Published in
Cell Press, Cell Reports, 1(16), p. 278, 2016
DOI: 10.1016/j.celrep.2016.06.039
Cell Press, Cell Reports, 5(15), p. 959-967, 2016
DOI: 10.1016/j.celrep.2016.03.082
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- Cell Press
- Cell Press
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- [www.researchgate.net] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
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A Molecular-Level Account of the Antigenic Hantaviral Surface
,
Antra Zeltina,
Jussi Hepojoki ,
Jayna Raghwani,
Karl Harlos,
Pybus Og,
Oliver G. Pybus ,
Juha T. Huiskonen ,
Huiskonen Jt,
Thomas A. Bowden,
Bowden Ta
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Abstract
Hantaviruses, a geographically diverse group of zoonotic pathogens, initiate cell infection through the concerted action of Gn and Gc viral surface glycoproteins. Here, we describe the high-resolution crystal structure of the antigenic ectodomain of Gn from Puumala hantavirus (PUUV), a causative agent of hemorrhagic fever with renal syndrome. Fitting of PUUV Gn into an electron cryomicroscopy reconstruction of intact Gn-Gc spike complexes from the closely related but non-pathogenic Tula hantavirus localized Gn tetramers to the membrane-distal surface of the virion. The accuracy of the fitting was corroborated by epitope mapping and genetic analysis of available PUUV sequences. Interestingly, Gn exhibits greater non-synonymous sequence diversity than the less accessible Gc, supporting a role of the host humoral immune response in exerting selective pressure on the virus surface. The fold of PUUV Gn is likely to be widely conserved across hantaviruses.