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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| Auteurs principaux: | , , , , , , , , |
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| Format: | article |
| Langue: | EN |
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Nature Portfolio
2021
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| Accès en ligne: | https://doaj.org/article/bbdaed596a724d62b77588f4c9ef5bc4 |
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| Résumé: | 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. |
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