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

Branson Thomas R. | Zendy; McAllister Tom E. | Zendy; GarciaHartjes Jaime | Zendy; Fascione Martin A. | Zendy; Ross James F. | Zendy; Warriner Stuart L. | Zendy; Wennekes Tom | Zendy; Zuilhof Han | Zendy; Turnbull W. Bruce | Zendy

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

Author(s) -

Branson Thomas R.,

McAllister Tom E.,

GarciaHartjes Jaime,

Fascione Martin A.,

Ross James F.,

Warriner Stuart L.,

Wennekes Tom,

Zuilhof Han,

Turnbull W. Bruce

Publication year - 2014

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201405672

Subject(s) - cholera toxin , protein subunit , toxin , chemistry , mutant , valency , clostridium difficile toxin b , clostridium difficile toxin a , microbiology and biotechnology , biochemistry , biology , philosophy , gene , linguistics , clostridium difficile , antibiotics

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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