Purification and characterization of lectin from fruiting body of Ganoderma lucidum: lectin from Ganoderma lucidum

Biochim Biophys Acta. 2007 Sep;1770(9):1404-12. doi: 10.1016/j.bbagen.2007.05.009. Epub 2007 Jun 14.


A novel 114 kDa hexameric lectin was purified from the fruiting bodies of the mushroom Ganoderma lucidum. Biochemical characterization revealed it to be a glycoprotein having 9.3% neutral sugar and it showed hemagglutinating activity on pronase treated human erythrocytes. The lectin was stable in the pH range of 5-9 and temperature up to 50 degrees C. The hemagglutinating activity was inhibited by glycoproteins that possessed N-as well as O-linked glycans. Chemical modification of the G. lucidum lectin revealed contribution of tryptophan and lysine to binding activity. The thermodynamics of binding of bi- and triantennary N-glycans to G. lucidum lectin was studied by spectrofluorimetry. The lectin showed very high affinity for asialo N-linked triantennary glycan and a preference for asialo glycans over sialylated glycans. The binding was accompanied with a large negative change in enthalpy as well as entropy, indicating primarily involvement of polar hydrogen, van der Waals and hydrophobic interactions in the binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hemagglutination Inhibition Tests
  • Humans
  • Lectins / chemistry
  • Lectins / isolation & purification*
  • Polysaccharides / chemistry
  • Reishi / chemistry*
  • Thermodynamics


  • Lectins
  • Polysaccharides