Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells
文献类型：期刊论文
| 作者 | Yang, YH; Jiang, YL; Zhang, J; Wang, L; Bai, XH; Zhang, SJ; Ren, YM; Li, N; Zhang, YH; Zhang, ZY |
| 刊名 | PLOS PATHOGENS
 |
| 出版日期 | 2014 |
| 卷号 | 10期号:6页码:e1004169-e1004169 |
| 通讯作者 | Yang, YH (reprint author), Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China.,cyxing@ustc.edu.cn ; zcz@ustc.edu.cn |
| 英文摘要 | Staphylococcus aureus, a Gram-positive bacterium causes a number of devastating human diseases, such as infective endocarditis, osteomyelitis, septic arthritis and sepsis. S. aureus SraP, a surface-exposed serine-rich repeat glycoprotein (SRRP), is required for the pathogenesis of human infective endocarditis via its ligand-binding region (BR) adhering to human platelets. It remains unclear how SraP interacts with human host. Here we report the 2.05 angstrom crystal structure of the BR of SraP, revealing an extended rod-like architecture of four discrete modules. The N-terminal legume lectin-like module specifically binds to N-acetylneuraminic acid. The second module adopts a beta-grasp fold similar to Ig-binding proteins, whereas the last two tandem repetitive modules resemble eukaryotic cadherins but differ in calcium coordination pattern. Under the conditions tested, small-angle X-ray scattering and molecular dynamic simulation indicated that the three C-terminal modules function as a relatively rigid stem to extend the N-terminal lectin module outwards. Structure-guided mutagenesis analyses, in addition to a recently identified trisaccharide ligand of SraP, enabled us to elucidate that SraP binding to sialylated receptors promotes S. aureus adhesion to and invasion into host epithelial cells. Our findings have thus provided novel structural and functional insights into the SraP-mediated host-pathogen interaction of S. aureus. |
| 学科主题 | Microbiology; Parasitology; Virology |
| 类目[WOS] | Microbiology ; Parasitology ; Virology |
| 关键词[WOS] | PROTEIN-L ; LEGUME LECTIN ; LIGHT-CHAIN ; PEPTOSTREPTOCOCCUS-MAGNUS ; STREPTOCOCCUS-PNEUMONIAE ; MOLECULAR SIMULATION ; SOLUTION SCATTERING ; BINDING-PROTEINS ; SURFACE PROTEIN ; DOMAIN |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000338197400015 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/195]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Yang, YH,Jiang, YL,Zhang, J,et al. Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells[J]. PLOS PATHOGENS,2014,10(6):e1004169-e1004169. |
| APA | Yang, YH.,Jiang, YL.,Zhang, J.,Wang, L.,Bai, XH.,...&Zhou, CZ.(2014).Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells.PLOS PATHOGENS,10(6),e1004169-e1004169. |
| MLA | Yang, YH,et al."Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells".PLOS PATHOGENS 10.6(2014):e1004169-e1004169. |
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