Dataset Information

The potential use of the Penicillium chrysogenum antifungal protein PAF, the designed variant PAFopt and its ?-core peptide P?opt in plant protection.

ABSTRACT: The prevention of enormous crop losses caused by pesticide-resistant fungi is a serious challenge in agriculture. Application of alternative fungicides, such as antifungal proteins and peptides, provides a promising basis to overcome this problem; however, their direct use in fields suffers limitations, such as high cost of production, low stability, narrow antifungal spectrum and toxicity on plant or mammalian cells. Recently, we demonstrated that a Penicillium chrysogenum-based expression system provides a feasible tool for economic production of P. chrysogenum antifungal protein (PAF) and a rational designed variant (PAFopt ), in which the evolutionary conserved ?-core motif was modified to increase antifungal activity. In the present study, we report for the first time that ?-core modulation influences the antifungal spectrum and efficacy of PAF against important plant pathogenic ascomycetes, and the synthetic ?-core peptide P?opt , a derivative of PAFopt , is antifungal active against these pathogens in vitro. Finally, we proved the protective potential of PAF against Botrytis cinerea infection in tomato plant leaves. The lack of any toxic effects on mammalian cells and plant seedlings, as well as the high tolerance to harsh environmental conditions and proteolytic degradation further strengthen our concept for applicability of these proteins and peptide in agriculture.

SUBMITTER: Toth L

PROVIDER: S-EPMC7415367 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Publications

The potential use of the Penicillium chrysogenum antifungal protein PAF, the designed variant PAF<sup>opt</sup> and its γ-core peptide Pγ<sup>opt</sup> in plant protection.

Tóth Liliána L Boros Éva É Poór Péter P Ördög Attila A Kele Zoltán Z Váradi Györgyi G Holzknecht Jeanett J Bratschun-Khan Doris D Nagy István I Tóth Gábor K GK Rákhely Gábor G Marx Florentine F Galgóczy László L

Microbial biotechnology 20200324 5

The prevention of enormous crop losses caused by pesticide-resistant fungi is a serious challenge in agriculture. Application of alternative fungicides, such as antifungal proteins and peptides, provides a promising basis to overcome this problem; however, their direct use in fields suffers limitations, such as high cost of production, low stability, narrow antifungal spectrum and toxicity on plant or mammalian cells. Recently, we demonstrated that a Penicillium chrysogenum-based expression syst ...[more]

PMID: 32207883

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Project description:PAFs are short cationic and tryptophan-rich synthetic peptides with cell-penetrating antifungal activity. They show potent and selective killing activity against major fungal pathogens and low toxicity to other eukaryotic and bacterial cells. These properties make them a promising alternative to fulfill the need of novel antifungals with potential applications in crop protection, food preservation, and medical therapies. However, the difficulties of cost-effective manufacturing of PAFs by chemical synthesis or biotechnological production in microorganisms have hampered their development for practical use. This work explores the feasibility of using rice seeds as an economical and safe production system of PAFs. The rationally designed PAF102 peptide with improved antifungal properties was selected for assessing PAF biotechnological production. Two different strategies are evaluated: (1) the production as a single peptide targeted to protein bodies and (2) the production as an oleosin fusion protein targeted to oil bodies. Both strategies are designed to offer stability to the PAF peptide in the host plant and to facilitate its downstream purification. Our results demonstrate that PAF does not accumulate to detectable levels in rice seeds when produced as a single peptide, whereas it is successfully produced as fusion protein to the Oleosin18, up to 20 μg of peptide per gram of grain. We show that the expression of the chimeric Ole18-PAF102 gene driven by the Ole18 promoter results in the specific accumulation of the fusion protein in the embryo and aleurone layer of the rice seed. Ole18-PAF102 accumulation has no deleterious effects on seed yield, germination capacity, or seedling growth. We also show that the Oleosin18 protein serves as carrier to target the fusion protein to oil bodies facilitating PAF102 recovery. Importantly, the recovered PAF102 is active against the fungal phytopathogen Fusarium proliferatum. Altogether, our results prove that the oleosin fusion technology allows the production of PAF bioactive peptides to assist the exploitation of these antifungal compounds.

Dataset Information

The potential use of the Penicillium chrysogenum antifungal protein PAF, the designed variant PAFopt and its ?-core peptide P?opt in plant protection.

Publications

The potential use of the Penicillium chrysogenum antifungal protein PAF, the designed variant PAF<sup>opt</sup> and its γ-core peptide Pγ<sup>opt</sup> in plant protection.

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