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Shiga-like toxin 1 (SLT) from Escherichia coli O157:H7 enters mammalian cells by endocytosis from the cell surface to the endoplasmic reticulum before translocating into the cytosol. Here, SLT was engineered at its N- or C-terminus to carry a peptide derived from influenza virus Matrix protein for delivery to major histocompatibility complex (MHC) class I molecules. We show that SLT N-Ma was capable of sensitising cells for lysis by appropriate cytotoxic T-lymphocytes whilst no killing of SLT-resistant cells was observed. Our results demonstrate that peptide was liberated intracellularly and that retrograde transport of a disarmed cytotoxic protein can intersect the MHC class 1 presentation pathway.

Type

Journal article

Journal

FEBS Lett

Publication Date

18/06/1999

Volume

453

Pages

95 - 99

Keywords

Antigen Presentation, Antigens, Viral, Bacterial Toxins, Biological Transport, Cytotoxicity, Immunologic, Endoplasmic Reticulum, Histocompatibility Antigens Class I, Recombinant Fusion Proteins, Shiga Toxin 1, T-Lymphocytes, Cytotoxic, Viral Matrix Proteins