The Botrytis cinerea aspartic proteinase family

Autores
Ten Have, Arjen; Espino, José J.; Dekkers, Ester; Van Sluyter, Steven C.; Brito, Nélida; Kay, John; González, Celedonio; van Kan, Jan A. L.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice. Scrutiny of the B. cinerea genome revealed the presence of nine additional Bcap genes, denoted Bcap6-14. The product of the Bcap8 gene was found to constitute up to 23% of the total protein secreted by B. cinerea. Bcap8-deficient mutants secreted approximately 70% less AP activity but were just as virulent as the wild-type strain. Phylogenetic analysis showed that Bcap8 has orthologs in many basidiomycetes but only few ascomycetes including the biocontrol fungus Trichoderma harzanium. Potential functions of the 14 APs in B. cinerea are discussed based on their sequence characteristics, phylogeny and predicted localization.
Fil: Ten Have, Arjen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina. Wageningen University. Laboratory of Phytopathology; Países Bajos
Fil: Espino, José J.. Universidad de la Laguna; España
Fil: Dekkers, Ester. Wageningen University. Laboratory of Phytopathology; Países Bajos
Fil: Van Sluyter, Steven C.. The Australian Wine Research Institute; Australia. The University Of Melbourne; Australia
Fil: Brito, Nélida. Universidad de la Laguna; España
Fil: Kay, John. Cardiff University; Reino Unido
Fil: González, Celedonio. Universidad de la Laguna; España
Fil: van Kan, Jan A. L.. Wageningen University. Laboratory of Phytopathology; Países Bajos
Materia
Gray Mould
Bioinformatics
Proteinase
Plant Pathogen
Phylogeny
Evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13256
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling The Botrytis cinerea aspartic proteinase familyTen Have, ArjenEspino, José J.Dekkers, EsterVan Sluyter, Steven C.Brito, NélidaKay, JohnGonzález, Celedoniovan Kan, Jan A. L.Gray MouldBioinformaticsProteinasePlant PathogenPhylogenyEvolutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice. Scrutiny of the B. cinerea genome revealed the presence of nine additional Bcap genes, denoted Bcap6-14. The product of the Bcap8 gene was found to constitute up to 23% of the total protein secreted by B. cinerea. Bcap8-deficient mutants secreted approximately 70% less AP activity but were just as virulent as the wild-type strain. Phylogenetic analysis showed that Bcap8 has orthologs in many basidiomycetes but only few ascomycetes including the biocontrol fungus Trichoderma harzanium. Potential functions of the 14 APs in B. cinerea are discussed based on their sequence characteristics, phylogeny and predicted localization.Fil: Ten Have, Arjen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina. Wageningen University. Laboratory of Phytopathology; Países BajosFil: Espino, José J.. Universidad de la Laguna; EspañaFil: Dekkers, Ester. Wageningen University. Laboratory of Phytopathology; Países BajosFil: Van Sluyter, Steven C.. The Australian Wine Research Institute; Australia. The University Of Melbourne; AustraliaFil: Brito, Nélida. Universidad de la Laguna; EspañaFil: Kay, John. Cardiff University; Reino UnidoFil: González, Celedonio. Universidad de la Laguna; EspañaFil: van Kan, Jan A. L.. Wageningen University. Laboratory of Phytopathology; Países BajosElsevier Inc2010-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13256Ten Have, Arjen; Espino, José J.; Dekkers, Ester; Van Sluyter, Steven C.; Brito, Nélida; et al.; The Botrytis cinerea aspartic proteinase family; Elsevier Inc; Fungal Genetics And Biology; 47; 1; 12-2010; 53-651087-1845enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1087184509001765info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fgb.2009.10.008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-05T10:08:36Zoai:ri.conicet.gov.ar:11336/13256instacron: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:34982025-11-05 10:08:37.151CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Botrytis cinerea aspartic proteinase family
title The Botrytis cinerea aspartic proteinase family
spellingShingle The Botrytis cinerea aspartic proteinase family
Ten Have, Arjen
Gray Mould
Bioinformatics
Proteinase
Plant Pathogen
Phylogeny
Evolution
title_short The Botrytis cinerea aspartic proteinase family
title_full The Botrytis cinerea aspartic proteinase family
title_fullStr The Botrytis cinerea aspartic proteinase family
title_full_unstemmed The Botrytis cinerea aspartic proteinase family
title_sort The Botrytis cinerea aspartic proteinase family
dc.creator.none.fl_str_mv Ten Have, Arjen
Espino, José J.
Dekkers, Ester
Van Sluyter, Steven C.
Brito, Nélida
Kay, John
González, Celedonio
van Kan, Jan A. L.
author Ten Have, Arjen
author_facet Ten Have, Arjen
Espino, José J.
Dekkers, Ester
Van Sluyter, Steven C.
Brito, Nélida
Kay, John
González, Celedonio
van Kan, Jan A. L.
author_role author
author2 Espino, José J.
Dekkers, Ester
Van Sluyter, Steven C.
Brito, Nélida
Kay, John
González, Celedonio
van Kan, Jan A. L.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Gray Mould
Bioinformatics
Proteinase
Plant Pathogen
Phylogeny
Evolution
topic Gray Mould
Bioinformatics
Proteinase
Plant Pathogen
Phylogeny
Evolution
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice. Scrutiny of the B. cinerea genome revealed the presence of nine additional Bcap genes, denoted Bcap6-14. The product of the Bcap8 gene was found to constitute up to 23% of the total protein secreted by B. cinerea. Bcap8-deficient mutants secreted approximately 70% less AP activity but were just as virulent as the wild-type strain. Phylogenetic analysis showed that Bcap8 has orthologs in many basidiomycetes but only few ascomycetes including the biocontrol fungus Trichoderma harzanium. Potential functions of the 14 APs in B. cinerea are discussed based on their sequence characteristics, phylogeny and predicted localization.
Fil: Ten Have, Arjen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina. Wageningen University. Laboratory of Phytopathology; Países Bajos
Fil: Espino, José J.. Universidad de la Laguna; España
Fil: Dekkers, Ester. Wageningen University. Laboratory of Phytopathology; Países Bajos
Fil: Van Sluyter, Steven C.. The Australian Wine Research Institute; Australia. The University Of Melbourne; Australia
Fil: Brito, Nélida. Universidad de la Laguna; España
Fil: Kay, John. Cardiff University; Reino Unido
Fil: González, Celedonio. Universidad de la Laguna; España
Fil: van Kan, Jan A. L.. Wageningen University. Laboratory of Phytopathology; Países Bajos
description The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice. Scrutiny of the B. cinerea genome revealed the presence of nine additional Bcap genes, denoted Bcap6-14. The product of the Bcap8 gene was found to constitute up to 23% of the total protein secreted by B. cinerea. Bcap8-deficient mutants secreted approximately 70% less AP activity but were just as virulent as the wild-type strain. Phylogenetic analysis showed that Bcap8 has orthologs in many basidiomycetes but only few ascomycetes including the biocontrol fungus Trichoderma harzanium. Potential functions of the 14 APs in B. cinerea are discussed based on their sequence characteristics, phylogeny and predicted localization.
publishDate 2010
dc.date.none.fl_str_mv 2010-12
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/11336/13256
Ten Have, Arjen; Espino, José J.; Dekkers, Ester; Van Sluyter, Steven C.; Brito, Nélida; et al.; The Botrytis cinerea aspartic proteinase family; Elsevier Inc; Fungal Genetics And Biology; 47; 1; 12-2010; 53-65
1087-1845
url http://hdl.handle.net/11336/13256
identifier_str_mv Ten Have, Arjen; Espino, José J.; Dekkers, Ester; Van Sluyter, Steven C.; Brito, Nélida; et al.; The Botrytis cinerea aspartic proteinase family; Elsevier Inc; Fungal Genetics And Biology; 47; 1; 12-2010; 53-65
1087-1845
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1087184509001765
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fgb.2009.10.008
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Inc
publisher.none.fl_str_mv Elsevier Inc
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
_version_ 1847977591511711744
score 13.121305

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