Abstract
A new mannose-recognizing lectin (MOL) was purified on an asialofetuin-column from fruiting bodies of Marasmius oreades grown in Japan. The lectin (MOA) from the fruiting bodies of the same fungi is well known to be a ribosome-inactivating type lectin that recognizes blood-group B sugar. However, in our preliminary investigation, MOA was not found in Japanese fruiting bodies of M. oreades, and instead, MOL was isolated. Gel filtration showed MOL is a homodimer noncovalently associated with two subunits of 13 kDa. The N-terminal sequence of MOL was blocked. The sequence of MOL was determined by cloning from cDNA and by protein sequencing of enzyme-digested peptides. The sequence shows mannose-binding motifs of bulb-type mannose-binding lectins from plants, and similarity to the sequences. Analyses of sugar-binding specificity by hemagglutination inhibition revealed the preference of MOL toward mannose and thyroglobulin, but asialofetuin was the strongest inhibitor of glycoproteins tested. Furthermore, glycan-array analysis showed that the specificity pattern of MOL was different from those of typical mannose-specific lectins. MOL preferred complex–type N-glycans rather than high-mannose N-glycans.
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Abbreviations
- GNA:
-
Galanthus nivalis agglutinin
- LDL:
-
Lyophyllum descades lectin
- MOA:
-
Marasmius oreades agglutinin
- MOL:
-
Marasmius oreades lectin
- RVL:
-
Remusatia vivipara lectin
- TxcL1:
-
Tulipa hybrid lectin 1 with complex specificity
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Shimokawa, M., Fukudome, A., Yamashita, R. et al. Characterization and cloning of GNA-like lectin from the mushroom Marasmius oreades . Glycoconj J 29, 457–465 (2012). https://doi.org/10.1007/s10719-012-9401-6
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DOI: https://doi.org/10.1007/s10719-012-9401-6