Folding of the SARS coronavirus spike glycoprotein immunological fragment (SARS-S1B): Thermodynamic and kinetic investigation correlating with three-dimensional structural modeling
文献类型：期刊论文
| 作者 | Yu, CY; Gui, CS; Luo, HB; Chen, LL; Zhang, L; Yu, H; Yang, S; Jiang, WH; Shen, JH ; Shen, X
|
| 刊名 | BIOCHEMISTRY
 |
| 出版日期 | 2005-02-08 |
| 卷号 | 44期号:5页码:1453-1463 |
| ISSN号 | 0006-2960 |
| DOI | 10.1021/bi0482396 |
| 文献子类 | Article |
| 英文摘要 | Spike glycoprotein of SARS coronavirus (S protein) plays a pivotal role in SARS coronavirus (SARS_CoV) infection. The immunological fragment of the S protein (Ala251-His641, SARS_S1b) is believed to be essential for SARS_CoV entering the host cell through S protein-ACE-2 interaction. We have quantitatively characterized the thermally induced and GuHCl-induced unfolding features of SARS_S1b using circular dichroism (CD), tryptophan fluorescence, and stopped-flow spectral techniques. For the thermally induced unfolding at pH 7.4, the apparent activation energy (E-app) and transition midpoint temperature (T-m) were determined to be 16.3 +/- 0.2 kcal/rnol and 52.5 +/- 0.4 degreesC, respectively. The CD spectra are not dependent on temperature, suggesting that the secondary structure of SARS_S1b has a relatively high thermal stability. GuHCl strongly affected SARS_S1b structure. Both the CD and fluorescent spectra resulted in consistent values of the transition middle concentration of the denaturant (C-m ranging from 2.30 to 2.45 M) and the standard free energy change (DeltaGdegrees, ranging from 2.1 to 2.5 kcal/mol) for the SARS_S1b unfolding reaction. Moreover, the kinetic features of the chemical unfolding and refolding of SARS_S1b were also characterized using a stopped-flow CD spectral technique. The obvious unfolding reaction rates and relaxation times were determined at various GuHCl concentrations, and the C-m value was obtained, which is very close to the data that resulted from CD and fluorescent spectral determinations. Secondary and three-dimensional structural predictions by homology modeling indicated that SARS_S1b folded as a globular-like structure by beta-sheets and loops; two of the four tryptophans are located on the protein surface, which is in agreement with the tryptophan fluorescence result. The three-dimensional model was also used to explain the recently published experimental results of S1-ACE-2 binding and immunizations. |
| WOS关键词 | ACUTE RESPIRATORY SYNDROME ; MASS-SPECTROMETRIC CHARACTERIZATION ; ANGIOTENSIN-CONVERTING ENZYME-2 ; CIRCULAR-DICHROISM ; MONOCLONAL-ANTIBODIES ; THERMAL-DENATURATION ; NUCLEOCAPSID PROTEIN ; BINDING DOMAIN ; HONG-KONG ; IDENTIFICATION |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000226802000009 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273910]  |
| 专题 | 药理学第三研究室 药物发现与设计中心 |
| 通讯作者 | Shen, X |
| 作者单位 | 1.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Shanghai Inst Plant Physiol & Ecol, Shanghai 200032, Peoples R China 2.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China 3.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci,Shanghai Inst Materia Med, Drug Discovery & Design Ctr,State Key Lab Drug Re, Shanghai 20123, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yu, CY,Gui, CS,Luo, HB,et al. Folding of the SARS coronavirus spike glycoprotein immunological fragment (SARS-S1B): Thermodynamic and kinetic investigation correlating with three-dimensional structural modeling[J]. BIOCHEMISTRY,2005,44(5):1453-1463. |
| APA | Yu, CY.,Gui, CS.,Luo, HB.,Chen, LL.,Zhang, L.,...&Jiang, HL.(2005).Folding of the SARS coronavirus spike glycoprotein immunological fragment (SARS-S1B): Thermodynamic and kinetic investigation correlating with three-dimensional structural modeling.BIOCHEMISTRY,44(5),1453-1463. |
| MLA | Yu, CY,et al."Folding of the SARS coronavirus spike glycoprotein immunological fragment (SARS-S1B): Thermodynamic and kinetic investigation correlating with three-dimensional structural modeling".BIOCHEMISTRY 44.5(2005):1453-1463. |
入库方式： OAI收割
来源：上海药物研究所
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