Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features
Autor(a) principal: | |
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Data de Publicação: | 2023 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/ijms24032251 http://hdl.handle.net/11449/248352 |
Resumo: | Cerato-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. |
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Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Featuresfungal PAMPhydrophobinsplant defenseself-assemblyCerato-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.Department of Medicine and Surgery University of ParmaDepartment of Biomedical Experimental and Clinical Sciences University of FlorenceInstitute for Sustainable Plant Protection National Research Council of ItalyDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)Department of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP)University of ParmaUniversity of FlorenceNational Research Council of ItalyUniversidade Estadual Paulista (UNESP)Gallo, MarianaLuti, SimoneBaroni, FabioBaccelli, IvanCilli, Eduardo Maffud [UNESP]Cicchi, CostanzaLeri, ManuelaSpisni, AlbertoPertinhez, Thelma A.Pazzagli, Luigia2023-07-29T13:41:34Z2023-07-29T13:41:34Z2023-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3390/ijms24032251International Journal of Molecular Sciences, v. 24, n. 3, 2023.1422-00671661-6596http://hdl.handle.net/11449/24835210.3390/ijms240322512-s2.0-85147895356Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInternational Journal of Molecular Sciencesinfo:eu-repo/semantics/openAccess2023-07-29T13:41:35Zoai:repositorio.unesp.br:11449/248352Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T13:54:45.805117Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
title |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
spellingShingle |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features Gallo, Mariana fungal PAMP hydrophobins plant defense self-assembly |
title_short |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
title_full |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
title_fullStr |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
title_full_unstemmed |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
title_sort |
Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features |
author |
Gallo, Mariana |
author_facet |
Gallo, Mariana Luti, Simone Baroni, Fabio Baccelli, Ivan Cilli, Eduardo Maffud [UNESP] Cicchi, Costanza Leri, Manuela Spisni, Alberto Pertinhez, Thelma A. Pazzagli, Luigia |
author_role |
author |
author2 |
Luti, Simone Baroni, Fabio Baccelli, Ivan Cilli, Eduardo Maffud [UNESP] Cicchi, Costanza Leri, Manuela Spisni, Alberto Pertinhez, Thelma A. Pazzagli, Luigia |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
University of Parma University of Florence National Research Council of Italy Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Gallo, Mariana Luti, Simone Baroni, Fabio Baccelli, Ivan Cilli, Eduardo Maffud [UNESP] Cicchi, Costanza Leri, Manuela Spisni, Alberto Pertinhez, Thelma A. Pazzagli, Luigia |
dc.subject.por.fl_str_mv |
fungal PAMP hydrophobins plant defense self-assembly |
topic |
fungal PAMP hydrophobins plant defense self-assembly |
description |
Cerato-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. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-07-29T13:41:34Z 2023-07-29T13:41:34Z 2023-02-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.3390/ijms24032251 International Journal of Molecular Sciences, v. 24, n. 3, 2023. 1422-0067 1661-6596 http://hdl.handle.net/11449/248352 10.3390/ijms24032251 2-s2.0-85147895356 |
url |
http://dx.doi.org/10.3390/ijms24032251 http://hdl.handle.net/11449/248352 |
identifier_str_mv |
International Journal of Molecular Sciences, v. 24, n. 3, 2023. 1422-0067 1661-6596 10.3390/ijms24032251 2-s2.0-85147895356 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
International Journal of Molecular Sciences |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128289249689600 |