Inside Cover: A Protein-Based Pentavalent Inhibitor of the Cholera Toxin B-Subunit (Angew. Chem. Int. Ed. 32/2014)

Authors

  • Dr. Thomas R. Branson,

    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
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  • Dr. Tom E. McAllister,

    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
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  • Jaime Garcia-Hartjes,

    1. Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703 HB Wageningen (The Netherlands)
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  • Dr. Martin A. Fascione,

    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
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  • Dr. James F. Ross,

    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
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  • Dr. Stuart L. Warriner,

    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
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  • Dr. Tom Wennekes,

    1. Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703 HB Wageningen (The Netherlands)
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  • Prof. Han Zuilhof,

    1. Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703 HB Wageningen (The Netherlands)
    2. Department of Chemical and Materials Engineering, King Abdulaziz University, Jeddah (Saudi-Arabia)
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  • Dr. W. Bruce Turnbull

    Corresponding author
    1. School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)
    • School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT (UK)===

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Abstract

original image

The cholera toxin B-subunit has been re-engineered to create a potent inhibitor of the parent toxin. Toxin adhesion can be blocked by a nonbinding mutant of the B subunit, which was modified with five copies of the carbohydrate ligand, as shown by W. B Turnbull and co-workers in their Communication on page 8323 ff. Site-specific modification of a protein scaffold that is matched in both size and valency to the target toxin may become a general strategy for inhibitor design.

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