Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of Parma-
Autor(es): dc.contributorUniversity of Florence-
Autor(es): dc.contributorNational Research Council of Italy-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorGallo, Mariana-
Autor(es): dc.creatorLuti, Simone-
Autor(es): dc.creatorBaroni, Fabio-
Autor(es): dc.creatorBaccelli, Ivan-
Autor(es): dc.creatorCilli, Eduardo Maffud-
Autor(es): dc.creatorCicchi, Costanza-
Autor(es): dc.creatorLeri, Manuela-
Autor(es): dc.creatorSpisni, Alberto-
Autor(es): dc.creatorPertinhez, Thelma A.-
Autor(es): dc.creatorPazzagli, Luigia-
Data de aceite: dc.date.accessioned2025-08-21T15:24:09Z-
Data de disponibilização: dc.date.available2025-08-21T15:24:09Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-01-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/ijms24032251-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/248352-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/248352-
Descrição: dc.descriptionCerato-ulmin (CU) is a 75-amino-acid-long protein that belongs to the hydrophobin family. It self-assembles at hydrophobic–hydrophilic interfaces, forming films that reverse the wettability properties of the bound surface: a capability that may confer selective advantages to the fungus in colonizing and infecting elm trees. Here, we show for the first time that CU can elicit a defense reaction (induction of phytoalexin synthesis and ROS production) in non-host plants (Arabidopsis) and exerts its eliciting capacity more efficiently when in its soluble monomeric form. We identified two hydrophobic clusters on the protein’s loops endowed with dynamical and physical properties compatible with the possibility of reversibly interconverting between a disordered conformation and a β-strand-rich conformation when interacting with hydrophilic or hydrophobic surfaces. We propose that the plasticity of those loops may be part of the molecular mechanism that governs the protein defense elicitation capability.-
Descrição: dc.descriptionDepartment of Medicine and Surgery University of Parma-
Descrição: dc.descriptionDepartment of Biomedical Experimental and Clinical Sciences University of Florence-
Descrição: dc.descriptionInstitute for Sustainable Plant Protection National Research Council of Italy-
Descrição: dc.descriptionDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)-
Descrição: dc.descriptionDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Molecular Sciences-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectfungal PAMP-
Palavras-chave: dc.subjecthydrophobins-
Palavras-chave: dc.subjectplant defense-
Palavras-chave: dc.subjectself-assembly-
Título: dc.titlePlant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.