Toxic isolectins from the mushroom Boletus venenatus

Horibe, Masashi; Kobayashi, Yuka; Dohra, Hideo; Morita, Tatsuya; Murata, Takeomi; Usui, Taichi; Nakamura-Tsuruta, Sachiko; Kamei, Masugu; Hirabayashi, Jun; Matsuura, Masanori; Yamada, Mina; Saikawa, Yoko; Hashimoto, Kimiko; Nakata, Masaya; Kawagishi, Hirokazu

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Title:	Toxic isolectins from the mushroom Boletus venenatus
Authors:	Horibe, Masashi Kobayashi, Yuka Dohra, Hideo Morita, Tatsuya Murata, Takeomi Usui, Taichi Nakamura-Tsuruta, Sachiko Kamei, Masugu Hirabayashi, Jun Matsuura, Masanori Yamada, Mina Saikawa, Yoko Hashimoto, Kimiko Nakata, Masaya Kawagishi, Hirokazu
Journal Title:	Phytochemistry
Publisher:	Elsevier
Journal Volume:	71
Journal Issue:	5-6
Start Page:	648
End Page:	657
Issue Date:	2010-04
Rights:	Copyright © 2009 Elsevier Ltd All rights reserved.
NDC:	464
Description:	Ingestion of the toxic mushroom Boletus venenatus causes a severe gastrointestinal syndrome, such as nausea, repetitive vomiting, diarrhea, and stomachache. A family of isolectins (B. venenatus lectins, BVLs) was isolated as the toxic principles from the mushroom by successive 80% ammonium sulfate-precipitation, Super Q anion-exchange chromatography, and TSK-gel G3000SW gel filtration. Although BVLs showed a single band on SDS-PAGE, they were further divided into eight isolectins (BVL-1 to -8) by BioAssist Q anion-exchange chromatography. All the isolectins showed lectin activity and had very similar molecular weights as detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis. Among them, BVL-1 and -3 were further characterized with their complete amino acid sequences of 99 amino acids determined and found to be identical to each other. In the hemagglutination inhibition assay, both proteins failed to bind to any mono- or oligo-saccharides tested and showed the same sugar-binding specificity to glycoproteins. Among the glycoproteins examined, asialo-fetuin was the strongest inhibitor. The sugar-binding specificity of each isolectin was also analyzed by using frontal affinity chromatography and surface plasmon resonance analysis, indicating that they recognized N-linked sugar chains, especially Galbeta1-->4GlcNAcbeta1-->4Manbeta1-->4GlcNAcbeta1-->4GlcNAc (Type II) residues in N-linked sugar chains. BVLs ingestion resulted in fatal toxicity in mice upon intraperitoneal administration and caused diarrhea upon oral administration in rats.
ISSN:	00319422
E-ISSN:	18733700
DOI:	10.1016/j.phytochem.2009.12.003
PMID:	20096904
Journal NCID:	AA00774558
Textversion:	publisher
Appears in Collections:	11. 雑誌論文・記事(Journal Article, Article, Preprint)

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Others By: Horibe, Masashi -- Kobayashi, Yuka -- Dohra, Hideo (道羅, 英夫) (ドウラ, ヒデオ) -- Morita, Tatsuya (森田, 達也) (モリタ, タツヤ) -- Murata, Takeomi (村田, 健臣) (ムラタ, タケオミ) -- Usui, Taichi (碓氷, 泰市) (ウスイ, タイイチ) (Usui, Taiichi) -- Nakamura-Tsuruta, Sachiko -- Kamei, Masugu -- Hirabayashi, Jun -- Matsuura, Masanori -- Yamada, Mina -- Saikawa, Yoko -- Hashimoto, Kimiko -- Nakata, Masaya -- Kawagishi, Hirokazu (河岸, 洋和) (カワギシ, ヒロカズ)