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dc.contributor.author
Zhang, Shizhu
dc.contributor.author
Widemann, Emilie
dc.contributor.author
Bernard, Grausem
dc.contributor.author
Lesot, Agnes
dc.contributor.author
Pinot, Franck
dc.contributor.author
Pedrini, Nicolás
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dc.contributor.author
Keyhani, Nemat O.
dc.date.available
2020-01-28T16:51:53Z
dc.date.issued
2012-04
dc.identifier.citation
Zhang, Shizhu; Widemann, Emilie; Bernard, Grausem; Lesot, Agnes; Pinot, Franck; et al.; CYP52X1, representing new cytochrome P450 subfamily, displays fatty acid hydroxylase activity and contributes to virulence and growth on insect cuticular substrates in entomopathogenic fungus Beauveria bassiana; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 16; 4-2012; 13477-13486
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/95970
dc.description.abstract
Infection of insects by the entomopathogenic fungus Beauveria bassiana proceeds via attachment and penetration of the host cuticle. The outermost epicuticular layer or waxy layer of the insect represents a structure rich in lipids including abundant amounts of hydrocarbons and fatty acids. A member of a novel cytochrome P450 subfamily, CYP52X1, implicated in fatty acid assimilation by B. bassiana was characterized. B. bassiana targeted gene knockouts lacking Bbcyp52x1 displayed reduced virulence when topically applied to Galleria mellonella, but no reduction in virulence was noted when the insect cuticle was bypassed using an intrahemoceol injection assay. No significant growth defects were noted in the mutant as compared with the wild-type parent on any lipids substrates tested including alkanes and fatty acids. Insect epicuticle germination assays, however, showed reduced germination of ΔBbcyp52x1 conidia on grasshopper wings as compared with the wild-type parent. Complementation of the gene-knock with the full-length gene restored virulence and insect epicuticle germination to wild-type levels. Heterologous expression of CYP52X1 in yeast was used to characterize the substrate specificity of the enzyme. CYP52X1 displayed the highest activity against midrange fatty acids (C12:0 and C14:0) and epoxy stearic acid, 4–8-fold lower activity against C16:0, C18:1, and C18:2, and little to no activity against C9:0 and C18:0. Analyses of the products of the C12:0 and C18:1 reactions confirmed NADPH-dependent regioselective addition of a terminal hydroxyl to the substrates (ω-hydroxylase). These data implicate CYP52X1 as contributing to the penetration of the host cuticle via facilitating the assimilation of insect epicuticle lipids.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Cytochrome P450
dc.subject
Beauveria Bassiana
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Fatty Acid Hydroxylase
dc.subject
Insect Cuticle
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
CYP52X1, representing new cytochrome P450 subfamily, displays fatty acid hydroxylase activity and contributes to virulence and growth on insect cuticular substrates in entomopathogenic fungus Beauveria bassiana
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-05-06T14:41:04Z
dc.journal.volume
287
dc.journal.number
16
dc.journal.pagination
13477-13486
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda
dc.description.fil
Fil: Zhang, Shizhu. Nanjing Normal University; China. University of Florida; Estados Unidos
dc.description.fil
Fil: Widemann, Emilie. Université de Strasbourg; Francia
dc.description.fil
Fil: Bernard, Grausem. Université de Strasbourg; Francia
dc.description.fil
Fil: Lesot, Agnes. Université de Strasbourg; Francia
dc.description.fil
Fil: Pinot, Franck. Université de Strasbourg; Francia
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Fil: Pedrini, Nicolás. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
dc.description.fil
Fil: Keyhani, Nemat O.. University of Florida; Estados Unidos
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/287/16/13477
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M111.338947
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