Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction
文献类型：期刊论文
| 作者 | Luo, HB; Wu, DL; Shen, C; Chen, KX ; Shen, X; Jiang, HL
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| 刊名 | INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
 |
| 出版日期 | 2006 |
| 卷号 | 38期号:4页码:589-599 |
| 关键词 | protein-protein interaction SARS coronavirus (SARS-CoV) membrane protein nucleocapsid protein surface plasmon resonance (SPR) yeast two-hybrid |
| ISSN号 | 1357-2725 |
| DOI | 10.1016/j.biocel.2005.10.022 |
| 文献子类 | Article |
| 英文摘要 | The severe acute respiratory syndrome coronavirus (SARS-CoV) membrane protein is an abundant virion protein, and its interaction with the nucleocapsid protein is crucial for viral assembly and morphogenesis. Although the interacting region in the nucleocapsid protein was mapped to residues 168-208, the interacting region in the membrane protein and the interaction nature are still unclear. In this work, by using yeast two-hybrid and surface plasmon resonance techniques, the residues 197-221 of the membrane protein and the residues 351-422 of the nucleocapsid protein were determined to be involved in their interaction. Sequence analysis revealed that these two fragments are highly charged at neutral pH, suggesting that their interaction may be of ionic nature. Kinetic assays indicated that the endodomain (aal02-221) of the membrane protein interacts with the nucleocapsid protein with high affinity (K-D=0.55 +/- 0.04 mu M), however, this interaction could be weakened greatly by acidification, higher salt concentration (400mM NaCl) and divalent cation (50mM Ca2+), Which Suggests that electrostatic attraction might play an important role in this interaction. In addition, it is noted that two highly conserved amino acids (L218 and L219) in the membrane protein are not involved in this interaction. Here, we show that electrostatic interactions between the carboxyl termini of SARS-CoV membrane protein and nucleocapsid protein largely mediate the interaction of these two proteins. These results might facilitate therapeutic strategies aiming at the disruption of the association between SARS-CoV membrane and nucleocapsid proteins. (c) 2005 Elsevier Ltd. All rights reserved. |
| WOS关键词 | SARS-ASSOCIATED CORONAVIRUS ; ENVELOPE ; CORE ; BINDS |
| WOS研究方向 | Biochemistry & Molecular Biology ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000235705100011 |
| 出版者 | PERGAMON-ELSEVIER SCIENCE LTD |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273735]  |
| 专题 | 药理学第三研究室 中科院受体结构与功能重点实验室 新药研究国家重点实验室 药物发现与设计中心 |
| 通讯作者 | Jiang, HL |
| 作者单位 | 1.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Shanghai Inst Mat Med,State Key Lab Drug Res,Drug, Shanghai 201203, Peoples R China 2.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China |
| 推荐引用方式 GB/T 7714 | Luo, HB,Wu, DL,Shen, C,et al. Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction[J]. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY,2006,38(4):589-599. |
| APA | Luo, HB,Wu, DL,Shen, C,Chen, KX,Shen, X,&Jiang, HL.(2006).Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY,38(4),589-599. |
| MLA | Luo, HB,et al."Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction".INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 38.4(2006):589-599. |
入库方式： OAI收割
来源：上海药物研究所
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