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-Structure paper
タイトル | A Molecular-Level Account of the Antigenic Hantaviral Surface. |
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ジャーナル・号・ページ | Cell Rep, Vol. 15, Issue 5, Page 959-967, Year 2016 |
掲載日 | 2016年5月3日 |
著者 | Sai Li / Ilona Rissanen / Antra Zeltina / Jussi Hepojoki / Jayna Raghwani / Karl Harlos / Oliver G Pybus / Juha T Huiskonen / Thomas A Bowden / |
PubMed 要旨 | 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. |
リンク | Cell Rep / PubMed:27117403 / PubMed Central |
手法 | EM (サブトモグラム平均) / X線回折 / EM (トモグラフィー) |
解像度 | 2.28 - 15.6 Å |
構造データ | EMDB-3364, PDB-5fyn: PDB-5fxu: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / HANTAVIRUS / GN / VIRAL GLYCOPROTEIN / BUNYAVIRUS / PUUMALA VIRUS / GLYCOPROTEIN / TULA VIRUS / MEMBRANE PROTEIN / RECEPTOR BINDING |