ArticleJournal of virology2026
Hepatitis C virus p7 regulates Core protein processing via signal peptide peptidase to promote virion assembly.
Article in Journal of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The hepatitis C virus (HCV) p7 protein is a viroporin essential for the production of infectious virus particles and has been implicated in regulating Core protein localization. Here, we identify a previously unrecognized role of p7 in modulating Core maturation through interaction with host signal peptide peptidase (SPP), a mechanism that remains intact even in ion-channel deficient mutants. Using a transient expression system, we show that p7 from genotype 1a (H77S) delays SPP-mediated cleavage of full-length Core (fl-Core) to mature Core (m-Core), while genotype 2a (JFH1) p7 exerts a weaker inhibitory effect. Both p7 variants bind endogenous SPP, but JFH1 p7 shows reduced affinity, correlating with diminished inhibition of Core processing. A conserved leucine-rich motif (L51-55) in the p7 C-terminus is essential for SPP binding; its mutation disrupts Core processing and markedly reduces infectious virus production. Moreover, fl-Core preferentially associates with E1 glycoprotein compared to m-Core, supporting its role in virion assembly. These findings uncover a mechanism by which p7 regulates the timing of Core maturation via SPP interaction to promote efficient HCV particle assembly.IMPORTANCEHepatitis C virus (HCV) assembly depends on the tightly regulated coordination of viral structural proteins and host factors. While p7 is well-known for its viroporin activity, its role in viral protein maturation has remained unclear. This study uncovers a novel function of p7 in modulating Core protein processing via interaction with host signal peptide peptidase (SPP). We identify a conserved leucine-rich motif in p7 essential for this interaction and demonstrate that delayed Core maturation enhances Core-E1 association and promotes efficient virus assembly. These findings expand our understanding of HCV morphogenesis and highlight the p7-SPP axis as a potential target for antiviral intervention.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.