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    • WISSENSCHAFTLICHE ARBEITEN
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    • Dpto. Bioquímica y Biología Molecular y Fisiología
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    Por favor, use este identificador para citar o enlazar este ítem:https://uvadoc.uva.es/handle/10324/62924

    Título
    Deciphering molecular determinants underlying Penicillium digitatum’s response to biological and chemical antifungal agents by tandem mass tag (TMT)-based high-resolution LC-MS/MS
    Autor
    Citores González, LucíaAutoridad UVA Orcid
    Valletta, Mariangela
    Singh, Vikram Pratap
    Pedone, Paolo Vincenzo
    Iglesias Álvarez, María del RosarioAutoridad UVA Orcid
    Ferreras Rodríguez, José MiguelAutoridad UVA Orcid
    Chambery, Angela
    Russo, Rosita
    Año del Documento
    2022
    Editorial
    MDPI
    Descripción
    Producción Científica
    Documento Fuente
    International Journal of Molecular Sciences, 2022, Vol. 23, Nº. 2, 680
    Zusammenfassung
    Penicillium digitatum is a widespread pathogen responsible for the postharvest decay of citrus, one of the most economically important crops worldwide. Currently, chemical fungicides are still the main strategy to control the green mould disease caused by the fungus. However, the increasing selection and proliferation of fungicide-resistant strains require more efforts to explore new alternatives acting via new or unexplored mechanisms for postharvest disease management. To date, several non-chemical compounds have been investigated for the control of fungal pathogens. In this scenario, understanding the molecular determinants underlying P. digitatum’s response to biological and chemical antifungals may help in the development of safer and more effective non-chemical control methods. In this work, a proteomic approach based on isobaric labelling and a nanoLC tandem mass spectrometry approach was used to investigate molecular changes associated with P. digitatum’s response to treatments with α-sarcin and beetin 27 (BE27), two proteins endowed with antifungal activity. The outcomes of treatments with these biological agents were then compared with those triggered by the commonly used chemical fungicide thiabendazole (TBZ). Our results showed that differentially expressed proteins mainly include cell wall-degrading enzymes, proteins involved in stress response, antioxidant and detoxification mechanisms and metabolic processes such as thiamine biosynthesis. Interestingly, specific modulations in response to protein toxins treatments were observed for a subset of proteins. Deciphering the inhibitory mechanisms of biofungicides and chemical compounds, together with understanding their effects on the fungal physiology, will provide a new direction for improving the efficacy of novel antifungal formulations and developing new control strategies.
    Materias (normalizadas)
    Penicillium digitatum
    Proteomics
    Proteómica
    Ribosome inactivating protein
    Ribosomes - Structure
    Proteins - Synthesis
    Ribotoxin
    Fungi
    Molds (Fungi)
    Citrus
    Cítricos
    Plant pathology
    Enfermedades de las plantas
    Fungal diseases of plants
    Biochemistry
    Molecular biology
    Materias Unesco
    2302.27 Proteínas
    3108.05 Hongos
    2414.09 Mohos
    2302 Bioquímica
    2302.21 Biología Molecular
    ISSN
    1422-0067
    Revisión por pares
    SI
    DOI
    10.3390/ijms23020680
    Patrocinador
    Ministero dell'Università e della Ricerca (MIUR) de Italia , project PON “Research and Innovation 2014–2020” - (Grant AIM 1890997-2)
    MISE, project NUTRABEST PON I&C 2014–2020 - (Grant F/200050/01–03/X45)
    Junta de Castilla y León, Consejería de Educación - (Grant VA033G19)
    Version del Editor
    https://www.mdpi.com/1422-0067/23/2/680
    Propietario de los Derechos
    © 2022 The Authors
    Idioma
    eng
    URI
    https://uvadoc.uva.es/handle/10324/62924
    Tipo de versión
    info:eu-repo/semantics/publishedVersion
    Derechos
    openAccess
    Aparece en las colecciones
    • DEP06 - Artículos de revista [352]
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    Dateien zu dieser Ressource
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    Deciphering-Molecular-Determinants-Underlying-Penicillium.pdf
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    Universidad de Valladolid

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