Dual-specificity protein phosphatase Msg5 controls cell wall integrity and virulence in Fusarium oxysporum

Tânia R Fernandes1, Encarnación Sánchez Salvador1, Ángela G Tapia1

  • 1Departamento de Genética, Campus de Excelencia Internacional Agroalimentario ceiA3, Universidad de Córdoba, 14071 Córdoba, Spain.

Insights

The fungal pathogen Fusarium oxysporum

Area of Science:

  • Molecular Biology
  • Mycology
  • Plant Pathology

Background:

  • Mitogen-activated protein kinase (MAPK) cascades regulate fungal development and virulence.
  • Protein phosphatases, like Msg5, control MAPK activity, crucial for adaptation to environmental stimuli.
  • Msg5 in Saccharomyces cerevisiae dephosphorylates MAPKs involved in cell wall integrity and pheromone responses.

Purpose of the Study:

  • To investigate the function of the Msg5 ortholog in the fungal phytopathogen Fusarium oxysporum.
  • To elucidate Msg5's role in regulating the Mpk1 MAPK pathway and its impact on virulence.

Main Methods:

  • Gene deletion to create msg5Δ mutants in F. oxysporum.
  • Analysis of Mpk1 phosphorylation levels.
  • Assessment of sensitivity to cell wall targeting agents (Calcofluor White).
  • Evaluation of colony growth, conidiation, hyphal chemotropism, and plant virulence.

Main Results:

  • msg5Δ mutants exhibited constitutive high Mpk1 phosphorylation and increased Calcofluor White sensitivity.
  • Colony growth and conidiation were reduced in msg5Δ mutants.
  • Hyphal chemotropism and virulence on tomato plants were significantly impaired in msg5Δ mutants.

Conclusions:

  • Msg5 is essential for regulating the cell wall integrity MAPK cascade in F. oxysporum.
  • Msg5 plays a critical role in infection-related signaling and virulence of this important fungal pathogen.

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