| Autor: |
Luo, Miao, Zhang, Xiang, Zhang, Shaocheng, Zhang, Hongpeng, Yang, Wei, Zhu, Zhongliang, Chen, Ke, Bai, Lei, Wei, Jie, Huang, Ailong, Wang, Deqiang |
| Předmět: |
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| Zdroj: |
PLoS ONE; 1/26/2017, Vol. 12 Issue 1, p1-11, 11p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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