Shizuoka University REpository  title image 

SURE: Shizuoka University REpository >
11. 創造科学技術大学院 = Graduate School of Science and Technology >
11. 雑誌論文・記事(Journal Article, Article, Preprint) >

Please use this identifier to cite or link to this item:
Bookmark and Share

Files in This Item:

File Description SizeFormat
100630001.pdf777.28 kBAdobe PDFThumbnail

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
Abstract: 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 OPAC
E-ISSN: 18733700 OPAC
Publisher's DOI: 10.1016/j.phytochem.2009.12.003   
PMID: 20096904
Journal NCID: AA00774558 OPAC ciniib
Textversion: publisher
Appears in Collections:11. 雑誌論文・記事(Journal Article, Article, Preprint)

Google™ Scholar: Cited By - Related - Other Copies

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)

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


DSpace Software Copyright © 2002-2010  Duraspace - Feedback