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Putative endogenous filovirus VP35-like protein potentially functions as an IFN antagonist but not a polymerase cofactor

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Title: Putative endogenous filovirus VP35-like protein potentially functions as an IFN antagonist but not a polymerase cofactor
Authors: Kondoh, Tatsunari Browse this author
Manzoor, Rashid Browse this author
Nao, Naganori Browse this author
Maruyama, Junki Browse this author
Furuyama, Wakako Browse this author
Miyamoto, Hiroko Browse this author
Shigeno, Asako Browse this author
Kuroda, Makoto Browse this author
Matsuno, Keita Browse this author
Fujikura, Daisuke Browse this author →KAKEN DB
Kajihara, Masahiro Browse this author
Yoshida, Reiko Browse this author
Igarashi, Manabu Browse this author →KAKEN DB
Takada, Ayato Browse this author →KAKEN DB
Issue Date: 17-Oct-2017
Publisher: PLOS
Journal Title: PLoS ONE
Volume: 12
Issue: 10
Start Page: 1
End Page: 17
Publisher DOI: 10.1371/journal.pone.0186450
Abstract: It has been proposed that some non-retroviral RNA virus genes are integrated into vertebrate genomes. Endogenous filovirus-like elements (EFLs) have been discovered in some mammalian genomes. However, their potential roles in ebolavirus infection are unclear. A filovirus VP35-like element (mlEFL35) is found in the little brown bat (Myotis lucifugus) genome. Putative mlEFL35-derived protein (mlEFL35p) contains nearly full-length amino acid sequences corresponding to ebolavirus VP35. Ebola virus VP35 has been shown to bind double-stranded RNA, leading to inhibition of type I interferon (IFN) production, and is also known as a viral polymerase cofactor that is essential for viral RNA transcription/replication. In this study, we transiently expressed mlEFL35p in human kidney cells and investigated its biological functions. We first found that mlEFL35p was coimmunoprecipitated with itself and ebolavirus VP35s but not with the viral nucleoprotein. Then the biological functions of mlEFL35p were analyzed by comparing it to ebolavirus VP35s. We found that the expression of mlEFL35p significantly inhibited human IFN-beta promoter activity as well as VP35s. By contrast, expression of mlEFL35p did not support viral RNA transcription/replication and indeed slightly decrease the reporter gene expression in a minigenome assay. These results suggest that mlEFL35p potentially acts as an IFN antagonist but not a polymerase cofactor.
Rights: https://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/67707
Appears in Collections:国際連携研究教育局 : GI-CoRE (Global Institution for Collaborative Research and Education : GI-CoRE) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 高田 礼人

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