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Structural basis of the interaction between the meningitis pathogenStreptococcus suisadhesin Fhb and its human receptor
- Source :
- FEBS Letters. 590:1384-1392
- Publication Year :
- 2016
- Publisher :
- Wiley, 2016.
-
Abstract
- 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.
- Subjects :
- 0301 basic medicine
Streptococcus suis
Biophysics
Plasma protein binding
Biochemistry
Microbiology
03 medical and health sciences
Structural Biology
Genetics
Humans
Point Mutation
Binding site
Adhesins, Bacterial
Receptor
Molecular Biology
Pathogen
Binding Sites
030102 biochemistry & molecular biology
biology
Chemistry
Trihexosylceramides
Mutagenesis
Isothermal titration calorimetry
Cell Biology
biology.organism_classification
Bacterial adhesin
030104 developmental biology
Protein Binding
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 590
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....35b4c7b3b817439c75e6694e180a843b