Function, Architecture, and Biogenesis of Reovirus Replication Neoorganelles

Tenorio, Raquel; Castro, Isabel Fernández de; Knowlton, Jonathan J.; Zamora, Paloma F.; Sutherland, Danica M.; Risco, Cristina; Dermody, Terence S.

doi:10.3390/v11030288

Cited by 30 publications

(21 citation statements)

References 126 publications

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“…Those organelles are referred as viroplasms. They constitute the site of viral genome transcription and replication, as well as the site of packaging of the newly synthesized pregenomic RNA segments into the viral cores [ [75] , [76] , [77] , [78] ]. Viroplasms appear to be spherical and can fuse together [ 79 , 80 ] which indicates that they have liquid properties.…”

Section: Beyond Mnv: Membrane-less Replication Compartments Of Dna Anmentioning

confidence: 99%

Negri bodies and other virus membrane-less replication compartments

Nevers

Albertini

Lagaudrière-Gesbert

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Viruses reshape the organization of the cell interior to achieve different steps of their cellular cycle. Particularly, viral replication and assembly often take place in viral factories where specific viral and cellular proteins as well as nucleic acids concentrate. Viral factories can be either membrane-delimited or devoid of any cellular membranes. In the latter case, they are referred as membrane-less replication compartments. The most emblematic ones are the Negri bodies, which are inclusion bodies that constitute the hallmark of rabies virus infection. Interestingly, Negri bodies and several other viral replication compartments have been shown to arise from a liquid-liquid phase separation process and, thus, constitute a new class of liquid organelles. This is a paradigm shift in the field of virus replication. Here, we review the different aspects of membrane-less virus replication compartments with a focus on the Mononegavirales order and discuss their interactions with the host cell machineries and the cytoskeleton. We particularly examine the interplay between viral factories and the cellular innate immune response, of which several components also form membrane-less condensates in infected cells.

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Section: Beyond Mnv: Membrane-less Replication Compartments Of Dna Anmentioning

confidence: 99%

Negri bodies and other virus membrane-less replication compartments

Nevers

Albertini

Lagaudrière-Gesbert

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…Moreover, in recent years, Tenorio et al (2018Tenorio et al ( , 2019 used light and electron microscopy to demonstrate that reovirus inclusions are membrane-containing structures and that the reovirus σNS and µNS proteins remodel the ER to build neoorganelles for replication. Our results revealed that the depletion of cellular cholesterol inhibited ARV inclusion formation and replication at the post-entry stage in a dose-dependent manner.…”

Section: Discussionmentioning

confidence: 99%

Cholesterol-Rich Lipid Rafts in the Cellular Membrane Play an Essential Role in Avian Reovirus Replication

Wang

Zhang

et al. 2020

Front. Microbiol.

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Cholesterol is an essential component of lipid rafts in cellular plasma membranes. Although lipid rafts have been reported to have several functions in multiple stages of the life cycles of many different enveloped viruses, the mechanisms by which nonenveloped viruses, which lack outer lipid membranes, infect host cells remain unclear. In this study, to investigate the dependence of non-enveloped avian reovirus (ARV) infection on the integrity of cholesterol-rich membrane rafts, methyl-β-cyclodextrin (MβCD) was used to deplete cellular membrane cholesterol at the ARV attachment, entry, and post-entry stages. Treatment with MβCD significantly inhibited ARV replication at both the entry and post-entry stages in a dose-dependent manner, but MβCD had a statistically insignificant effect when it was added at the attachment stage. Moreover, MβCD treatment markedly reduced syncytium formation, which occurs at a relatively late stage of the ARV life cycle and is involved in cell-cell transmission and release. Furthermore, the addition of exogenous cholesterol reversed the effects mentioned above. Colocalization data also showed that the ARV proteins σC, µNS, and p10 prefer to localize to cholesterol-rich lipid raft regions during ARV infection. Altogether, these results suggest that cellular cholesterol in lipid rafts plays a critical role in ARV replication.

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“…While it has been established that the virus factories or VIBs utilized by members of the Reoviridae family are responsible for replication and the assembly of virus particles [30][31][32], crucial stages of these processes remain ill-defined. This includes the egress of virus cores from VIBs, and in the context of BTV, their subsequent associating with the outer capsid proteins VP5 and VP2 to generate mature infectious virus particles that are ready for egress from the cell.…”

Section: Discussionmentioning

confidence: 99%

Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle

Mohl

Kerviel

Labadie

et al. 2020

Viruses

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Members of the Reoviridae family assemble virus factories within the cytoplasm of infected cells to replicate and assemble virus particles. Bluetongue virus (BTV) forms virus inclusion bodies (VIBs) that are aggregates of viral RNA, certain viral proteins, and host factors, and have been shown to be sites of the initial assembly of transcriptionally active virus-like particles. This study sought to characterize the formation, composition, and ultrastructure of VIBs, particularly in relation to virus replication. In this study we have utilized various microscopic techniques, including structured illumination microscopy, and virological assays to show for the first time that the outer capsid protein VP5, which is essential for virus maturation, is also associated with VIBs. The addition of VP5 to assembled virus cores exiting VIBs is required to arrest transcriptionally active core particles, facilitating virus maturation. Furthermore, we observed a time-dependent association of the glycosylated non-structural protein 3 (NS3) with VIBs, and report on the importance of the two polybasic motifs within NS3 that facilitate virus trafficking and egress from infected cells at the plasma membrane. Thus, the presence of VP5 and the dynamic nature of NS3 association with VIBs that we report here provide novel insight into these previously less well-characterized processes.

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Function, Architecture, and Biogenesis of Reovirus Replication Neoorganelles

Cited by 30 publications

References 126 publications

Negri bodies and other virus membrane-less replication compartments

Negri bodies and other virus membrane-less replication compartments

Cholesterol-Rich Lipid Rafts in the Cellular Membrane Play an Essential Role in Avian Reovirus Replication

Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle

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