- Hantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome.
The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection.
In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe.
We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics of N protein complex formation and investigating co-localization with host proteins as well as the viral glycoproteins Gc and Gn.
We observed formation of large, fibrillar PUUV N protein aggregates, rapidly coalescing from early punctate and spike-like assemblies.
Moreover, we found significant spatial correlation of N with vimentin, actin, and P-bodies but not with microtubules. N constructs also co-localized with Gn and Gc albeitHantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome.
The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection.
In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe.
We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics of N protein complex formation and investigating co-localization with host proteins as well as the viral glycoproteins Gc and Gn.
We observed formation of large, fibrillar PUUV N protein aggregates, rapidly coalescing from early punctate and spike-like assemblies.
Moreover, we found significant spatial correlation of N with vimentin, actin, and P-bodies but not with microtubules. N constructs also co-localized with Gn and Gc albeit not as strongly as the glycoproteins associated with each other.
Finally, we assessed oligomerization of N constructs, observing efficient and concentration-dependent multimerization, with complexes comprising more than 10 individual proteins.…
MetadatenAuthor details: | Robert-William Welke, Hannah Sabeth SperberORCiD, Ronny Bergmann, Amit KoikkarahORCiDGND, Laura Menke, Christian Sieben, Detlev H. Krüger, Salvatore ChiantiaORCiDGND, Andreas HerrmannORCiD, Roland SchwarzerORCiD |
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DOI: | https://doi.org/10.3390/v14030457 |
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ISSN: | 1999-4915 |
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Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/35336863 |
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Title of parent work (English): | Viruses |
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Publisher: | MDPI |
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Place of publishing: | Basel |
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Publication type: | Article |
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Language: | English |
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Date of first publication: | 2022/02/23 |
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Publication year: | 2022 |
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Release date: | 2024/06/17 |
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Tag: | N protein; Number and Brightness; P-bodies; Puumalavirus; actin; hantavirus; macromolecular assemblies; oligomerization; vimentin |
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Volume: | 14 |
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Issue: | 3 |
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Article number: | 457 |
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Number of pages: | 14 |
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Funding institution: | German Research Foundation (DFG) [407961559]; Infect-ERA project; HantaHunt [031L0096A, 031L0096B]; Helmholtz Association; Initiative and; Networking Fund for Infection Research Greifswald (Project HANTadapt);; University of Duisburg-Essen |
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Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
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DDC classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Peer review: | Referiert |
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Publishing method: | Open Access / Gold Open-Access |
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| DOAJ gelistet |
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License (German): | CC-BY - Namensnennung 4.0 International |
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