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Updated: Aug 5, 2026

Label-Free Quantitative Proteomics Workflow for Discovery-Driven Host-Pathogen Interactions
05:37

Label-Free Quantitative Proteomics Workflow for Discovery-Driven Host-Pathogen Interactions

Published on: October 20, 2020

Phosphoproteomics of WHO-Priority Fungal Pathogens: Conserved Signaling Architecture, Pathogen-Specific Outputs, and

Yuhan Ding1, Chao Huang1, Shuo Ning1

  • 1NHC Key Laboratory of Enteric Pathogenic Microbiology, Jiangsu Provincial Center for Disease Control and Prevention, Nanjing 210009, China.

Pathogens (Basel, Switzerland)
|July 28, 2026
PubMed

Insights

Pathogenic fungi use protein phosphorylation to adapt and resist antifungal drugs. This study maps phosphorylation in key fungal pathogens, revealing conserved regulatory hubs but divergent virulence strategies, guiding new drug target discovery.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Protein phosphorylation is a critical post-translational modification regulating essential cellular processes in pathogenic fungi.
  • Understanding phosphorylation dynamics is key to addressing fungal infections, particularly concerning drug resistance and virulence.

Purpose of the Study:

  • To systematically map and compare phosphorylation dynamics across WHO-priority fungal pathogens.
  • To identify conserved and divergent phosphorylation events and regulatory networks.
  • To guide the development of novel antifungal drug targets.

Main Methods:

  • High-resolution mass spectrometry-based phosphoproteomics was employed to analyze phosphorylation patterns.
  • Comparative analysis of phosphoproteomic data from *Candida albicans*, *Aspergillus fumigatus*, *Cryptococcus neoformans*, and *Candidozyma auris*.
  • Integration of existing phosphoproteomic datasets to identify conserved regulatory mechanisms.

Main Results:

  • Thousands of phosphorylation events are reprogrammed in response to antifungal drugs, oxidative stress, and temperature changes.
  • A 'conserved-core/divergent-output' organization was identified, with shared kinase hubs (e.g., cAMP-PKA, HOG-MAPK, calcineurin) but diverged downstream networks.
  • Distinct virulence outputs were observed for each pathogen, highlighting species-specific adaptations.

Conclusions:

  • Phosphorylation plays a dynamic role in fungal adaptation, stress response, and antifungal drug resistance.
  • Conserved kinase hubs regulate fundamental processes, while downstream targets dictate pathogen-specific virulence.
  • Phosphoproteomic insights are crucial for prioritizing kinases and phosphatases as next-generation antifungal drug targets.
Keywords:
WHO-priority pathogensantifungal resistancedrug targetmass spectrometryphosphoproteomicssignaling networks

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