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Opassi, G.* ; Encarnação, J.C.* ; Napolitano, V.* ; Dubin, G.* ; Popowicz, G.M. ; Andersson, K.* ; Danielson, U.H.*

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

FEBS Lett., DOI: 10.1002/1873-3468.70403 (2026)
Publ. Version/Full Text DOI PMC
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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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Gb3 Receptors ; Shiga Toxin ; Biosensor ; Grating‐coupled Interferometry ; Real‐time Cell‐binding Assay ; Surface Plasmon Resonance
ISSN (print) / ISBN 0014-5793
e-ISSN 1873-3468
Journal FEBS Letters
Publisher Wiley
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)