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

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...

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Main Authors: Takasuke Fukuhara, Tomokazu Tamura, Chikako Ono, Mai Shiokawa, Hiroyuki Mori, Kentaro Uemura, Satomi Yamamoto, Takeshi Kurihara, Toru Okamoto, Ryosuke Suzuki, Kentaro Yoshii, Takeshi Kurosu, Manabu Igarashi, Hiroshi Aoki, Yoshihiro Sakoda, Yoshiharu Matsuura
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-06-01
Series:PLoS Pathogens
Online Access:https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006475&type=printable
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author Takasuke Fukuhara
Tomokazu Tamura
Chikako Ono
Mai Shiokawa
Hiroyuki Mori
Kentaro Uemura
Satomi Yamamoto
Takeshi Kurihara
Toru Okamoto
Ryosuke Suzuki
Kentaro Yoshii
Takeshi Kurosu
Manabu Igarashi
Hiroshi Aoki
Yoshihiro Sakoda
Yoshiharu Matsuura
author_facet Takasuke Fukuhara
Tomokazu Tamura
Chikako Ono
Mai Shiokawa
Hiroyuki Mori
Kentaro Uemura
Satomi Yamamoto
Takeshi Kurihara
Toru Okamoto
Ryosuke Suzuki
Kentaro Yoshii
Takeshi Kurosu
Manabu Igarashi
Hiroshi Aoki
Yoshihiro Sakoda
Yoshiharu Matsuura
author_sort Takasuke Fukuhara
collection DOAJ
description 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.
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spelling doaj-art-fa1c2028f09b40eb9785b7f9bce7d1b62025-08-20T02:03:54ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742017-06-01136e100647510.1371/journal.ppat.1006475Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.Takasuke FukuharaTomokazu TamuraChikako OnoMai ShiokawaHiroyuki MoriKentaro UemuraSatomi YamamotoTakeshi KuriharaToru OkamotoRyosuke SuzukiKentaro YoshiiTakeshi KurosuManabu IgarashiHiroshi AokiYoshihiro SakodaYoshiharu MatsuuraAmphipathic 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.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006475&type=printable
spellingShingle Takasuke Fukuhara
Tomokazu Tamura
Chikako Ono
Mai Shiokawa
Hiroyuki Mori
Kentaro Uemura
Satomi Yamamoto
Takeshi Kurihara
Toru Okamoto
Ryosuke Suzuki
Kentaro Yoshii
Takeshi Kurosu
Manabu Igarashi
Hiroshi Aoki
Yoshihiro Sakoda
Yoshiharu Matsuura
Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
PLoS Pathogens
title Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
title_full Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
title_fullStr Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
title_full_unstemmed Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
title_short Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
title_sort host derived apolipoproteins play comparable roles with viral secretory proteins erns and ns1 in the infectious particle formation of flaviviridae
url https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006475&type=printable
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