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Article: Virus subtype-specific suppression of MAVS aggregation and activation by PB1-F2 protein of influenza A (H7N9) virus

TitleVirus subtype-specific suppression of MAVS aggregation and activation by PB1-F2 protein of influenza A (H7N9) virus
Authors
KeywordsH7N9
Wireless sensor networks
H5N1
Mitochondria
Transfection
Issue Date2020
PublisherPublic Library of Science. The Journal's web site is located at http://pathogens.plosjournals.org/perlserv/?request=index-html&issn=1553-7374
Citation
PLoS Pathogens, 2020, v. 16 n. 6, p. article no. e1008611 How to Cite?
AbstractHuman infection with avian influenza A (H5N1) and (H7N9) viruses causes severe respiratory diseases. PB1-F2 protein is a critical virulence factor that suppresses early type I interferon response, but the mechanism of its action in relation to high pathogenicity is not well understood. Here we show that PB1-F2 protein of H7N9 virus is a particularly potent suppressor of antiviral signaling through formation of protein aggregates on mitochondria and inhibition of TRIM31-MAVS interaction, leading to prevention of K63-polyubiquitination and aggregation of MAVS. Unaggregated MAVS accumulated on fragmented mitochondria is prone to degradation by both proteasomal and lysosomal pathways. These properties are proprietary to PB1-F2 of H7N9 virus but not shared by its counterpart in WSN virus. A recombinant virus deficient of PB1-F2 of H7N9 induces more interferon β in infected cells. Our findings reveal a subtype-specific mechanism for destabilization of MAVS and suppression of interferon response by PB1-F2 of H7N9 virus.
Persistent Identifierhttp://hdl.handle.net/10722/288399
ISSN
2023 Impact Factor: 5.5
2023 SCImago Journal Rankings: 2.223
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCHEUNG, PHH-
dc.contributor.authorLEE, TWT-
dc.contributor.authorKew, C-
dc.contributor.authorChen, H-
dc.contributor.authorYuen, KY-
dc.contributor.authorChan, CP-
dc.contributor.authorJin, DY-
dc.date.accessioned2020-10-05T12:12:19Z-
dc.date.available2020-10-05T12:12:19Z-
dc.date.issued2020-
dc.identifier.citationPLoS Pathogens, 2020, v. 16 n. 6, p. article no. e1008611-
dc.identifier.issn1553-7366-
dc.identifier.urihttp://hdl.handle.net/10722/288399-
dc.description.abstractHuman infection with avian influenza A (H5N1) and (H7N9) viruses causes severe respiratory diseases. PB1-F2 protein is a critical virulence factor that suppresses early type I interferon response, but the mechanism of its action in relation to high pathogenicity is not well understood. Here we show that PB1-F2 protein of H7N9 virus is a particularly potent suppressor of antiviral signaling through formation of protein aggregates on mitochondria and inhibition of TRIM31-MAVS interaction, leading to prevention of K63-polyubiquitination and aggregation of MAVS. Unaggregated MAVS accumulated on fragmented mitochondria is prone to degradation by both proteasomal and lysosomal pathways. These properties are proprietary to PB1-F2 of H7N9 virus but not shared by its counterpart in WSN virus. A recombinant virus deficient of PB1-F2 of H7N9 induces more interferon β in infected cells. Our findings reveal a subtype-specific mechanism for destabilization of MAVS and suppression of interferon response by PB1-F2 of H7N9 virus.-
dc.languageeng-
dc.publisherPublic Library of Science. The Journal's web site is located at http://pathogens.plosjournals.org/perlserv/?request=index-html&issn=1553-7374-
dc.relation.ispartofPLoS Pathogens-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectH7N9-
dc.subjectWireless sensor networks-
dc.subjectH5N1-
dc.subjectMitochondria-
dc.subjectTransfection-
dc.titleVirus subtype-specific suppression of MAVS aggregation and activation by PB1-F2 protein of influenza A (H7N9) virus-
dc.typeArticle-
dc.identifier.emailChen, H: hlchen@hku.hk-
dc.identifier.emailYuen, KY: kyyuen@hkucc.hku.hk-
dc.identifier.emailChan, CP: chancp10@hku.hk-
dc.identifier.emailJin, DY: dyjin@hku.hk-
dc.identifier.authorityChen, H=rp00383-
dc.identifier.authorityYuen, KY=rp00366-
dc.identifier.authorityChan, CP=rp02031-
dc.identifier.authorityJin, DY=rp00452-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.ppat.1008611-
dc.identifier.pmid32511263-
dc.identifier.pmcidPMC7302872-
dc.identifier.scopuseid_2-s2.0-85086747763-
dc.identifier.hkuros315279-
dc.identifier.volume16-
dc.identifier.issue6-
dc.identifier.spagearticle no. e1008611-
dc.identifier.epagearticle no. e1008611-
dc.identifier.isiWOS:000544026400001-
dc.publisher.placeUnited States-
dc.identifier.issnl1553-7366-

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