Identification of a wide range of motifs inhibitory to shiga toxin by affinity-driven screening of customized divalent peptides synthesized on a membrane.

ABSTRACT: Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, binds to target cells through a multivalent interaction between its B-subunit pentamer and the cell surface receptor globotriaosylceramide, resulting in a remarkable increase in its binding affinity. This phenomenon is referred to as the "clustering effect." Previously, we developed a multivalent peptide library that can exert the clustering effect and identified Stx neutralizers with tetravalent peptides by screening this library for high-affinity binding to the specific receptor-binding site of the B subunit. However, this technique yielded only a limited number of binding motifs, with some redundancy in amino acid selectivity. In this study, we established a novel technique to synthesize up to 384 divalen

SUBMITTER: Kato M 

PROVIDER: S-EPMC4292467 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature