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

• Published in: Biochimica et biophysica acta Vol. 1770; no. 9; p. 1404
• Main Authors: Thakur, Atul, Rana, Monika, Lakhanpal, T N, Ahmad, Absar, Khan, M I
• Format: Journal Article
• Language: English
• Published: Netherlands 01.09.2007
• Subjects: Hemagglutination Inhibition Tests; Humans; Lectins - chemistry; Lectins - isolation & purification; Polysaccharides - chemistry; Reishi - chemistry; Thermodynamics
• ISSN: 0006-3002
• DOI: 10.1016/j.bbagen.2007.05.009

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.