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However, it is unclear how Fhb interacts with its receptor. Here, we determined the complex structure of factor H\u2010binding protein receptor\u2010binding domain (Fhb <jats:styled-content style=\"fixed-case\">RBD<\/jats:styled-content>) with Gb2, an analog of its receptor, revealing that Gb2 binds in a pocket of the \u03b2 sandwich core domain. We identified the key residues for Fhb <jats:styled-content style=\"fixed-case\">RBD<\/jats:styled-content> receptor binding using mutagenesis and isothermal titration calorimetry. Mutagenesis analyses indicated that Fhb binds to Gb2 mainly through hydrogen and hydrophobic interactions. Our findings provided structural insights into the Fhb\u2010mediated host\u2013pathogen interactions of <jats:italic>S. suis<\/jats:italic>.<\/jats:p>","DOI":"10.1002\/1873-3468.12174","type":"journal-article","created":{"date-parts":[[2016,4,18]],"date-time":"2016-04-18T01:38:52Z","timestamp":1460943532000},"page":"1384-1392","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Structural basis of the interaction between the meningitis pathogen <i>Streptococcus suis<\/i> adhesin Fhb and its human receptor"],"prefix":"10.1002","volume":"590","author":[{"given":"Chunmao","family":"Zhang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Pathogen and Biosecurity Beijing Institute of Microbiology and Epidemiology China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huaijie","family":"Hao","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Pathogen and Biosecurity 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