ArticleScientific reports2026
ORF3 protein of porcine circovirus type 2 induced RIPK3 phosphorylation-driven autophagy to promote viral replication.
Article in Scientific reports, 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
8 authors.
Funding
Abstract
Receptor-interacting protein kinase-3 (RIPK3), a critical regulator of necroptosis and inflammation, has been implicated in modulating viral infections by either promoting host defense or facilitating viral replication. In this study, it was found that porcine circovirus type 2 (PCV2) infection selectively induced RIPK3 phosphorylation in PK-15 cells without activating its canonical downstream effector MLKL. This indicated that the virus exploits RIPK3 in a necroptosis-independent manner. Inhibition of RIPK3 phosphorylation using GSK872 or RIPK3 knockdown significantly reduced viral replication, as evidenced by viral DNA levels in PK-15 cells, with a concomitant reduction in Rep protein expression. Through functional screening of viral proteins, we found that only ORF3 triggered RIPK3 phosphorylation, while capsid (Cap) and replication-associated (Rep) proteins did not. Both PCV2 infection and ORF3 could induce autophagy. RIPK3 knockdown suppressed PCV2-induced autophagy, and subsequently knockdown of the autophagy-related protein ATG7 resulted in the reduction of PCV2 replication. These findings indicated that PCV2 employed its ORF3 protein to hijack RIPK3 phosphorylation-dependent autophagy, thereby creating a promoted viral replication environment. In conclusion, this study demonstrated that PCV2 manipulated host cell machinery through its ORF3 protein, which hijacked RIPK3 phosphorylation to activate autophagy-a mechanism distinct from RIPK3's classical necroptosis function. This ORF3-RIPK3 phosphorylation-autophagy axis represented a novel therapeutic target for PCV2 control.
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.