Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells

	Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells
	Yang, YH; Jiang, YL; Zhang, J; Wang, L; Bai, XH; Zhang, SJ; Ren, YM; Li, N; Zhang, YH; Zhang, ZY
刊名	PLOS PATHOGENS
	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
内容类型	期刊论文
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.