ArticlePLoS pathogens2017
Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- N-linked glycosylation of NS1 protein modulates progeny virion assembly in orthoflaviviruses.PLoS pathogens · 2026Article
- Re-mining serum proteomics data reveals extensive post-translational modifications upon Zika and dengue infection.Molecular omics · 2023Article
- Secretory glycoprotein NS1 plays a crucial role in the particle formation of flaviviruses.PLoS pathogens · 2022Article
- Recent Progress on Tick-Borne Animal Diseases of Veterinary and Public Health Significance in China.Viruses · 2022Review
- Positively Charged Amino Acids in the Pestiviral EViruses · 2021Article
- Hepatitis C Virus Uses Host Lipids to Its Own Advantage.Metabolites · 2021Review
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- The ATGL lipase cooperates with ABHD5 to mobilize lipids for hepatitis C virus assembly.PLoS pathogens · 2020Article
- Review
- Article
- The Role of ApoE in HCV Infection and Comorbidity.International journal of molecular sciences · 2019Review
- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- CEACAM1 Is Associated With the Suppression of Natural Killer Cell Function in Patients With Chronic Hepatitis C.Hepatology communications · 2018Article
- Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Scientific reports · 2018Article
- Rewiring cellular networks by members of the Flaviviridae family.Nature reviews. Microbiology · 2018Review
- Tick-Borne Viruses.Virologica Sinica · 2018Review
- Hepatitis C Virus (HCV)-Apolipoprotein Interactions and Immune Evasion and Their Impact on HCV Vaccine Design.Frontiers in immunology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.