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Identification of MpPR1-I protein ligands and structural and functional analyses of MpPR-1s of Moniliophthora perniciosa in vitro

Grant number: 17/13319-6
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): March 01, 2018
Effective date (End): February 05, 2022
Field of knowledge:Biological Sciences - Genetics - Molecular Genetics and Genetics of Microorganisms
Principal researcher:Gonçalo Amarante Guimarães Pereira
Grantee:Renata Moro Baroni
Home Institution: Instituto de Biologia (IB). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:16/10498-4 - Investigation of strategies of adaptation to the pathogenic life style of fungi from the Moniliophthora genus at various levels of biological organizations: species, biotypes, and geographic lineages, AP.TEM
Associated scholarship(s):19/01418-5 - Structural charactherization of MpPR-1i and MpPR-1k proteins of the fungus Moniliophthora perniciosa that causes the Witches' Broom Disease, BE.EP.PD

Abstract

One of the best-studied gene families related to plant defense mechanisms encode proteins known as PR-1 (pathogenesis related protein 1). These proteins play an important role during pathogen-host interactions, can block the development of fungi and act as systemic acquired resistance marker. Interestingly, protein members of this superfamily SCP/TAPS that expressed by pathogenic nematodes, both from animals and plants, have immunomodulatory effects and suppress the host's defense response. Recently, it was found that proteins belonging to the SCP/TAPS superfamily, which includes PR-1 proteins, are capable of transporting cholesterol and bind to fatty acids and steroid molecules. Furthermore, it was shown that SCP/TAPS proteins have the ability to inhibit the action of hydrophobic plant-derived antifungal molecules. Notably, previous results from our group indicate that the protein MpPR-1k from Moniliophthora perniciosa would have the ability to export cholesterol and selectively bind to cholesterol, and MpPR-1i, binding palmitate.Thus, this project seeks to expand the understanding the mechanism action of these two proteins regarding their ability to interact with hydrophobic molecules such as sterols and fatty acids, as well as to elucidate the relevance of this ability during plant-pathogen interaction. So, the following activities will be performed: 1) quantification of the level of gene expression of the different MpPR-1s in the presence of steroidal antifungal agents such as eugenol and alpha-tomatine; 2) identification of a lipid molecule that was detected as bound to MpPR1-i protein; 3) characterization of the interaction of MpPR-1i with binders by co-crystallization assays followed by structural resolution by X-ray diffraction; 4) structural resolution of a mutant version of MpPR-1i that has acquired the ability to bind to cholesterol and o fMpPR-1ik that was found to bind to cholesterol. Therefore, we intend to understand more closely the mechanisms of action of these proteins in the plant-pathogen interaction, and especially during the interaction of M. perniciosa -cacao.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
VASCONCELOS, ADRIELLE A.; JOSE, JULIANA; TOKIMATU, PAULO M.; CAMARGO, ANTONIO P.; TEIXEIRA, PAULO J. P. L.; THOMAZELLA, DANIELA P. T.; DO PRADO, V, PAULA F.; FIORIN, GABRIEL L.; COSTA, JULIANA L.; FIGUEIRA, ANTONIO; CARAZZOLLE, MARCELO F.; PEREIRA, GONCALO A. G.; BARONI, RENATA M. Adaptive evolution of Moniliophthora PR-1 proteins towards its pathogenic lifestyle. BMC ECOLOGY AND EVOLUTION, v. 21, n. 1 MAY 14 2021. Web of Science Citations: 0.
BARSOTTINI, MARIO R. O.; COPSEY, ALICE; YOUNG, LUKE; BARONI, RENATA M.; CORDEIRO, ARTUR T.; PEREIRA, GONCALO A. G.; MOORE, ANTHONY L. Biochemical characterization and inhibition of the alternative oxidase enzyme from the fungal phytopathogen Moniliophthora perniciosa. COMMUNICATIONS BIOLOGY, v. 3, n. 1 MAY 25 2020. Web of Science Citations: 2.

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