Analysis of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Interactome
Issued Date
2025-11-07
Resource Type
ISSN
15353893
eISSN
15353907
Scopus ID
2-s2.0-105021050414
Pubmed ID
40994299
Journal Title
Journal of Proteome Research
Volume
24
Issue
11
Start Page
5390
End Page
5411
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of Proteome Research Vol.24 No.11 (2025) , 5390-5411
Suggested Citation
Kovanich D., Ketsuwan K., Hengphasatporn K., Thepparit C., Sittipaisankul P., Wongkongkathep P., Sirisereewan C., Techakriengkrai N., Nedumpun T., Shigeta Y., Pisitkun T., Suradhat S. Analysis of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Interactome. Journal of Proteome Research Vol.24 No.11 (2025) , 5390-5411. 5411. doi:10.1021/acs.jproteome.5c00121 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/113115
Title
Analysis of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Interactome
Corresponding Author(s)
Other Contributor(s)
Abstract
Porcine reproductive and respiratory syndrome virus (PRRSV) is a major swine pathogen that causes significant economic losses worldwide. The nucleocapsid (N) protein, the most abundant viral protein in infected cells, plays roles beyond its structural function, influencing various host cellular processes. Here, we report the identification of 301 cellular protein candidates interacting with PRRSV N using EGFP immunoprecipitation combined with label-free quantitative mass spectrometry. The analysis underscores the versatile nature of the N protein in targeting a wide range of cellular proteins and processes across multiple subcellular compartments. We observed strong enrichment of ribosomal proteins, nucleolar proteins involved in ribosome biogenesis, splicing factors, RNA helicases, and DNA-binding proteins involved in chromatin remodeling and DNA damage response. Additionally, we identified proteins involved in viral RNA sensing and intrinsic antiviral mechanisms that may contribute to the immunosuppressive properties of the viral protein. Several interactions were validated and further characterized for RNA dependence, including MYBBP1A, NCL, IGF2BP1, UPF3B, G3BP1, EIF2S1, RFC4, ABCF1, PPM1G, NSUN2, and NOP2. Notably, RTCB and MYBBP1A were identified as host dependency factors for PRRSV infection. Our findings expand the current understanding of PRRSV-host interactions and reveal novel N-interacting proteins that may contribute to viral pathogenesis and immune evasion.