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Structural basis of the interaction between the meningitis pathogen Streptococcus suis adhesin Fhb and its human receptor
Author(s) -
Zhang Chunmao,
Hao Huaijie,
Yu You,
Kong Decong,
Chen Shaolong,
Jiang Hua,
Yuan Yuan,
Zheng Yuling,
Yang Maojun,
Jiang Yongqiang
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12174
Subject(s) - isothermal titration calorimetry , streptococcus suis , mutagenesis , bacterial adhesin , receptor , biology , pathogen , binding site , chemistry , microbiology and biotechnology , computational biology , biophysics , genetics , mutation , biochemistry , virulence , gene
The recently identified Streptococcus suis adhesin factor H‐binding protein (Fhb) targets the host cellular receptor glycolipid GbO3 through its N terminus. However, it is unclear how Fhb interacts with its receptor. Here, we determined the complex structure of factor H‐binding protein receptor‐binding domain (Fhb RBD ) with Gb2, an analog of its receptor, revealing that Gb2 binds in a pocket of the β sandwich core domain. We identified the key residues for Fhb RBD 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‐mediated host–pathogen interactions of S. suis .