The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding

Autores
de Oliveira, Aline L.; Gallo, Mariana; Pazzagli, Luigia; Benedetti, Celso E.; Cappugi, Gianni; Scala, Aniello; Pantera, Barbara; Spisni, Alberto; Pertinhez, Thelma A.; Cicero, Daniel Oscar
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated molecular pattern because it induces various defense responses in the host, including production of phytoalexins and cell death. Although much is known about the properties of CP and related proteins as elicitors of plant defense mechanisms, its biochemical activity and host target(s) remain elusive. Here, we present the three-dimensional structure of CP. The protein, which exhibits a remarkable pH and thermal stability, has a double ψβ-barrel fold quite similar to those found in expansins, endoglucanases, and the plant defense protein barwin. Interestingly, although CP lacks lytic activity against a variety of carbohydrates, it binds oligosaccharides. We identified the CP region responsible for binding as a shallow surface located at one side of the β-barrel. Chemical shift perturbation of the protein amide protons, induced by oligo-N-acetylglucosamines of various size, showed that all the residues involved in oligosaccharide binding are conserved among the members of the CP family. Overall, the results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.
Fil: de Oliveira, Aline L.. National Laboratory of Biosciences; Brasil
Fil: Gallo, Mariana. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
Fil: Pazzagli, Luigia. University of Florence. Department of Biochemical Sciences; Italia
Fil: Benedetti, Celso E.. National Laboratory of Biosciences; Brasil
Fil: Cappugi, Gianni. University of Florence. Department of Biochemical Sciences; Italia
Fil: Scala, Aniello. University of Florence. Department of Agricultural Biotechnologies; Italia
Fil: Pantera, Barbara. University of Florence. Department of Biochemical Sciences; Italia
Fil: Spisni, Alberto. University of Parma. Department of Experimental Medicine; Italia
Fil: Pertinhez, Thelma A.. University of Parma. Department of Experimental Medicine; Italia
Fil: Cicero, Daniel Oscar. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
Materia
Cerato-Platanin
Nmr
Structure
Expansin
Fungal Elicitor
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/12834
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/12834
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate bindingde Oliveira, Aline L.Gallo, MarianaPazzagli, LuigiaBenedetti, Celso E.Cappugi, GianniScala, AnielloPantera, BarbaraSpisni, AlbertoPertinhez, Thelma A.Cicero, Daniel OscarCerato-PlataninNmrStructureExpansinFungal Elicitorhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated molecular pattern because it induces various defense responses in the host, including production of phytoalexins and cell death. Although much is known about the properties of CP and related proteins as elicitors of plant defense mechanisms, its biochemical activity and host target(s) remain elusive. Here, we present the three-dimensional structure of CP. The protein, which exhibits a remarkable pH and thermal stability, has a double ψβ-barrel fold quite similar to those found in expansins, endoglucanases, and the plant defense protein barwin. Interestingly, although CP lacks lytic activity against a variety of carbohydrates, it binds oligosaccharides. We identified the CP region responsible for binding as a shallow surface located at one side of the β-barrel. Chemical shift perturbation of the protein amide protons, induced by oligo-N-acetylglucosamines of various size, showed that all the residues involved in oligosaccharide binding are conserved among the members of the CP family. Overall, the results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.Fil: de Oliveira, Aline L.. National Laboratory of Biosciences; BrasilFil: Gallo, Mariana. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Pazzagli, Luigia. University of Florence. Department of Biochemical Sciences; ItaliaFil: Benedetti, Celso E.. National Laboratory of Biosciences; BrasilFil: Cappugi, Gianni. University of Florence. Department of Biochemical Sciences; ItaliaFil: Scala, Aniello. University of Florence. Department of Agricultural Biotechnologies; ItaliaFil: Pantera, Barbara. University of Florence. Department of Biochemical Sciences; ItaliaFil: Spisni, Alberto. University of Parma. Department of Experimental Medicine; ItaliaFil: Pertinhez, Thelma A.. University of Parma. Department of Experimental Medicine; ItaliaFil: Cicero, Daniel Oscar. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaAmerican Society For Biochemistry And Molecular Biology2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/12834de Oliveira, Aline L.; Gallo, Mariana; Pazzagli, Luigia; Benedetti, Celso E.; Cappugi, Gianni; et al.; The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 20; 2011; 17560-175680021-9258enginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/286/20/17560.fullinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.223644info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3093830/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-26T10:24:46Zoai:ri.conicet.gov.ar:11336/12834instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-02-26 10:24:46.838CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
title The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
spellingShingle The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
de Oliveira, Aline L.
Cerato-Platanin
Nmr
Structure
Expansin
Fungal Elicitor
title_short The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
title_full The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
title_fullStr The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
title_full_unstemmed The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
title_sort The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
dc.creator.none.fl_str_mv de Oliveira, Aline L.
Gallo, Mariana
Pazzagli, Luigia
Benedetti, Celso E.
Cappugi, Gianni
Scala, Aniello
Pantera, Barbara
Spisni, Alberto
Pertinhez, Thelma A.
Cicero, Daniel Oscar
author de Oliveira, Aline L.
author_facet de Oliveira, Aline L.
Gallo, Mariana
Pazzagli, Luigia
Benedetti, Celso E.
Cappugi, Gianni
Scala, Aniello
Pantera, Barbara
Spisni, Alberto
Pertinhez, Thelma A.
Cicero, Daniel Oscar
author_role author
author2 Gallo, Mariana
Pazzagli, Luigia
Benedetti, Celso E.
Cappugi, Gianni
Scala, Aniello
Pantera, Barbara
Spisni, Alberto
Pertinhez, Thelma A.
Cicero, Daniel Oscar
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cerato-Platanin
Nmr
Structure
Expansin
Fungal Elicitor
topic Cerato-Platanin
Nmr
Structure
Expansin
Fungal Elicitor
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated molecular pattern because it induces various defense responses in the host, including production of phytoalexins and cell death. Although much is known about the properties of CP and related proteins as elicitors of plant defense mechanisms, its biochemical activity and host target(s) remain elusive. Here, we present the three-dimensional structure of CP. The protein, which exhibits a remarkable pH and thermal stability, has a double ψβ-barrel fold quite similar to those found in expansins, endoglucanases, and the plant defense protein barwin. Interestingly, although CP lacks lytic activity against a variety of carbohydrates, it binds oligosaccharides. We identified the CP region responsible for binding as a shallow surface located at one side of the β-barrel. Chemical shift perturbation of the protein amide protons, induced by oligo-N-acetylglucosamines of various size, showed that all the residues involved in oligosaccharide binding are conserved among the members of the CP family. Overall, the results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.
Fil: de Oliveira, Aline L.. National Laboratory of Biosciences; Brasil
Fil: Gallo, Mariana. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
Fil: Pazzagli, Luigia. University of Florence. Department of Biochemical Sciences; Italia
Fil: Benedetti, Celso E.. National Laboratory of Biosciences; Brasil
Fil: Cappugi, Gianni. University of Florence. Department of Biochemical Sciences; Italia
Fil: Scala, Aniello. University of Florence. Department of Agricultural Biotechnologies; Italia
Fil: Pantera, Barbara. University of Florence. Department of Biochemical Sciences; Italia
Fil: Spisni, Alberto. University of Parma. Department of Experimental Medicine; Italia
Fil: Pertinhez, Thelma A.. University of Parma. Department of Experimental Medicine; Italia
Fil: Cicero, Daniel Oscar. University of Rome. Department of Chemical Science and Technology; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
description Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated molecular pattern because it induces various defense responses in the host, including production of phytoalexins and cell death. Although much is known about the properties of CP and related proteins as elicitors of plant defense mechanisms, its biochemical activity and host target(s) remain elusive. Here, we present the three-dimensional structure of CP. The protein, which exhibits a remarkable pH and thermal stability, has a double ψβ-barrel fold quite similar to those found in expansins, endoglucanases, and the plant defense protein barwin. Interestingly, although CP lacks lytic activity against a variety of carbohydrates, it binds oligosaccharides. We identified the CP region responsible for binding as a shallow surface located at one side of the β-barrel. Chemical shift perturbation of the protein amide protons, induced by oligo-N-acetylglucosamines of various size, showed that all the residues involved in oligosaccharide binding are conserved among the members of the CP family. Overall, the results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/12834
de Oliveira, Aline L.; Gallo, Mariana; Pazzagli, Luigia; Benedetti, Celso E.; Cappugi, Gianni; et al.; The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 20; 2011; 17560-17568
0021-9258
url http://hdl.handle.net/11336/12834
identifier_str_mv de Oliveira, Aline L.; Gallo, Mariana; Pazzagli, Luigia; Benedetti, Celso E.; Cappugi, Gianni; et al.; The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 20; 2011; 17560-17568
0021-9258
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/286/20/17560.full
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.223644
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3093830/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.176822

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