ArticleNucleic acids research2025
SARS-CoV-2 Nsp2 recruits GIGYF2 near viral replication sites and supports viral protein production.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
The SARS-CoV-2 genome encodes 16 nonstructural proteins (Nsps), with Nsp2 being the least conserved and understood. This study highlights a crucial role for Nsp2 in the early phase of the viral life cycle, particularly its interaction with GIGYF2, which relocates near double-membrane vesicles (DMVs) and enhances viral protein production. Deletion of the Nsp2-coding region from the viral genome led to a drastic reduction in viral RNA synthesis early in infection (3-4 h after infection). Interactome analysis in virus-infected cells identified GIGYF2, a host-encoded translational regulation protein, as a key Nsp2 partner. This interaction was confirmed for both SARS-CoV-1 and SARS-CoV-2. Depletion of GIGYF2 or its cofactor ZNF598 phenocopied the replication defects observed with Nsp2 deletion, suggesting their critical roles in viral reproduction. Upon infection, GIGYF2 and ZNF598 relocate to areas near DMVs, viral replication sites. This relocation does not occur with the Nsp2-deleted virus, indicating Nsp2's role in directing GIGYF2 to DMVs. Formaldehyde crosslinking and immunoprecipitation sequencing (fCLIP-seq) identified regions within viral RNAs that potentially interact with GIGYF2, including those encoding M and Orf6. Depletion of GIGYF2 resulted in decreased protein expression of M and Orf6. Our findings reveal the function of Nsp2 in supporting viral protein production by exploiting GIGYF2 as a host factor.
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.