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Keywords:

  • carbohydrates;
  • glycoproteins;
  • multivalency;
  • protein modifications;
  • protein structures
Thumbnail image of graphical abstract

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.