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Interaction of Host Proteins with Cell Surface Molecules of the Pathogenic Yeast Trichosporon asahii

Tomoe Ichikawa1, Misato Okumura2, Tomoya Mizumura2

  • 1Department of Microbiology and Immunology, Faculty of Pharmaceutical Sciences, Shonan University of Medical Sciences.

Medical Mycology Journal
|May 31, 2023
PubMed

Insights

This study identified key host proteins, including serum albumin, alpha-1-antitrypsin (AAT), and vitronectin (VTN), that bind to the pathogenic yeast Trichosporon asahii. These interactions may be crucial for T. asahii infection mechanisms in vulnerable patients.

Area of Science:

  • Mycology
  • Immunology
  • Biochemistry

Background:

  • Trichosporon asahii is an invasive yeast causing infections in immunocompromised individuals.
  • The specific factors driving T. asahii infections are not fully understood.
  • Adhesins are known virulence factors in pathogenic fungi, prompting investigation into host-fungal interactions.

Purpose of the Study:

  • To identify host proteins that interact with the cell surface of Trichosporon asahii.
  • To elucidate potential mechanisms of T. asahii pathogenesis through host-pathogen protein binding.

Main Methods:

  • Screening of yeast-binding serum proteins using pull-down assays with Trichosporon asahii and Candida albicans.
  • Investigating interactions between T. asahii cell surface molecules (CSM) and specific human proteins (vitronectin, fibronectin, fetuin-A, alpha-1-antitrypsin).
  • Utilizing surface plasmon resonance (SPR) and pull-down assays to confirm protein interactions.

Main Results:

  • Serum albumin and elongation factor 2 were identified as yeast-binding serum proteins.
  • Serum albumin, alpha-1-antitrypsin (AAT), and vitronectin (VTN) were confirmed to interact with T. asahii.
  • Interactions were validated using both SPR and pull-down assay methods.

Conclusions:

  • Several host proteins, including serum albumin, AAT, and VTN, bind to the T. asahii cell surface.
  • These identified protein interactions suggest a role in the infection mechanisms of T. asahii.
  • Further research into these interactions could reveal novel therapeutic targets for T. asahii infections.
Keywords:
Trichosporon asahiialpha-1 antitrypsincell surface moleculesvitronectin

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