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dc.contributor.authorLópez Fernández, Loida
dc.contributor.authorRuiz Roldán, Carmen
dc.contributor.authorPareja Jaime, Y.
dc.contributor.authorPrieto, A.
dc.contributor.authorKhraiwesh, Husam M.
dc.contributor.authorGonzález Roncero, M. Isabel
dc.date.accessioned2017-12-01T11:31:36Z
dc.date.available2017-12-01T11:31:36Z
dc.date.issued2013
dc.identifier.urihttp://hdl.handle.net/10396/15624
dc.description.abstractWith the aim to decipher the molecular dialogue and cross talk between Fusarium oxysporum f.sp. lycopersci and its host during infection and to understand the molecular bases that govern fungal pathogenicity, we analysed genes presumably encoding N-acetylglucosaminyl transferases, involved in glycosylation of glycoproteins, glycolipids, proteoglycans or small molecule acceptors in other microorganisms. In silico analysis revealed the existence of seven putative N-glycosyl transferase encoding genes (named gnt) in F. oxysporum f.sp. lycopersici genome. gnt2 deletion mutants showed a dramatic reduction in virulence on both plant and animal hosts. Δgnt2 mutants had αalterations in cell wall properties related to terminal αor β-linked N-acetyl glucosamine. Mutant conidia and germlings also showed differences in structure and physicochemical surface properties. Conidial and hyphal aggregation differed between the mutant and wild type strains, in a pH independent manner. Transmission electron micrographs of germlings showed strong cell-to-cell adherence and the presence of an extracellular chemical matrix. Δgnt2 cell walls presented a significant reduction in N-linked oligosaccharides, suggesting the involvement of Gnt2 in N-glycosylation of cell wall proteins. Gnt2 was localized in Golgi-like sub-cellular compartments as determined by fluorescence microscopy of GFP::Gnt2 fusion protein after treatment with the antibiotic brefeldin A or by staining with fluorescent sphingolipid BODIPY-TR ceramide. Furthermore, density gradient ultracentrifugation allowed colocalization of GFP::Gnt2 fusion protein and Vps10p in subcellular fractions enriched in Golgi specific enzymatic activities. Our results suggest that N-acetylglucosaminyl transferases are key components for cell wall structure and influence interactions of F. oxysporum with both plant and animal hosts during pathogenicity.es_ES
dc.format.mimetypeapplication/pdfes_ES
dc.language.isoenges_ES
dc.publisherPublic Library of Sciencees_ES
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/4.0/es_ES
dc.sourcePLoS ONE 8(12): e84690 (2013)es_ES
dc.subjectPlant fungal pathogenses_ES
dc.subjectFungal structurees_ES
dc.subjectFusarium oxysporumes_ES
dc.subjectPlant cell wallses_ES
dc.subjectGlycosylationes_ES
dc.subjectFungal diseaseses_ES
dc.subjectSaccharomyces cerevisiaees_ES
dc.subjectTomatoeses_ES
dc.titleThe Fusarium oxysporum gnt2, Encoding a Putative NAcetylglucosamine Transferase, Is Involved in Cell Wall Architecture and Virulencees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1371/journal.pone.0084690es_ES
dc.relation.projectIDGobierno de España. BIO2010-015505es_ES
dc.relation.projectIDJunta de Andalucía. P08-CVI-3847es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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