A subpopulation of arenavirus nucleoprotein localizes to mitochondria

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Baggio , F , Hetzel , U , Nufer , L , Kipar , A & Hepojoki , J 2021 , ' A subpopulation of arenavirus nucleoprotein localizes to mitochondria ' , Scientific Reports , vol. 11 , no. 1 , 21048 . https://doi.org/10.1038/s41598-021-99887-5

Title: A subpopulation of arenavirus nucleoprotein localizes to mitochondria
Author: Baggio, Francesca; Hetzel, Udo; Nufer, Lisbeth; Kipar, Anja; Hepojoki, Jussi
Contributor organization: Veterinary Pathology and Parasitology
Veterinary Biosciences
Helsinki One Health (HOH)
Viral Zoonosis Research Unit
Department of Virology
Medicum
Date: 2021-10-26
Language: eng
Number of pages: 19
Belongs to series: Scientific Reports
ISSN: 2045-2322
DOI: https://doi.org/10.1038/s41598-021-99887-5
URI: http://hdl.handle.net/10138/337313
Abstract: Viruses need cells for their replication and, therefore, ways to hijack cellular functions. Mitochondria play fundamental roles within the cell in metabolism, immunity and regulation of homeostasis due to which some viruses aim to alter mitochondrial functions. Herein we show that the nucleoprotein (NP) of arenaviruses enters the mitochondria of infected cells, affecting the mitochondrial morphology. Reptarenaviruses cause boid inclusion body disease (BIBD) that is characterized, especially in boas, by the formation of cytoplasmic inclusion bodies (IBs) comprising reptarenavirus NP within the infected cells. We initiated this study after observing electron-dense material reminiscent of IBs within the mitochondria of reptarenavirus infected boid cell cultures in an ultrastructural study. We employed immuno-electron microscopy to confirm that the mitochondrial inclusions indeed contain reptarenavirus NP. Mutations to a putative N-terminal mitochondrial targeting signal (MTS), identified via software predictions in both mamm- and reptarenavirus NPs, did not affect the mitochondrial localization of NP, suggesting that it occurs independently of MTS. In support of MTS-independent translocation, we did not detect cleavage of the putative MTSs of arenavirus NPs in reptilian or mammalian cells. Furthermore, in vitro translated NPs could not enter isolated mitochondria, suggesting that the translocation requires cellular factors or conditions. Our findings suggest that MTS-independent mitochondrial translocation of NP is a shared feature among arenaviruses. We speculate that by targeting the mitochondria arenaviruses aim to alter mitochondrial metabolism and homeostasis or affect the cellular defense.
Subject: INCLUSION-BODY DISEASE
PROTEIN IMPORT
VIRUS NUCLEOPROTEIN
INNATE
INHIBITION
SNAKES
IDENTIFICATION
TRANSLOCASE
INDUCTION
RESPONSES
11832 Microbiology and virology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


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