HnRNP H1 binds to nucleocapsid protein and potential guanine-quadruplex site of viral RNA to promote PRRSV-2 proliferation

  • Res Vet Sci. 2026 Jul:206:106188. doi: 10.1016/j.rvsc.2026.106188.
Liwei Zhang  1 ,  Huiyuan Jing  2 ,  Yvzhen Song  1 ,  Pandeng Zhao  1 ,  Zhewei Zhang  1 ,  Erzhen Duan  3 ,  Jie Liu  4 ,  Huawei Li  5
Affiliations
  • 1. Key Laboratory of Veterinary Biological Products, College of Veterinary Medicine, Henan University of Animal Husbandry and Economy, Zhengzhou 450046, China.
  • 2. Key Laboratory of Veterinary Biological Products, College of Veterinary Medicine, Henan University of Animal Husbandry and Economy, Zhengzhou 450046, China. Electronic address: [email protected].
  • 3. College of Biological Engineering, Henan university of technology, Zhengzhou 450001, China.
  • 4. College of Animal & Veterinary Sciences, Southwest Minzu University, Chengdu 610041, China.
  • 5. Key Laboratory of Veterinary Biological Products, College of Veterinary Medicine, Henan University of Animal Husbandry and Economy, Zhengzhou 450046, China. Electronic address: [email protected].
PMID: 41996971 DOI: 10.1016/j.rvsc.2026.106188
Abstract

Porcine reproductive and respiratory syndrome (PRRS) is a highly contagious swine disease that causes huge economic losses to the pork industry worldwide. The heterogeneous nuclear ribonucleoprotein H1 (HnRNP H1) participates in a diverse range of cellular biological processes and has previously been reported to bind the nucleocapsid (N) protein of PRRSV-2; however, its role in PRRSV-2 proliferation remains largely unknown. Herein, we report that PRRSV-2 Infection upregulated the cytoplasm expression levels of HnRNP H1 but decreased its abundance in the nucleus. Co-immunoprecipitation studies revealed an interaction between HnRNP H1 and the N protein. Furthermore, depletion of HnRNP H1 by siRNA significantly inhibited viral RNA levels, N protein expression, and virus yield in porcine alveolar macrophages (PAMs), whereas ectopic expression of HnRNP H1 favored such activities. Most importantly, we showed that HnRNP H1 binds to a potential guanine-quadruplex site (PGS) in PRRSV-2 negative-strand RNA, whereas the guanine-quadruplex ligand PhenDC3 abolished this interaction and significantly suppressed PRRSV-2 propagation. Collectively, our results demonstrate new functions of HnRNP H1 in facilitating PRRSV-2 proliferation and provide a potential option for combating PRRSV-2 Infection by targeting the PGS.

Keywords
Heterogeneous nuclear ribonucleoprotein (HnRNP) H1; Nucleoprotein (N) protein; PhenDC3; Porcine reproductive and respiratory syndrome virus (PRRSV); Potential guanine-quadruplex site (PGS).
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