ArticleCommunications biology2021
Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Novel endogenous protein-based strategies to inhibit clinically relevant bacterial AB-type toxins including pertussis toxin.Archives of toxicology · 2026Review
- Clustered peptide regulating the multivalent interaction between RANK and TRAF6 inhibits osteoclastogenesis by fine-tuning signals.Communications biology · 2025Article
- Article
- Utilizing Adenovirus Knob Proteins as Carriers in Cancer Gene Therapy Amidst the Presence of Anti-Knob Antibodies.International journal of molecular sciences · 2024Article
- Synthetic phage-based approach for sensitive and specific detection of Escherichia coli O157.Communications biology · 2024Article
- A tailored tetravalent peptide displays dual functions to inhibit amyloid β production and aggregation.Communications biology · 2023Article
- A unique peptide-based pharmacophore identifies an inhibitory compound against the A-subunit of Shiga toxin.Scientific reports · 2022Article
- Therapeutic Uses of Bacterial Subunit Toxins.Toxins · 2021Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shiga toxin (Stx) is a major virulence factor of enterohemorrhagic Escherichia coli, which causes fatal systemic complications. Here, we identified a tetravalent peptide that inhibited Stx by targeting its receptor-binding, B-subunit pentamer through a multivalent interaction. A monomeric peptide with the same motif, however, did not bind to the B-subunit pentamer. Instead, the monomer inhibited cytotoxicity with remarkable potency by binding to the catalytic A-subunit. An X-ray crystal structure analysis to 1.6 Å resolution revealed that the monomeric peptide fully occupied the catalytic cavity, interacting with Glu167 and Arg170, both of which are essential for catalytic activity. Thus, the peptide motif demonstrated potent inhibition of two functionally distinct subunits of Stx.
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Registered trials
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