An octamer of enolase from Streptococcus suis
文献类型：期刊论文
| 作者 | Lu, Qiong1,2; Lu, Hao1; Qi, Jianxun1; Lu, Guangwen1; Gao, George F.1,2,3,4 |
| 刊名 | PROTEIN & CELL
 |
| 出版日期 | 2012-10-01 |
| 卷号 | 3期号:10页码:769-780 |
| 关键词 | enolase octamer Streptococcus suis structure plasminogen binding |
| 英文摘要 | Enolase is a conserved cytoplasmic metalloenzyme existing universally in both eukaryotic and prokaryotic cells. The enzyme can also locate on the cell surface and bind to plasminogen, via which contributing to the mucosal surface localization of the bacterial pathogens and assisting the invasion into the host cells. The functions of the eukaryotic enzymes on the cell surface expression (including T cells, B cells, neutrophils, monocytoes, neuronal cells and epithelial cells) are not known. Streptococcus suis serotype 2 (S. suis 2, SS2) is an important zoonotic pathogen which has recently caused two large-scale outbreaks in southern China with severe streptococcal toxic shock syndrome (STSS) never seen before in human sufferers. We recently identified the SS2 enolase as an important protective antigen which could protect mice from fatal S. suis 2 infection. In this study, a 2.4-angstrom structure of the SS2 enolase is solved, revealing an octameric arrangement in the crystal. We further demonstrated that the enzyme exists exclusively as an octamer in solution via a sedimentation assay. These results indicate that the octamer is the biological unit of SS2 enolase at least in vitro and most likely in vivo as well. This is, to our knowledge, the first comprehensive characterization of the SS2 enolase octamer both structurally and biophysically, and the second octamer enolase structure in addition to that of Streptococcus pneumoniae. We also investigated the plasminogen binding property of the SS2 enzyme. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Cell Biology |
| 研究领域[WOS] | Cell Biology |
| 关键词[WOS] | COLI RNA DEGRADOSOME ; TOXIC-SHOCK-SYNDROME ; ALPHA-ENOLASE ; CRYSTAL-STRUCTURE ; HUMAN PLASMINOGEN ; DIVERGENT EVOLUTION ; BINDING-PROTEIN ; SURFACE ENOLASE ; CELL-SURFACE ; SEROTYPE-2 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000310535700006 |
| 源URL | [http://124.16.173.210/handle/834782/1302]  |
| 专题 | 天津工业生物技术研究所_蛋白质工程与疫苗实验室 高福_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, CAS Key Lab Pathogen Microbiol & Immunol, Inst Microbiol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Chinese Acad Sci, RNIH, Beijing Inst Life Sci, Beijing 100101, Peoples R China 4.Chinese Acad Sci, Lab Prot Engn & Vaccines, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lu, Qiong,Lu, Hao,Qi, Jianxun,et al. An octamer of enolase from Streptococcus suis[J]. PROTEIN & CELL,2012,3(10):769-780. |
| APA | Lu, Qiong,Lu, Hao,Qi, Jianxun,Lu, Guangwen,&Gao, George F..(2012).An octamer of enolase from Streptococcus suis.PROTEIN & CELL,3(10),769-780. |
| MLA | Lu, Qiong,et al."An octamer of enolase from Streptococcus suis".PROTEIN & CELL 3.10(2012):769-780. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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