Structural highlights
Publication Abstract from PubMed
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.
A Molecular-Level Account of the Antigenic Hantaviral Surface.,Li S, Rissanen I, Zeltina A, Hepojoki J, Raghwani J, Harlos K, Pybus OG, Huiskonen JT, Bowden TA Cell Rep. 2016 May 3;15(5):959-67. doi: 10.1016/j.celrep.2016.03.082. Epub 2016, Apr 21. PMID:27117403[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li S, Rissanen I, Zeltina A, Hepojoki J, Raghwani J, Harlos K, Pybus OG, Huiskonen JT, Bowden TA. A Molecular-Level Account of the Antigenic Hantaviral Surface. Cell Rep. 2016 May 3;15(5):959-67. doi: 10.1016/j.celrep.2016.03.082. Epub 2016, Apr 21. PMID:27117403 doi:http://dx.doi.org/10.1016/j.celrep.2016.03.082