Identification of heparin‐binding proteins expressed on <i>Trichosporon asahii</i> cell surface

DOI Web Site 参考文献25件
  • Tomoe Ichikawa
    Department of Microbiology and Immunology, Faculty of Pharmaceutical Sciences Shonan University of Medical Sciences Yokohama Japan
  • Yuka Ikeda
    Meiji Pharmaceutical University Kiyose Japan
  • Jumpei Sadanaga
    Meiji Pharmaceutical University Kiyose Japan
  • Ayano Kikuchi
    Meiji Pharmaceutical University Kiyose Japan
  • Kohei Kawamura
    Meiji Pharmaceutical University Kiyose Japan
  • Reiko Ikeda
    Meiji Pharmaceutical University Kiyose Japan
  • Yoshio Ishibashi
    Department of Microbiology and Immunology, Faculty of Pharmaceutical Sciences Shonan University of Medical Sciences Yokohama Japan

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<jats:title>Abstract</jats:title><jats:p><jats:italic>Trichosporon asahii</jats:italic> is a pathogenic yeast that cause trichosporonosis. <jats:italic>T. asahii</jats:italic> exhibits several colony morphologies, such as white (W)‐ or off‐white (O)‐type, which may affect virulence. In this study, we compared the expression pattern of heparin‐binding proteins in various colony morphologies and identified heparin‐binding protein in <jats:italic>T. asahii</jats:italic>. Surface plasmon resonance analysis revealed that cell surface molecules attached more strongly to heparin in W‐ than O‐type cells. We purified and identified a heparin‐binding protein strongly expressed in W‐type cells using heparin‐Sepharose beads, named it heparin‐binding protein 1 (HepBP1), and expressed Flag‐tagged HepBP1 in mammalian cells. The heparin‐binding ability of Flag‐tagged HepBP1 was confirmed by pulldown assay using heparin‐Sepharose beads. Thus, HepBP1 is a heparin‐binding protein on <jats:italic>T. asahii</jats:italic> cell surface. These results suggest that several <jats:italic>T. asahii</jats:italic> cell surface proteins interact with glycosaminoglycans; therefore, they could contribute to infection.</jats:p>

収録刊行物

  • Yeast

    Yeast 41 (5), 299-306, 2024-01-31

    Wiley

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