Self-association and subcellular localization of Puumala hantavirus envelope proteins
- Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER whileHantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.…
Author details: | Hannah Sabeth Sperber, Robert-William Welke, Roberto Arturo Petazzi, Ronny Bergmann, Matthias Schade, Yechiel Shai, Salvatore ChiantiaORCiDGND, Andreas HerrmannORCiD, Roland SchwarzerORCiD |
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URN: | urn:nbn:de:kobv:517-opus4-425040 |
DOI: | https://doi.org/10.25932/publishup-42504 |
ISSN: | 1866-8372 |
Title of parent work (English): | Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe |
Publication series (Volume number): | Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (648) |
Publication type: | Postprint |
Language: | English |
Date of first publication: | 2019/02/25 |
Publication year: | 2019 |
Publishing institution: | Universität Potsdam |
Release date: | 2019/02/25 |
Tag: | G1; Gn; autophagic clearance; brightness; cytoplasmic tails; electron cryotomography; fever; glycoprotein; nucleocapsid protein Sin-Nombre-Virus |
Issue: | 648 |
Number of pages: | 15 |
Source: | Scientific Reports 9 (2019), Art. 707 DOI 10.1038/s41598-018-36879-y |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät |
DDC classification: | 5 Naturwissenschaften und Mathematik / 50 Naturwissenschaften / 500 Naturwissenschaften und Mathematik |
6 Technik, Medizin, angewandte Wissenschaften / 60 Technik / 600 Technik, Technologie | |
Peer review: | Referiert |
Publishing method: | Open Access |
License (German): | CC-BY - Namensnennung 4.0 International |
External remark: | Bibliographieeintrag der Originalveröffentlichung/Quelle |