PerspectiveStructural Biology

Unraveling a Flavivirus Enigma

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Science  21 Feb 2014:
Vol. 343, Issue 6173, pp. 849-850
DOI: 10.1126/science.1251249

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There is growing concern about the spread of flaviviruses, such as dengue virus and West Nile virus, to new geographic areas as they can cause major epidemics and represent global public health threats. Controlling these viruses requires a better molecular understanding of how they infect cells. Nonstructural protein 1 (NS1) is perhaps the most enigmatic flavivirus protein. During infection, NS1 exists in two distinct forms, travels to various compartments, decorates itself with different molecular disguises, and plays numerous roles in its infectious cycle and disease pathogenesis (1). How this protein manages all of this has been a puzzle since its discovery in 1970 (2). Crystallizing NS1 has daunted many researchers because of the heterogeneity of its glycosylation and association with lipids, but as reported on page 881 of this issue, Akey et al. (3) have accomplished this task. The unusual structural details revealed about NS1 may guide the design of compounds that inhibit viral replication and provide clues as to how it contributes to different stages of the virus life cycle and disease.