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Characterization and cloning of GNA-like lectin from the mushroom Marasmius oreades

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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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Correspondence to Fumio Yagi.

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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

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