Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis
文献类型：期刊论文
| 作者 | Shen, X; Xue, JH; Yu, CY; Luo, HB; Qin, L; Yu, XJ; Chen, J; Chen, LL; Xiong, B; Yue, LD |
| 刊名 | ACTA PHARMACOLOGICA SINICA
 |
| 出版日期 | 2003 |
| 卷号 | 24期号:6页码:505-511 |
| 关键词 | severe acute respiratory syndrome (SARS) small envelope protein gene expression bioinformatics circular dichroism spectroscopy |
| 通讯作者 | Shen, X (reprint author), Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai Inst Biol Sci, State Key Lab Drug Res,Drug Discovery & Design Ct, Shanghai 201203, Peoples R China., |
| 英文摘要 | AIM: To obtain the pure sample of SARS small envelope E protein (SARS E protein), study its properties and analyze its possible functions. METHODS: The plasmid of SARS E protein was constructed by the polymerase chain reaction (PCR), and the protein was expressed in the E coli strain. The secondary structure feature of the protein was determined by circular dichroism (CD) technique. The possible functions of this protein were annotated by bioinformatics methods, and its possible three-dimensional model was constructed by molecular modeling. RESULTS: The pure sample of SARS E protein was obtained. The secondary structure feature derived from CD determination is similar to that from the secondary structure prediction. Bioinformatics analysis indicated that the key residues of SARS E protein were much conserved compared to the E proteins of other coronaviruses. In particular, the primary amino acid sequence of SARS E protein is much more similar to that of murine hepatitis virus (MHV) and other mammal coronaviruses. The transmembrane (TM) segment of the SARS E protein is relatively more conserved in the whole protein than other regions. CONCLUSION: The success of expressing the SARS E protein is a good starting point for investigating the structure and functions of this protein and SARS coronavirus itself as well. The SARS E protein may fold in water solution in a similar way as it in membrane-water mixed environment. It is possible that beta-sheet I of the SARS E protein interacts with the membrane surface via hydrogen bonding, this beta-sheet may uncoil to a random structure in water solution. |
| 学科主题 | Chemistry; Pharmacology & Pharmacy |
| 类目[WOS] | Chemistry, Multidisciplinary ; Pharmacology & Pharmacy |
| 关键词[WOS] | MURINE CORONAVIRUS ; MEMBRANE-PROTEIN ; VIRUS ; PARTICLES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000183575100004 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2317]  |
| 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 | Shen, X,Xue, JH,Yu, CY,et al. Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis[J]. ACTA PHARMACOLOGICA SINICA,2003,24(6):505-511. |
| APA | Shen, X.,Xue, JH.,Yu, CY.,Luo, HB.,Qin, L.,...&Jiang, HL.(2003).Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis.ACTA PHARMACOLOGICA SINICA,24(6),505-511. |
| MLA | Shen, X,et al."Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis".ACTA PHARMACOLOGICA SINICA 24.6(2003):505-511. |
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