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.…
Verfasserangaben: | 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 |
Titel des übergeordneten Werks (Englisch): | Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe |
Schriftenreihe (Bandnummer): | Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (648) |
Publikationstyp: | Postprint |
Sprache: | Englisch |
Datum der Erstveröffentlichung: | 25.02.2019 |
Erscheinungsjahr: | 2019 |
Veröffentlichende Institution: | Universität Potsdam |
Datum der Freischaltung: | 25.02.2019 |
Freies Schlagwort / Tag: | G1; Gn; autophagic clearance; brightness; cytoplasmic tails; electron cryotomography; fever; glycoprotein; nucleocapsid protein Sin-Nombre-Virus |
Ausgabe: | 648 |
Seitenanzahl: | 15 |
Quelle: | Scientific Reports 9 (2019), Art. 707 DOI 10.1038/s41598-018-36879-y |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät |
DDC-Klassifikation: | 5 Naturwissenschaften und Mathematik / 50 Naturwissenschaften / 500 Naturwissenschaften und Mathematik |
6 Technik, Medizin, angewandte Wissenschaften / 60 Technik / 600 Technik, Technologie | |
Peer Review: | Referiert |
Publikationsweg: | Open Access |
Lizenz (Deutsch): | CC-BY - Namensnennung 4.0 International |
Externe Anmerkung: | Bibliographieeintrag der Originalveröffentlichung/Quelle |