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  • Title: A mushroom lectin from ascomycete Cordyceps militaris.
    Author: Jung EC, Kim KD, Bae CH, Kim JC, Kim DK, Kim HH.
    Journal: Biochim Biophys Acta; 2007 May; 1770(5):833-8. PubMed ID: 17306462.
    Abstract:
    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 degrees C. Circular dichroism spectrum analysis revealed that CML comprises 27% alpha-helix, 12% beta-sheets, 29% beta-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.
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