Isolation and characterization of a 30 kD antifungal protein from seeds of Sorghum bicolor

Res Microbiol. 2006 May;157(4):326-32. doi: 10.1016/j.resmic.2005.09.009. Epub 2005 Oct 24.

Abstract

An antifungal protein of about 30,000 Da was isolated from seeds of Sorghum bicolor L. using chromatographic techniques, including gel filtration, ion exchange, and high-performance liquid chromatography in a reverse-phase column. This protein (termed 30 kD protein) showed a minimal inhibitory concentration of 36 microg/ml for Candida parapsilosis and C. tropicalis, and 18 microg/ml for C. albicans. The 30 kD protein inhibited adherence to the cover glass and formation of a germinative tube of C. albicans at concentrations over 300 and 150 microg/ml, respectively. Transmission electron microscopy of yeast forms of C. albicans after incubation with 18 mug/ml of the 30 kD protein for 24 h revealed marked ultrastructural changes in the fungus. No toxicity of the 30 kD protein to the culture of Hep2 cells at concentrations equal to or less than 1,000 microg/ml was observed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antifungal Agents / isolation & purification
  • Antifungal Agents / pharmacology*
  • Candida / drug effects*
  • Candida / physiology
  • Candida / ultrastructure
  • Candida albicans / drug effects
  • Candida albicans / physiology
  • Candida albicans / ultrastructure
  • Candida tropicalis / drug effects
  • Candida tropicalis / physiology
  • Candida tropicalis / ultrastructure
  • Cell Adhesion / drug effects
  • Glass
  • Microscopy, Electron, Transmission
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology*
  • Seeds / chemistry*
  • Sorghum / chemistry*

Substances

  • Antifungal Agents
  • Plant Proteins