HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Global Institution for Collaborative Research and Education : GI-CoRE >
Peer-reviewed Journal Articles, etc >

Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae

Creative Commons License

Files in This Item:

The file(s) associated with this item can be obtained from the following URL:https://doi.org/10.1371/journal.ppat.1006475


Title: Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae
Authors: Fukuhara, Takasuke Browse this author →KAKEN DB
Tamura, Tomokazu Browse this author
Ono, Chikako Browse this author →KAKEN DB
Shiokawa, Mai Browse this author
Mori, Hiroyuki Browse this author
Uemura, Kentaro Browse this author
Yamamoto, Satomi Browse this author
Kurihara, Takeshi Browse this author
Okamoto, Toru Browse this author →KAKEN DB
Suzuki, Ryosuke Browse this author
Yoshii, Kentaro Browse this author →KAKEN DB
Kurosu, Takeshi Browse this author →KAKEN DB
Igarashi, Manabu Browse this author →KAKEN DB
Aoki, Hiroshi Browse this author →KAKEN DB
Sakoda, Yoshihiro Browse this author →KAKEN DB
Matsuura, Yoshiharu Browse this author →KAKEN DB
Issue Date: 23-Jun-2017
Publisher: PLOS
Journal Title: PLoS pathogens
Volume: 13
Issue: 6
Start Page: e1006475
Publisher DOI: 10.1371/journal.ppat.1006475
PMID: 28644867
Abstract: Amphipathic α-helices of exchangeable apolipoproteins have shown to play crucial roles in the formation of infectious hepatitis C virus (HCV) particles through the interaction with viral particles. Among the Flaviviridae members, pestivirus and flavivirus possess a viral structural protein Erns or a non-structural protein 1 (NS1) as secretory glycoproteins, respectively, while Hepacivirus including HCV has no secretory glycoprotein. In case of pestivirus replication, the C-terminal long amphipathic α-helices of Erns are important for anchoring to viral membrane. Here we show that host-derived apolipoproteins play functional roles similar to those of virally encoded Erns and NS1 in the formation of infectious particles. We examined whether Erns and NS1 could compensate for the role of apolipoproteins in particle formation of HCV in apolipoprotein B (ApoB) and ApoE double-knockout Huh7 (BE-KO), and non-hepatic 293T cells. We found that exogenous expression of either Erns or NS1 rescued infectious particle formation of HCV in the BE-KO and 293T cells. In addition, expression of apolipoproteins or NS1 partially rescued the production of infectious pestivirus particles in cells upon electroporation with an Erns-deleted non-infectious RNA. As with exchangeable apolipoproteins, the C-terminal amphipathic α-helices of Erns play the functional roles in the formation of infectious HCV or pestivirus particles. These results strongly suggest that the host- and virus-derived secretory glycoproteins have overlapping roles in the viral life cycle of Flaviviridae, especially in the maturation of infectious particles, while Erns and NS1 also participate in replication complex formation and viral entry, respectively. Considering the abundant hepatic expression and liver-specific propagation of these apolipoproteins, HCV might have evolved to utilize them in the formation of infectious particles through deletion of a secretory viral glycoprotein gene.
Rights: https://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/76370
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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)

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

Feedback - Hokkaido University