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-Structure paper
Title | A Molecular-Level Account of the Antigenic Hantaviral Surface. |
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Journal, issue, pages | Cell Rep, Vol. 15, Issue 5, Page 959-967, Year 2016 |
Publish date | May 3, 2016 |
Authors | Sai Li / Ilona Rissanen / Antra Zeltina / Jussi Hepojoki / Jayna Raghwani / Karl Harlos / Oliver G Pybus / Juha T Huiskonen / Thomas A Bowden / |
PubMed 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- ...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. |
External links | Cell Rep / PubMed:27117403 / PubMed Central |
Methods | EM (subtomogram averaging) / X-ray diffraction / EM (tomography) |
Resolution | 2.28 - 15.6 Å |
Structure data | EMDB-3364, PDB-5fyn: PDB-5fxu: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | VIRAL PROTEIN / HANTAVIRUS / GN / VIRAL GLYCOPROTEIN / BUNYAVIRUS / PUUMALA VIRUS / GLYCOPROTEIN / TULA VIRUS / MEMBRANE PROTEIN / RECEPTOR BINDING |