5FXU

Crystal Structure of Puumala virus Gn glycoprotein ectodomain

Summary for 5FXU

• Entry DOI: 10.2210/pdb5fxu/pdb
• Descriptor: ENVELOPE POLYPROTEIN, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: hantavirus, gn, viral glycoprotein, bunyavirus, puumala virus, glycoprotein, viral protein
• Biological source: Puumala orthohantavirus
• Total number of polymer chains: 2
• Total formula weight: 82307.16

Authors

Li, S.,Rissanen, I.,Zeltina, A.,Hepojoki, J.,Raghwani, J.,Harlos, K.,Pybus, O.G.,Huiskonen, J.T.,Bowden, T.A. (deposition date: 2016-03-02, release date: 2016-05-18, Last modification date: 2024-11-06)

Primary citation

Li, S.,Rissanen, I.,Zeltina, A.,Hepojoki, J.,Raghwani, J.,Harlos, K.,Pybus, O.G.,Huiskonen, J.T.,Bowden, T.A.
A Molecular-Level Account of the Antigenic Hantaviral Surface.
Cell Rep., 15:959-, 2016

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-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.

PubMed: 27117403
DOI: 10.1016/J.CELREP.2016.03.082

Experimental method

X-RAY DIFFRACTION (2.28 Å)