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5FYN

Sub-tomogram averaging of Tula virus glycoprotein spike

Summary for 5FYN
Entry DOI10.2210/pdb5fyn/pdb
EMDB information3364
DescriptorPUUMALA VIRUS GN GLYCOPROTEIN, 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, ... (4 entities in total)
Functional Keywordsviral protein, tula virus, membrane protein, glycoprotein, hantavirus, bunyavirus, receptor binding
Biological sourcePUUMALA VIRUS
Total number of polymer chains2
Total formula weight80074.75
Authors
Li, S.,Rissanen, I.,Zeltina, A.,Hepojoki, J.,Raghwani, J.,Harlos, K.,Pybus, O.G.,Huiskonen, J.T.,Bowden, T.A. (deposition date: 2016-03-08, release date: 2016-06-08, Last modification date: 2024-11-13)
Primary citationLi, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (15.6 Å)
Structure validation

243531

数据于2025-10-22公开中

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