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Part of the series Current Topics in Microbiology and Immunology pp 1-29

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Multivalent Inhibitors of Channel-Forming Bacterial Toxins

  • Goli YaminiAffiliated withDepartment of Biology, The Catholic University of America
  • , Ekaterina M. NestorovichAffiliated withDepartment of Biology, The Catholic University of America Email author 

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Abstract

Rational design of multivalent molecules represents a remarkable modern tool to transform weak non-covalent interactions into strong binding by creating multiple finely-tuned points of contact between multivalent ligands and their supposed multivalent targets. Here, we describe several prominent examples where the multivalent blockers were investigated for their ability to directly obstruct oligomeric channel-forming bacterial exotoxins, such as the pore-forming bacterial toxins and B component of the binary bacterial toxins. We address problems related to the blocker/target symmetry match and nature of the functional groups, as well as chemistry and length of the linkers connecting the functional groups to their multivalent scaffolds. Using the anthrax toxin and AB5 toxin case studies, we briefly review how the oligomeric toxin components can be successfully disabled by the multivalent non-channel-blocking inhibitors, which are based on a variety of multivalent scaffolds.