Viperin interacts with PEX19 to mediate peroxisomal augmentation of the innate antiviral response.
Khantisitthiporn, O
Shue, B
Eyre, NS
Nash, CW
Turnbull, L
Whitchurch, CB
Van der Hoek, KH
Helbig, KJ
Beard, MR
- Publisher:
- Life Science Alliance, LLC
- Publication Type:
- Journal Article
- Citation:
- Life Sci Alliance, 2021, 4, (7), pp. e202000915
- Issue Date:
- 2021-07
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Khantisitthiporn, O | |
dc.contributor.author | Shue, B | |
dc.contributor.author | Eyre, NS | |
dc.contributor.author | Nash, CW | |
dc.contributor.author | Turnbull, L | |
dc.contributor.author | Whitchurch, CB | |
dc.contributor.author | Van der Hoek, KH | |
dc.contributor.author | Helbig, KJ | |
dc.contributor.author | Beard, MR | |
dc.date.accessioned | 2022-01-07T00:10:48Z | |
dc.date.available | 2021-05-27 | |
dc.date.available | 2022-01-07T00:10:48Z | |
dc.date.issued | 2021-07 | |
dc.identifier.citation | Life Sci Alliance, 2021, 4, (7), pp. e202000915 | |
dc.identifier.issn | 2575-1077 | |
dc.identifier.issn | 2575-1077 | |
dc.identifier.uri | http://hdl.handle.net/10453/152791 | |
dc.description.abstract | Peroxisomes are recognized as significant platforms for the activation of antiviral innate immunity where stimulation of the key adapter molecule mitochondrial antiviral signaling protein (MAVS) within the RIG-I like receptor (RLR) pathway culminates in the up-regulation of hundreds of ISGs, some of which drive augmentation of multiple innate sensing pathways. However, whether ISGs can augment peroxisome-driven RLR signaling is currently unknown. Using a proteomics-based screening approach, we identified Pex19 as a binding partner of the ISG viperin. Viperin colocalized with numerous peroxisomal proteins and its interaction with Pex19 was in close association with lipid droplets, another emerging innate signaling platform. Augmentation of the RLR pathway by viperin was lost when Pex19 expression was reduced. Expression of organelle-specific MAVS demonstrated that viperin requires both mitochondria and peroxisome MAVS for optimal induction of IFN-β. These results suggest that viperin is required to enhance the antiviral cellular response with a possible role to position the peroxisome at the mitochondrial/MAM MAVS signaling synapse, furthering our understanding of the importance of multiple organelles driving the innate immune response against viral infection. | |
dc.format | Electronic-Print | |
dc.language | eng | |
dc.publisher | Life Science Alliance, LLC | |
dc.relation.ispartof | Life Sci Alliance | |
dc.relation.isbasedon | 10.26508/lsa.202000915 | |
dc.rights | License: This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/ licenses/by/4.0/) | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject.mesh | Adaptor Proteins, Signal Transducing | |
dc.subject.mesh | Antiviral Agents | |
dc.subject.mesh | Cell Line | |
dc.subject.mesh | Cell Line, Tumor | |
dc.subject.mesh | Gene Expression | |
dc.subject.mesh | Gene Expression Regulation | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Immunity, Innate | |
dc.subject.mesh | Interferon Regulatory Factors | |
dc.subject.mesh | Membrane Proteins | |
dc.subject.mesh | Mitochondria | |
dc.subject.mesh | Mitochondrial Membranes | |
dc.subject.mesh | Oxidoreductases Acting on CH-CH Group Donors | |
dc.subject.mesh | Peroxisomes | |
dc.subject.mesh | Signal Transduction | |
dc.subject.mesh | Cell Line | |
dc.subject.mesh | Cell Line, Tumor | |
dc.subject.mesh | Peroxisomes | |
dc.subject.mesh | Mitochondria | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Oxidoreductases Acting on CH-CH Group Donors | |
dc.subject.mesh | Adaptor Proteins, Signal Transducing | |
dc.subject.mesh | Membrane Proteins | |
dc.subject.mesh | Antiviral Agents | |
dc.subject.mesh | Signal Transduction | |
dc.subject.mesh | Gene Expression | |
dc.subject.mesh | Gene Expression Regulation | |
dc.subject.mesh | Interferon Regulatory Factors | |
dc.subject.mesh | Mitochondrial Membranes | |
dc.subject.mesh | Immunity, Innate | |
dc.title | Viperin interacts with PEX19 to mediate peroxisomal augmentation of the innate antiviral response. | |
dc.type | Journal Article | |
utslib.citation.volume | 4 | |
utslib.location.activity | United States | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation | |
utslib.copyright.status | open_access | * |
dc.date.updated | 2022-01-07T00:10:43Z | |
pubs.issue | 7 | |
pubs.publication-status | Published online | |
pubs.volume | 4 | |
utslib.citation.issue | 7 |
Abstract:
Peroxisomes are recognized as significant platforms for the activation of antiviral innate immunity where stimulation of the key adapter molecule mitochondrial antiviral signaling protein (MAVS) within the RIG-I like receptor (RLR) pathway culminates in the up-regulation of hundreds of ISGs, some of which drive augmentation of multiple innate sensing pathways. However, whether ISGs can augment peroxisome-driven RLR signaling is currently unknown. Using a proteomics-based screening approach, we identified Pex19 as a binding partner of the ISG viperin. Viperin colocalized with numerous peroxisomal proteins and its interaction with Pex19 was in close association with lipid droplets, another emerging innate signaling platform. Augmentation of the RLR pathway by viperin was lost when Pex19 expression was reduced. Expression of organelle-specific MAVS demonstrated that viperin requires both mitochondria and peroxisome MAVS for optimal induction of IFN-β. These results suggest that viperin is required to enhance the antiviral cellular response with a possible role to position the peroxisome at the mitochondrial/MAM MAVS signaling synapse, furthering our understanding of the importance of multiple organelles driving the innate immune response against viral infection.
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