PLoS ONE (Jan 2016)

Label-Free Quantitative Proteomic Analysis of Puccinia psidii Uredospores Reveals Differences of Fungal Populations Infecting Eucalyptus and Guava.

  • Maria Carolina Quecine,
  • Thiago Falda Leite,
  • Andressa Peres Bini,
  • Thais Regiani,
  • Lívia Maria Franceschini,
  • Ilara Gabriela Frasson Budzinski,
  • Felipe Garbelini Marques,
  • Mônica Teresa Veneziano Labate,
  • Simone Guidetti-Gonzalez,
  • David Henry Moon,
  • Carlos Alberto Labate

DOI
https://doi.org/10.1371/journal.pone.0145343
Journal volume & issue
Vol. 11, no. 1
p. e0145343

Abstract

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Puccinia psidii sensu lato (s.l.) is the causal agent of eucalyptus and guava rust, but it also attacks a wide range of plant species from the myrtle family, resulting in a significant genetic and physiological variability among populations accessed from different hosts. The uredospores are crucial to P. psidii dissemination in the field. Although they are important for the fungal pathogenesis, their molecular characterization has been poorly studied. In this work, we report the first in-depth proteomic analysis of P. psidii s.l. uredospores from two contrasting populations: guava fruits (PpGuava) and eucalyptus leaves (PpEucalyptus). NanoUPLC-MSE was used to generate peptide spectra that were matched to the UniProt Puccinia genera sequences (UniProt database) resulting in the first proteomic analysis of the phytopathogenic fungus P. psidii. Three hundred and fourty proteins were detected and quantified using Label free proteomics. A significant number of unique proteins were found for each sample, others were significantly more or less abundant, according to the fungal populations. In PpGuava population, many proteins correlated with fungal virulence, such as malate dehydrogenase, proteossomes subunits, enolases and others were increased. On the other hand, PpEucalyptus proteins involved in biogenesis, protein folding and translocation were increased, supporting the physiological variability of the fungal populations according to their protein reservoirs and specific host interaction strategies.