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The requirement for protein O-mannosylation for Ustilago maydis virulence seems to be linked to intrinsic aspects of the infection process rather than an altered plant response

AutorFernández-Álvarez, Alfonso ; Elías-Villalobos, Alberto ; Ibeas, José I.
Fecha de publicación2010
EditorTaylor & Francis
CitaciónPlant Signaling and Behavior 5(4): 412-414 (2010)
ResumenFungal plant pathogenesis involves complex crosstalk between fungi and their plant hosts. In the case of biotrophic fungi, the host interaction is finely controlled to maintain plant viability during infection since the fungus depends on the survival of colonized plant cells. Many proteins which participate in this process are thought to be glycosylated. Thus, defects in the glycosylation of fungal proteins might alter the normally attenuated plant response and consequently affect fungal progression. O-mannosyltransferases are responsible for adding mannose residues onto target proteins, with each O-mannosyltransferase having individual target specificities. In an earlier study, we showed that O-mannosylation is essential for Ustilago maydis virulence. We found that the loss of O-mannosyltransferase PMT4 was associated with a reduced formation frequency of the invasive morphogenic structure known as the appressorium, combined with a loss in their ability to penetrate plant cuticle. Here, we discuss the possible molecular causes of these phenotypes and present additional evidence, which argue against an alteration of plant response to fungal infection as the primary cause of the Δpmt4 phenotype.
DescripciónArticle Addendum.
Versión del editorhttp://dx.doi.org/10.4161/psb.5.4.10805
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