Send to

Choose Destination
PLoS One. 2017 Jan 26;12(1):e0168814. doi: 10.1371/journal.pone.0168814. eCollection 2017.

Crystal Structure of an Invasivity-Associated Domain of SdrE in S. aureus.

Author information

Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), Institute for Viral Hepatitis, Department of Infectious Diseases, The Second Affiliated Hospital, Chongqing Medical University, Chongqing, PR China.
Department of Laboratory Medicine, People's Hospital of YuBei District, YuBei District, Chongqing, People's Republic of China.
Department of Laboratory Medicine, Chongqing Medical University, YixueYuanlu-1, Chongqing, People's Republic of China.
Department of Laboratory Medicine, Hospital of Zhejiang, Xihu District, Hangzhou, People's Republic of China.
School of Life Science, the University of Science and Technology of China, Hefei, Anhui, People's Republic of China.


The surface protein SdrE, a microbial surface components recognizing adhesive matrix molecule (MSCRAMM) family protein expressed on the surface of Staphylococcus aureus (S. aureus), can recognize human complement regulator Factor H and C4BP, thus making it a potentially promising vaccine candidate. In this study, SdrE278-591 was found to directly affect S. aureus host cell invasion. Additionally, the crystal structure of SdrE278-591 at a resolution of 1.25 Å was established, with the three-dimensional structure revealing N2-N3 domains which fold in a manner similar to an IgG fold. Furthermore, a putative ligand binding site located at a conserved charged groove formed by the interface between N2 and N3 domains was identified, with β2 suspected to occupy the ligand recognizing site and undergo a structural rearrangement to allow ligand binding. Overall, these findings have further contributed to the understanding of SdrE as a key factor for S. aureus invasivity and will enable a better understanding of bacterial infection processes.

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Public Library of Science Icon for PubMed Central
Loading ...
Support Center