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Pathogen adhesins that bind to host cells initiate disease pathogenesis and represent potential therapeutic targets. We have shown previously that the BspC adhesin in Group B<jats:italic>Streptococcus<\/jats:italic>(GBS), the leading cause of bacterial neonatal meningitis, interacts with host vimentin to promote attachment to brain endothelium and disease development. Here we determined that the BspC variable (V-) domain contains the vimentin binding site and promotes GBS adherence to brain endothelium. Site directed mutagenesis identified a binding pocket necessary for GBS host cell interaction and development of meningitis. Using a virtual structure-based drug screen we identified compounds that targeted the V-domain binding pocket, which blocked GBS adherence and entry into the brain<jats:italic>in vivo<\/jats:italic>. These data indicate the utility of targeting the pathogen-host interface to develop anti-virulence therapeutics.<\/jats:p>","DOI":"10.1371\/journal.ppat.1010397","type":"journal-article","created":{"date-parts":[[2022,3,22]],"date-time":"2022-03-22T17:24:08Z","timestamp":1647969848000},"page":"e1010397","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":10,"title":["Targeting the BspC-vimentin interaction to develop anti-virulence therapies during Group B streptococcal meningitis"],"prefix":"10.1371","volume":"18","author":[{"given":"Haider S.","family":"Manzer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricardo I.","family":"Villarreal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4232-6837","authenticated-orcid":true,"given":"Kelly 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