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Blocking bacterial adhesion represents a promising therapeutic strategy to treat infections without promoting drug resistance. FrhA contains a peptide\u2010binding domain (PBD) that is key for hemagglutination, human epithelial cell binding, and\n                    <jats:italic>V. cholerae<\/jats:italic>\n                    biofilm formation. Previous studies identified a lead pentapeptide ligand with the sequence Ala\u2010Gly\u2010Tyr\u2010Thr\u2010Asp (AGYTD) that blocks\n                    <jats:italic>V. cholerae<\/jats:italic>\n                    colonization of the mouse small intestine at high micromolar concentrations. In this study, a structure\u2010guided approach identified a minimal D\u2010amino acid\u2010containing tripeptide motif with higher\u00a0affinity for the FrhA\u2010PBD and predicted metabolic stability. Our results contribute to the development of anti\u2010adhesion strategies to combat infections.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:boxed-text content-type=\"box\" position=\"anchor\">\n                      <jats:caption>\n                        <jats:title>Impact statement<\/jats:title>\n                      <\/jats:caption>\n                      <jats:p>\n                        Our study elucidates the molecular basis of peptide recognition by the\n                        <jats:italic>Vibrio cholerae<\/jats:italic>\n                        adhesin FrhA and develops minimal D\u2010amino\u2010acid peptides that block adhesion with nanomolar affinity. These findings advance understanding of RTX adhesins and provide a structural blueprint for next\u2010generation anti\u2010adhesion therapeutics against cholera and related infections.\n                      <\/jats:p>\n                    <\/jats:boxed-text>\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70231","type":"journal-article","created":{"date-parts":[[2025,11,20]],"date-time":"2025-11-20T08:42:37Z","timestamp":1763628157000},"page":"631-643","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Peptide\u2010based ligand antagonists block a\n                    <i>Vibrio cholerae<\/i>\n                    adhesin"],"prefix":"10.1002","volume":"600","author":[{"given":"Mingyu","family":"Wang","sequence":"first","affiliation":[{"name":"Department of Anatomy and Cell Biology McGill University  Montreal Canada"},{"name":"Centre de recherche en biologie structurale McGill University  Montreal 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