[Identification of Heparin-binding Proteins on the Cell Surface of Cryptococcus neoformans]

Med Mycol J. 2018;59(3):E47-E52. doi: 10.3314/mmj.18-00001.
[Article in Japanese]

Abstract

Interactions between virulence factors of pathogens and host responses play an important role in the establishment of infection by microbes. We focused on interactions between Cryptococcus neoformans proteins and heparin, which is abundant on host epithelial cells. Surface proteins were extracted and analyzed. Fractions from anion-exchange column chromatography interacted with heparin in surface plasmon resonance analyses. Heparin-binding proteins were purified and then separated by gel electrophoresis; and were identified as transaldolase, glutathione-disulfide reductase, and glyoxal oxidase. These results imply that multifunctional molecules on C. neoformans cells, such as those involved in heparin binding, may play roles in adhesion that trigger responses in the host.

Keywords: Cryptococcus neoformans; heparin; transaldolase.

MeSH terms

  • Alcohol Oxidoreductases / isolation & purification*
  • Alcohol Oxidoreductases / metabolism*
  • Bacterial Outer Membrane Proteins / isolation & purification*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Cryptococcus neoformans / cytology*
  • Cryptococcus neoformans / metabolism*
  • Cryptococcus neoformans / pathogenicity
  • Glutathione Reductase / isolation & purification*
  • Glutathione Reductase / metabolism*
  • Heparin / metabolism*
  • Protein Binding
  • Transaldolase / isolation & purification*
  • Transaldolase / metabolism*
  • Virulence Factors / isolation & purification*
  • Virulence Factors / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Virulence Factors
  • Heparin
  • Alcohol Oxidoreductases
  • glyoxal oxidase
  • Glutathione Reductase
  • Transaldolase