a signal peptide for classical secretion, predicting a cytoplasmic localization of the protein. The calculated molecular weight of the protein is slightly higher than the one reported for native ageritin. The; A. aegerita; ageritin-encoding gene,; AaeAGT1; , is highly induced during fruiting, and toxicity assays with; AaeAGT1; heterologously expressed in; Escherichia coli; showed a strong toxicity against; Aedes aegypti; larvae yet not against nematodes. The activity of recombinant; A. aegerita; ageritin toward rabbit ribosomes was confirmed; in vitro; Mutagenesis studies revealed a correlation between; in vivo; and; in vitro; activities, indicating that entomotoxicity is mediated by ribonucleolytic cleavage. The strong larvicidal activity of ageritin makes this protein a promising candidate for novel biopesticide development.; IMPORTANCE; Our results suggest a pronounced organismal specificity of a protein toxin with a very conserved intracellular molecular target. The molecular details of the toxin-target interaction will provide important insight into the mechanism of action of protein toxins and the ribosome. This insight might be exploited to develop novel bioinsecticides.
Faculties and Departments:09 Associated Institutions > Swiss Tropical and Public Health Institute (Swiss TPH)
09 Associated Institutions > Swiss Tropical and Public Health Institute (Swiss TPH) > Department of Epidemiology and Public Health (EPH) > Health Interventions > Vector Control (Müller)
UniBasel Contributors:Müller, Pie
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Microbiology
ISSN:0099-2240
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:12 Dec 2019 11:00
Deposited On:12 Dec 2019 11:00

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