Hepatitis C Virus p7 is Critical for Capsid Assembly and Envelopment.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Perin, Paula Monteiro
MetadataShow full item record
AbstractHepatitis C virus (HCV) p7 is a membrane-associated ion channel protein crucial for virus production. To analyze how p7 contributes to this process, we dissected HCV morphogenesis into sub-steps including recruitment of HCV core to lipid droplets (LD), virus capsid assembly, unloading of core protein from LDs and subsequent membrane envelopment of capsids. Interestingly, we observed accumulation of slowly sedimenting capsid-like structures lacking the viral envelope in cells transfected with HCV p7 mutant genomes which possess a defect in virion production. Concomitantly, core protein was enriched at the surface of LDs. This indicates a defect in core/capsid unloading from LDs and subsequent membrane envelopment rather than defective trafficking of core to this cellular organelle. Protease and ribonuclease digestion protection assays, rate zonal centrifugation and native, two dimensional gel electrophoresis revealed increased amounts of high-order, non-enveloped core protein complexes unable to protect viral RNA in cells transfected with p7 mutant genomes. These results suggest accumulation of capsid assembly intermediates that had not yet completely incorporated viral RNA in the absence of functional p7. Thus, functional p7 is necessary for the final steps of capsid assembly as well as for capsid envelopment. These results support a model where capsid assembly is linked with membrane envelopment of nascent RNA-containing core protein multimers, a process coordinated by p7. In summary, we provide novel insights into the sequence of HCV assembly events and essential functions of p7.
CitationHepatitis C Virus p7 is Critical for Capsid Assembly and Envelopment. 2013, 9 (5):e1003355 PLoS Pathog.
AffiliationInstitute of Experimental Virology, TWINCORE, Centre for Experimental and Clinical Infection Research; a joint venture between the Medical School Hannover (MHH) and the Helmholtz Centre for Infection Research (HZI), Hannover, Germany.
The following license files are associated with this item:
- A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly.
- Authors: Boson B, Granio O, Bartenschlager R, Cosset FL
- Issue date: 2011 Jul
- Detergent-resistant membrane association of NS2 and E2 during hepatitis C virus replication.
- Authors: Shanmugam S, Saravanabalaji D, Yi M
- Issue date: 2015 Apr
- The amino-terminus of the hepatitis C virus (HCV) p7 viroporin and its cleavage from glycoprotein E2-p7 precursor determine specific infectivity and secretion levels of HCV particle types.
- Authors: Denolly S, Mialon C, Bourlet T, Amirache F, Penin F, Lindenbach B, Boson B, Cosset FL
- Issue date: 2017 Dec
- Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production.
- Authors: Wozniak AL, Griffin S, Rowlands D, Harris M, Yi M, Lemon SM, Weinman SA
- Issue date: 2010 Sep 2
- Ultrastructural and biochemical basis for hepatitis C virus morphogenesis.
- Authors: Falcón V, Acosta-Rivero N, González S, Dueñas-Carrera S, Martinez-Donato G, Menéndez I, Garateix R, Silva JA, Acosta E, Kourı J
- Issue date: 2017 Apr