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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kuo, Nai-wei Isern, Nancy Gao, Yong-guang Dupureur, Cynthia M. Liwang, Patricia J. Schill, Megan S. |
| Description | Author Affiliation: Kuo NW ( From the Molecular Cell Biology, University of California, Merced, California 95343.) |
| Abstract | 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 vCCI·MIP-1ß (macrophage inflammatory protein-1ß) complex indicated that vCCI uses negatively charged residues in ß-sheet II to interact with positively charged residues in the MIP-1ß 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 vCCI·MIP-1ß 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-1ß, 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. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 10 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-03-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Chemokine CCL11 Immunology Viral Proteins Virulence Factors Amino Acid Sequence Chemistry Genetics Chemokine CCL2 Chemokine CCL4 Chemokine CCL5 Inflammation Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Structure, Secondary Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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