Virus Factories and Mini-Organelles Generated for Virus Replication

Wileman, Tom; Netherton, Christopher L.; Powell, Penny P.

doi:10.1016/b978-0-12-394447-4.20102-8

Cited by 6 publications

(3 citation statements)

References 45 publications

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“…Some viruses have evolved massive strategies in their arms race with their host cells: to protect themselves from host recognition of unique virally induced molecules, such as double-stranded RNA, many viruses have evolved to form viral factories (i.e., cellular mini-organelles where most replication and assembly steps are executed in a concealed space) [17,18]. The fact that viral factories are built from host-cell components illustrates viruses' agility in recruiting host-cell proteins and reorganizing subcellular compartments, as well as in arranging membraneless organelles [19], liquid-like phase separations [20], and aggresome-like complexes shielded by a vimentincontaining cage [17].…”

Section: How Can Specific Virus-induced Host Cellular Pathology Elucimentioning

confidence: 99%

Viruses as ‘Truffle Hounds’: Molecular Tools for Untangling Brain Cellular Pathology

Müller‐Schiffmann

Trossbach

Lingappa³

et al. 2021

Trends in Neurosciences

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Section: How Can Specific Virus-induced Host Cellular Pathology Elucimentioning

confidence: 99%

Viruses as ‘Truffle Hounds’: Molecular Tools for Untangling Brain Cellular Pathology

Müller‐Schiffmann

Trossbach

Lingappa³

et al. 2021

Trends in Neurosciences

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“…Aggregates of p62-bound ubiquitinated proteins interact with HDAC6 and are transported to the microtubule-organizing center, where they form aggresomes 48 49 . The aggresomes are surrounded by mitochondria 50 . In blue light-exposed cells, overexpressed OptoTau induced increased levels of ubiquitinated protein, compared with the CRY2olig control (Fig.…”

Section: Resultsmentioning

confidence: 99%

Intracellular Tau Fragment Droplets Serve as Seeds for Tau Fibrils

Soeda,

Yoshimura,

Bannai

et al. 2023

Preprint

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Intracellular tau aggregation requires a local protein concentration increase, referred to as droplets. However, the cellular mechanism remains insufficiently understood. We expressed OptoTau, a fusion of P301L mutant tau with CRY2olig, a light-sensitive protein that forms homo-oligomers. Under blue light exposure, OptoTau increased tau phosphorylation and was sequestered in aggresomes. Suppressing aggresome formation by nocodazole formed tau granular clusters in the cytoplasm. The granular clusters disappeared by discontinuing blue light exposure or 1,6-hexanediol treatment, which can dissolve droplets, suggesting that intracellular tau droplet formation requires the microtubules collapse. Expressing OptoTau-ΔN, a species of N-terminal cleaved tau that was observed in the Alzheimer’s disease brain, formed 1,6-hexanediol and detergent-resistant tau clusters in the cytoplasm by blue light stimulation. This intracellular stable tau clusters acted as seeds for tau fibrils in vitro. These results suggest that both tau droplet formation and N-terminal cleavage are necessary for neurofibrillary tangles formation in neurodegenerative diseases.

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“…Human immunodeficiency virus (HIV-1) accumulates MTOCs at the pre-integration step, elongating the centrosomes and recruiting γ-tubulin by a role attributed to Vpr ( Hossain et al, 2018 ). Other viruses, such as poxviruses or African swine fever virus (ASFV), create VFs at MTOCs ( Wileman et al, 2016 ). β-coronaviruses, including SARS-CoV, adapt their replication vesicles surrounding MTOCs ( Angelini et al, 2013 ).…”

Section: Discussionmentioning

confidence: 99%

Mammalian orthoreovirus core protein μ2 reorganizes host microtubule-organizing center components

2020

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Filamentous mammalian orthoreovirus (MRV) viral factories (VFs) are membrane-less cytosolic inclusions in which virus transcription, replication of dsRNA genome segments, and packaging of virus progeny into newly synthesized virus cores take place. In infected cells, the MRV μ2 protein forms punctae in the enlarged region of the filamentous VFs that are co-localized with γ-tubulin and resistant to nocodazole treatment, and permitted microtubule (MT)-extension, features common to MT-organizing centers (MTOCs). Using a previously established reconstituted VF model, we addressed the functions of MT-components and MTOCs concerning their roles in the formation of filamentous VFs. Indeed, the MTOC markers γ-tubulin and centrin were redistributed within the VF-like structures (VFLS) in a μ2-dependent manner. Moreover, the MT-nucleation centers significantly increased in numbers, and γ-tubulin was pulled-down in a binding assay when co-expressed with histidine-tagged-μ2 and μNS. Thus, μ2, by interaction with γ-tubulin, can modulate MTOCs localization and function according to viral needs.

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Virus Factories and Mini-Organelles Generated for Virus Replication

Cited by 6 publications

References 45 publications

Viruses as ‘Truffle Hounds’: Molecular Tools for Untangling Brain Cellular Pathology

Viruses as ‘Truffle Hounds’: Molecular Tools for Untangling Brain Cellular Pathology

Intracellular Tau Fragment Droplets Serve as Seeds for Tau Fibrils

Mammalian orthoreovirus core protein μ2 reorganizes host microtubule-organizing center components

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