Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin

Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding. On the other hand, a monomeric peptide containing the same motif occupies the Stx catalytic cavi...

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Autores principales:	Miho Watanabe-Takahashi, Masakazu Tamada, Miki Senda, Masahiro Hibino, Eiko Shimizu, Akiko Okuta, Atsuo Miyazawa, Toshiya Senda, Kiyotaka Nishikawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bbdaed596a724d62b77588f4c9ef5bc4
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spelling	oai:doaj.org-article:bbdaed596a724d62b77588f4c9ef5bc42021-12-02T15:36:12ZIdentification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin10.1038/s42003-021-02068-32399-3642https://doaj.org/article/bbdaed596a724d62b77588f4c9ef5bc42021-05-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02068-3https://doaj.org/toc/2399-3642Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding. On the other hand, a monomeric peptide containing the same motif occupies the Stx catalytic cavity, suggesting that this peptide motif can inhibit two subunits of Stx.Miho Watanabe-TakahashiMasakazu TamadaMiki SendaMasahiro HibinoEiko ShimizuAkiko OkutaAtsuo MiyazawaToshiya SendaKiyotaka NishikawaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-7 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Miho Watanabe-Takahashi Masakazu Tamada Miki Senda Masahiro Hibino Eiko Shimizu Akiko Okuta Atsuo Miyazawa Toshiya Senda Kiyotaka Nishikawa Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
description	Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding. On the other hand, a monomeric peptide containing the same motif occupies the Stx catalytic cavity, suggesting that this peptide motif can inhibit two subunits of Stx.
format	article
author	Miho Watanabe-Takahashi Masakazu Tamada Miki Senda Masahiro Hibino Eiko Shimizu Akiko Okuta Atsuo Miyazawa Toshiya Senda Kiyotaka Nishikawa
author_facet	Miho Watanabe-Takahashi Masakazu Tamada Miki Senda Masahiro Hibino Eiko Shimizu Akiko Okuta Atsuo Miyazawa Toshiya Senda Kiyotaka Nishikawa
author_sort	Miho Watanabe-Takahashi
title	Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
title_short	Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
title_full	Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
title_fullStr	Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
title_full_unstemmed	Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin
title_sort	identification of a peptide motif that potently inhibits two functionally distinct subunits of shiga toxin
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/bbdaed596a724d62b77588f4c9ef5bc4
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_version_	1718386378000039936

Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin

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