Structural Insights into the Interaction between a Potent Anti-inflammatory Protein, Viral CC Chemokine Inhibitor (vCCI), and the Human CC Chemokine, Eotaxin-1
文献类型：期刊论文
| 作者 | Kuo, NW; Gao, YG; Schill, MS; Isern, N; Dupureur, CM; LiWang, PJ |
| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
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| 出版日期 | 2014 |
| 卷号 | 289期号:10页码:6592-6603 |
| 关键词 | Biophysics Chemokines Molecular Docking NMR Protein-Protein Interactions Anti-inflammatory Protein Chemokine-binding Protein Eotaxin Fluorescence Anisotropy vCCI |
| 通讯作者 | LiWang, PJ (reprint author), Univ Calif, Dept Mol Cell Biol, 5200 N Lake Rd, Merced, CA 95343 USA.,pliwang@ucmerced.edu |
| 英文摘要 | Background: The mechanism used by viral protein vCCI to tightly bind to many CC chemokines is not known. Results: Specific positively charged residues in the chemokine eotaxin-1 mediate binding to vCCI. Conclusion: Basic residues in the chemokine each provide incremental affinity for vCCI. Significance: This work shows how vCCI can bind a variety of CC chemokines. Chemokines play important roles in the immune system, not only recruiting leukocytes to the site of infection and inflammation but also guiding cell homing and cell development. The soluble poxvirus-encoded protein viral CC chemokine inhibitor (vCCI), a CC chemokine inhibitor, can bind to human CC chemokines tightly to impair the host immune defense. This protein has no known homologs in eukaryotes and may represent a potent method to stop inflammation. Previously, our structure of the vCCIMIP-1 (macrophage inflammatory protein-1) complex indicated that vCCI uses negatively charged residues in -sheet II to interact with positively charged residues in the MIP-1 N terminus, 20s region and 40s loop. However, the interactions between vCCI and other CC chemokines have not yet been fully explored. Here, we used NMR and fluorescence anisotropy to study the interaction between vCCI and eotaxin-1 (CCL11), a CC chemokine that is an important factor in the asthma response. NMR results reveal that the binding pattern is very similar to the vCCIMIP-1 complex and suggest that electrostatic interactions provide a major contribution to binding. Fluorescence anisotropy results on variants of eotaxin-1 further confirm the critical roles of the charged residues in eotaxin-1. In addition, the binding affinity between vCCI and other wild type CC chemokines, MCP-1 (monocyte chemoattractant protein-1), MIP-1, and RANTES (regulated on activation normal T cell expressed and secreted), were determined as 1.1, 1.2, and 0.22 nm, respectively. To our knowledge, this is the first work quantitatively measuring the binding affinity between vCCI and multiple CC chemokines. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | TRIPLE-RESONANCE EXPERIMENTS ; BINDING-PROTEIN ; VACCINIA VIRUS ; DECOY RECEPTOR ; CRYSTAL-STRUCTURE ; WEB SERVER ; INFLAMMATION ; RECOGNITION ; BLOCKADE ; DETERMINANTS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000332389400024 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/238]  |
| 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 | Kuo, NW,Gao, YG,Schill, MS,et al. Structural Insights into the Interaction between a Potent Anti-inflammatory Protein, Viral CC Chemokine Inhibitor (vCCI), and the Human CC Chemokine, Eotaxin-1[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2014,289(10):6592-6603. |
| APA | Kuo, NW,Gao, YG,Schill, MS,Isern, N,Dupureur, CM,&LiWang, PJ.(2014).Structural Insights into the Interaction between a Potent Anti-inflammatory Protein, Viral CC Chemokine Inhibitor (vCCI), and the Human CC Chemokine, Eotaxin-1.JOURNAL OF BIOLOGICAL CHEMISTRY,289(10),6592-6603. |
| MLA | Kuo, NW,et al."Structural Insights into the Interaction between a Potent Anti-inflammatory Protein, Viral CC Chemokine Inhibitor (vCCI), and the Human CC Chemokine, Eotaxin-1".JOURNAL OF BIOLOGICAL CHEMISTRY 289.10(2014):6592-6603. |
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