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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.

Original publication

DOI

10.1016/j.celrep.2016.03.082

Type

Journal article

Journal

Cell Rep

Publication Date

03/05/2016

Volume

15

Pages

959 - 967

Keywords

Antibodies, Viral, Antigens, Viral, Cryoelectron Microscopy, Crystallography, X-Ray, Epitopes, Glycoproteins, HEK293 Cells, Humans, Models, Molecular, Polysaccharides, Protein Domains, Puumala virus, Surface Properties, Viral Proteins, Virion