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

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• 作者：Michiko Shimokawa (1)
  Ayako Fukudome (2)
  Ryoko Yamashita (2)
  Yuji Minami (2)
  Fumio Yagi (2) fyagi@chem.agri.kagoshima-u.ac.jp
  Hiroaki Tateno (3)
  Jun Hirabayashi (3)
• 关键词：Keyword Fungus – ; GNA ; like – ; Lectin – ; Mannose ; binding – ; Marasmius oreades
• 刊名：Glycoconjugate Journal
• 出版年：2012
• 出版时间：October 2012
• 年：2012
• 卷：29
• 期：7
• 页码：457-465
• 全文大小：506.5 KB
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• 作者单位：1. Department of Applied Biological Chemistry, The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065 Japan2. Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065 Japan3. Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Central 2, 1-1-1 Umezono, Ibaraki, 305-8568 Japan
• ISSN：1573-4986

文摘

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.