Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system
| Autor: | David L. Akey, Georgios Skiniotis, Craig M. Ogata, Thomas J. Jurkiw, Richard J. Kuhn, Joyce Jose, Somnath Dutta, Jamie R. Konwerski, W. Clay Brown, Janet L. Smith, James Delproposto |
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| Rok vydání: | 2014 |
| Předmět: |
Viral protein
Protein Conformation Lipid Bilayers Random hexamer Viral Nonstructural Proteins medicine.disease_cause Crystallography X-Ray Dengue fever Cell membrane DEAD-box RNA Helicases Immune system Protein structure medicine Humans Receptors Immunologic Lipid bilayer Multidisciplinary biology Cell Membrane biology.organism_classification medicine.disease Virology Immunity Innate Flavivirus Microscopy Electron medicine.anatomical_structure Immune System DEAD Box Protein 58 Protein Multimerization Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Science (New York, N.Y.). 343(6173) |
| ISSN: | 1095-9203 |
| Popis: | Two-Faced Viral Protein Flaviviruses cause human diseases such as West Nile fever and dengue fever. The flavivirus nonstructural protein 1 (NS1) has multiple functions in flavivirus biology and is a target for vaccine development. Dimeric NS1 is essential for replication of the viral genome inside host cells, while hexameric NS1 is secreted and plays a role in evasion of the immune system. Akey et al. (p. 881 , published online 6 February; see the Perspective by Shi ) report crystal structures for full-length glycosylated NS1 from West Nile and dengue viruses. The structures show a hexamer comprised of three dimers. The structural analysis together with liposome and mutational studies identify a membrane interacting surface on one face of the dimer and an immune evasion surface on the other. |
| Databáze: | OpenAIRE |
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