Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

Authors

Giulia Opassi, João C Encarnação, Valeria Napolitano, Grzegorz Dubin, Grzegorz Popowicz, Karl Andersson, U Helena Danielson

Published in

FEBS letters. Jul 04, 2026. Epub Jul 04, 2026.

Abstract

Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug carriers. Using time-resolved biosensor-based assays we examined the interaction between a variety of STxA peptides (varying in length and end groups) and the cell receptor binding subunit (STxB). Peptides which bound STxB included the C-terminal α-helix protruding into the interior of STxB and the ß-strands binding to its surface. Specifically, the C-terminal 26-mer resulted in a stable complex in a physiologically relevant pH range for drug delivery. Real-time cell-binding analysis showed that the peptide-STxB complex binds to and is internalized by Gb3-overexpressing cancer cell lines with surface-exposed Gb3 receptors. It highlights STxA-derived peptides as potential as drug carriers.

PMID:
42400325
Bibliographic data and abstract were imported from PubMed on 04 Jul 2026.

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