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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.