In vitro study showing that G3BP1 and G3BP2 proteins redundantly suppress SARS-CoV-2 infection by inhibiting viral replication beyond their roles in stress granule formation. Authors identified G3BP1/2 as key host factors that interact with the SARS-CoV-2 nucleocapsid (N) protein through a comparative analysis of multiple proteomic datasets.
Xu et al., 27 Jun 2025, peer-reviewed, 9 authors.
Contact: ronghai@ucr.edu (corresponding author), duox@ucr.edu, christine.light@email.ucr.edu, ywu548@ucr.edu, mbisw002@ucr.edu, jikuis@ucr.edu, quanqinz@ucr.edu, chenjinye@txbiomed.org, lmartinez@txbiomed.org.
In vitro studies are an important part of preclinical research, however results may be very different in vivo.
Beyond Stress Granules: G3BP1 and G3BP2 Redundantly Suppress SARS-CoV-2 Infection
Viruses, doi:10.3390/v17070912
The global pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has posed unprecedented challenges to public health and economic stability. Central to SARS-CoV-2 pathogenesis is its ability to evade the host immune response by hijacking host pathways via the interaction between viral and host proteins. We identified Ras-GTPase-activating protein SH3 domain-binding protein 1/2 (G3BP1/G3BP2) as a critical host factor that interacts with the viral nucleocapsid (N) protein, emerging from a comparative analysis of proteomic data from multiple studies. We revisited the underlying molecular mechanisms by confirming the residues required for the interaction between G3BP1/G3BP2 and SARS-CoV-2 N protein and showed that this interaction disrupts stress granule formation. Intriguingly, we observed that the ablation of both G3BP1 and G3BP2 enhanced SARS-CoV-2 replication. Our data collectively supports the notion that G3BP1 and G3BP2 play a critical role in modulating the host-virus interface during SARS-CoV-2 infection, and that their multifaceted function in cellular defense extends beyond the stress granule pathway.
Supplementary Materials: The following supporting information can be downloaded at: https: //www.mdpi.com/article/10.3390/v17070912/s1 , Figure S1 : Linear representation of the SARS-CoV-2 nucleocapsid (N) protein, highlighting peptides identified by LC-MS analysis. The full-length protein sequence is shown, with tryptic digestion sites indicated in green. Red indicates the peptides that were successfully identified in our LC-MS analysis; Figure S2 : Coomassie blue-stained protein gel of pull-down assays using SARS-CoV-2 N protein versus mock samples, prepared for LC-MS analysis to compare interacting proteins; Figure S3 : Schematic of specific mutations in genes induced by CRISPR-Cas9 in A549 Cell Lines; Table S1 -1: The SARS-CoV-2 N protein associated host proteins obtained by MS data search; Table S1 -2: The selected SARS-CoV-2 N associated host proteins after intensity comparison; Table S2 -1: The Protein IDs summary and Venn results from our analysis and previously studies; Table S2 -2: The KEGG pathway summary and Venn results from our analysis and previously studies; Table S3 -1: The result of QIAGEN Ingenuity Pathway Analysis: Table S3
Conflicts of Interest: The authors declare no conflicts of interest.
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