ArticleFrontiers in microbiology2025
The role and mechanism of p53 F229V mutation in inhibiting pseudorabies virus replication.
Article in Frontiers in microbiology, 2025. 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
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The p53 protein is a key transcription factor that regulates cellular responses to stress and is widely recognized as a host restriction factor against various viral infections. However, its specific role in pseudorabies virus (PRV) replication, pathogenesis, and host response remains unclear. This study identified a swine p53 (sp53) mutation in the PK15 cell line under prolonged passage stress, characterized by an amino acid substitution at position 229, replacing phenylalanine with valine (sp53 F229V). This mutation eliminates the transcriptional activity of wild-type p53 and confers resistance to PRV infection. Notably, it reverses p53's original pro-viral role, converting it into an inhibitor of PRV proliferation. Further analysis revealed that the PRV early protein EP0 promotes the degradation of sp53 F229V through the proteasome pathway. These findings indicate that a defined p53 alteration can decouple transcriptional and antiviral functions in a mutation-specific, context-dependent manner. The EP0-p53 interface emerges as a candidate target to modulate PRV replication, pending validation. These findings were obtained
Indexed as
Identifiers
What Socratic 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 Socratic graph.