Structural highlights
Publication Abstract from PubMed
The recently identified Streptococcus suis adhesin 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 Fhb RBD with Gb2, an analog of its receptor, revealing that Gb2 binds in a pocket of the beta 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. This article is protected by copyright. All rights reserved.
Structural Basis of the Interaction between the Meningitis Pathogen Streptococcus suis Adhesin Fhb and its Human Receptor.,Zhang C, Hao H, Yu Y, Kong D, Chen S, Jiang H, Yuan Y, Zheng Y, Yang M, Jiang Y FEBS Lett. 2016 Apr 17. doi: 10.1002/1873-3468.12174. PMID:27086582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang C, Hao H, Yu Y, Kong D, Chen S, Jiang H, Yuan Y, Zheng Y, Yang M, Jiang Y. Structural Basis of the Interaction between the Meningitis Pathogen Streptococcus suis Adhesin Fhb and its Human Receptor. FEBS Lett. 2016 Apr 17. doi: 10.1002/1873-3468.12174. PMID:27086582 doi:http://dx.doi.org/10.1002/1873-3468.12174
