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Identification of glycoproteins involved in virulence in Ustilago maydis

AutorMoreno-Sánchez, Ismael; Ibeas, José I.
Fecha de publicación2016
EditorSociedad Española de Microbiología
CitaciónXI Reunión Microbiología Molecular (2016)
ResumenUstilago maydis has raised as an excellent model for the study of plant-pathogen interactions, and its relation with maize plant is one of the systems in which studies can be tackled from both plant and pathogen perspective (Djamei & Kahmann, 2012). U. maydis genome contains more than 500 putative secreted proteins, of which more than 50% doesn`t have known functional domains and many of these proteins have been related to infection process (Kämper et al., 2006). Protein N- and O- glycosylation are critical processes in host-pathogen relations, in fact mutations in genes pmt4, gls1 and gas2 compromise U. maydis virulence on maize, affecting different steps in the infection process (Fernandez-Alvarez et al., 2009; Fernandez-Alvarez et al., 2013). We have now performed a secretome analysis in order to identify proteins glycosylated by Pmt4 and/or Gls1, produced only when the virulence program is activated by over-expressing the transcription factor Biz1. Up today we have identified by mass spectrometry and MASCOT analysis two proteins glycosylated by Pmt4 and seven proteins glycosylated by Gls1, all dependent of the virulence program activation. These proteins are actually being characterized. Moreover, we have also isolated cell wall proteins from wild-type, Δpmt4 and Δgls1 mutants that will be analysed in a similar way.
DescripciónResumen del trabajo presentado a la XI Reunión del Grupo de Microbiología Molecular, celebrada en Sevilla del 6 al 8 de septiembre de 2016.
URIhttp://hdl.handle.net/10261/163787
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