A mushroom lectin from ascomycete Cordyceps militaris

• Published in: Biochimica et biophysica acta Vol. 1770; no. 5; pp. 833 - 838
• Main Authors: Jung, Eui Cha, Kim, Ki Don, Bae, Chan Hyung, Kim, Ju Cheol, Kim, Dae Kyong, Kim, Ha Hyung
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2007
• Subjects: Amino Acid Sequence; Animals; Ascomycete; Ascomycota - chemistry; Chromatography, Gel; Circular Dichroism; Cordyceps - chemistry; Cordyceps militaris; Electrophoresis, Polyacrylamide Gel; Freezing; Hemagglutination - drug effects; Hemagglutination Tests; Hydrogen-Ion Concentration; Lectin; Mice; Mitosis - drug effects; Molecular Sequence Data; Molecular Weight; Mushroom; Oxidation-Reduction; Plant Lectins - chemistry; Plant Lectins - isolation & purification; Plant Lectins - metabolism; Plant Lectins - pharmacology; Protein Binding; Protein Structure, Secondary; Rats; Sialoglycoproteins - pharmacology; Silver Staining; Spleen - cytology; Spleen - drug effects; Lectin; Cordyceps militaris; Ascomycete; Mushroom
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2007.01.005

A mushroom lectin has been purified from ascomycete Cordyceps militaris, which is one of the most popular mushrooms in eastern Asia used as a nutraceutical and in traditional Chinese medicine. This lectin, designated CML, exhibited hemagglutination activity in mouse and rat erythrocytes, but not in human ABO erythrocytes. SDS-PAGE of CML revealed a single band with a molecular mass of 31.0 kDa under both nonreducing and reducing conditions that was stained by silver nitrate, and a 31.4 kDa peak in a Superdex-200 HR gel-filtration column. The hemagglutination activity was inhibited by sialoglycoproteins, but not in by mono- or disaccharides, asialoglycoproteins, or de- O-acetylated glycoprotein. The activity was maximal at pH 6.0–9.1 and at temperatures below 50 °C. Circular dichroism spectrum analysis revealed that CML comprises 27% α-helix, 12% β-sheets, 29% β-turns, and 32% random coils. Its binding specificity and secondary structure are similar to those of a fungal lectin from Arthrobotrys oligospora. However, the N-terminal amino acid sequence of CML differs greatly from those of other lectins. CML exhibits mitogenic activity against mouse splenocytes.