Two-Faced Viral Protein
| Autor: | Valda K. Vinson |
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| Rok vydání: | 2014 |
| Předmět: | |
| Zdroj: | Science Signaling. 7 |
| ISSN: | 1937-9145 1945-0877 |
| DOI: | 10.1126/scisignal.2005205 |
| Popis: | 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 . (see the Perspective by Shi) report crystal structures for full-length glycosylated NS1 from West Nile and dengue viruses. The structures show a hexamer composed 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. D. L. Akey, W. C. Brown, S. Dutta, J. Konwerski, J. Jose, T. J. Jurkiw, J. DelProposto, C. M. Ogata, G. Skiniotis, R. J. Kuhn, J. L. Smith, Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system. Science 343 , 881–885 (2014). [Abstract][Full Text] P.-Y. Shi, Unraveling a flavivirus enigma. Science 343 , 849–850 (2014). [Abstract][Full Text] |
| Databáze: | OpenAIRE |
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