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  1. C. 医薬保健学域; 医学類・薬学類・医薬科学類・保健学類
  2. c 10. 学術雑誌掲載論文(医・保健)
  3. 1. 査読済論文(医学・保健)

Multivalency effects of hemagglutinin component of type B botulinum neurotoxin complex on epithelial barrier disruption

https://doi.org/10.24517/00050508
https://doi.org/10.24517/00050508
0aceb8ec-72b3-4054-960b-5de6fd649758
名前 / ファイル ライセンス アクション
ME-PR-AMATSU-S-80.pdf ME-PR-AMATSU-S-80.pdf (8.0 MB)
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Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-04-16
タイトル
タイトル Multivalency effects of hemagglutinin component of type B botulinum neurotoxin complex on epithelial barrier disruption
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
ID登録
ID登録 10.24517/00050508
ID登録タイプ JaLC
著者 Amatsu, Sho

× Amatsu, Sho

WEKO 74179
e-Rad 90827346

Amatsu, Sho

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Matsumura, Takuhiro

× Matsumura, Takuhiro

WEKO 74180
e-Rad 00456930

Matsumura, Takuhiro

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Yutani, Masahiro

× Yutani, Masahiro

WEKO 74181
e-Rad 20648810

Yutani, Masahiro

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Fujinaga, Yukako

× Fujinaga, Yukako

WEKO 74182
e-Rad 60252954

Fujinaga, Yukako

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著者別表示 阿松, 翔

× 阿松, 翔

阿松, 翔

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松村, 拓大

× 松村, 拓大

松村, 拓大

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油谷, 雅広

× 油谷, 雅広

油谷, 雅広

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藤永, 由佳子

× 藤永, 由佳子

藤永, 由佳子

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提供者所属
内容記述タイプ Other
内容記述 金沢大学医薬保健研究域医学系
書誌情報 Microbiology and Immunology

巻 62, 号 2, p. 80-89, 発行日 2018-02-01
ISSN
収録物識別子タイプ ISSN
収録物識別子 0385-5600
NCID
収録物識別子タイプ NCID
収録物識別子 AA00738350
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 10.1111/1348-0421.12565
出版者
出版者 日本細菌学会 Japanese Society for Bacteriology / Wiley
抄録
内容記述タイプ Abstract
内容記述 Hemagglutinin (HA) is one of the components of botulinum neurotoxin (BoNT) complexes and it promotes the absorption of BoNT through the intestinal epithelium by at least two specific mechanisms: cell surface attachment by carbohydrate binding, and epithelial barrier disruption by E-cadherin binding. It is known that HA forms a three-arm structure, in which each of three protomers has three carbohydrate-binding sites and one E-cadherin-binding site. A three-arm form of HA is considered to bind to these ligands simultaneously. In the present study, we investigated how the multivalency effect of HA influences its barrier-disrupting activity. We prepared type B full-length HA (three-arm form) and mini-HA, which is a deletion mutant lacking the trimer-forming domain. Size-exclusion chromatography analysis showed that mini-HA exists as dimers (two-arm form) and monomers (one-arm form), which are then separated. We examined the multivalency effect of HA on the barrier-disrupting activity, the E-cadherin-binding activity, and the attachment activity to the basolateral cell surface. Our results showed that HA initially attaches to the basal surface of Caco-2 cells by carbohydrate binding and then moves to the lateral cell surface, where the HA acts to disrupt the epithelial barrier. Our results showed that the multivalency effect of HA enhances the barrier-disrupting activity in Caco-2 cells. We found that basal cell surface attachment and binding ability to immobilized E-cadherin were enhanced by the multivalency effect of HA. These results suggest that at least these two factors induced by the multivalency effect of HA cause the enhancement of the barrier-disrupting activity. © 2017 The Societies and John Wiley & Sons Australia, Ltd
内容記述
内容記述タイプ Other
内容記述 Embargo Period 12 months
権利
権利情報 Copyright © 2017 The Societies and John Wiley & Sons Australia, Ltd
著者版フラグ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
関連URI
識別子タイプ URI
関連識別子 https://www.jstage.jst.go.jp/browse/mandi1977/-char/ja/
関連名称 https://www.jstage.jst.go.jp/browse/mandi1977/-char/ja/
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