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

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dc.contributor.authorGallo, Mariana
dc.contributor.authorLuti, Simone
dc.contributor.authorBaroni, Fabio
dc.contributor.authorBaccelli, Ivan
dc.contributor.authorCilli, Eduardo Maffud [UNESP]
dc.contributor.authorCicchi, Costanza
dc.contributor.authorLeri, Manuela
dc.contributor.authorSpisni, Alberto
dc.contributor.authorPertinhez, Thelma A.
dc.contributor.authorPazzagli, Luigia
dc.contributor.institutionUniversity of Parma
dc.contributor.institutionUniversity of Florence
dc.contributor.institutionNational Research Council of Italy
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2023-07-29T13:41:34Z
dc.date.available2023-07-29T13:41:34Z
dc.date.issued2023-02-01
dc.description.abstractCerato-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.en
dc.description.affiliationDepartment of Medicine and Surgery University of Parma
dc.description.affiliationDepartment of Biomedical Experimental and Clinical Sciences University of Florence
dc.description.affiliationInstitute for Sustainable Plant Protection National Research Council of Italy
dc.description.affiliationDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)
dc.description.affiliationUnespDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)
dc.identifierhttp://dx.doi.org/10.3390/ijms24032251
dc.identifier.citationInternational Journal of Molecular Sciences, v. 24, n. 3, 2023.
dc.identifier.doi10.3390/ijms24032251
dc.identifier.issn1422-0067
dc.identifier.issn1661-6596
dc.identifier.scopus2-s2.0-85147895356
dc.identifier.urihttp://hdl.handle.net/11449/248352
dc.language.isoeng
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.sourceScopus
dc.subjectfungal PAMP
dc.subjecthydrophobins
dc.subjectplant defense
dc.subjectself-assembly
dc.titlePlant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Featuresen
dc.typeArtigo
unesp.author.orcid0000-0002-0022-4499[1]
unesp.author.orcid0000-0001-7050-6590[2]
unesp.author.orcid0000-0002-1368-1250[4]
unesp.author.orcid0000-0002-3785-0805[7]
unesp.author.orcid0000-0002-3065-6567[9]
unesp.author.orcid0000-0002-6365-1615[10]

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