The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2

  • Bai Y
  • Wang S
  • Sun Y
  • et al.
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Abstract

The virus assembly process of arteriviruses remains largely elusive, including the direct interaction between N protein and viral envelope proteins or the potential requirement for additional proteins in facilitating assembly. Moreover, where the N protein assembles with viral envelope proteins during the virus lifecycle remains unclear. This study reveals a novel role for nonstructural protein 2 (nsp2) in highly pathogenic porcine reproductive and respiratory syndrome virus type 2 (HP-PRRSV-2), highlighting its involvement in HP-PRRSV-2 assembly. These findings provide crucial insights into HP-PRRSV-2 assembly and enhance our understanding of their lifecycle. Overall, this study offers an alternative approach to developing a new antiviral strategy targeting PRRSV-2 assembly.

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Bai, Y.-Z., Wang, S., Sun, Y., Liu, Y.-G., Zhang, H.-L., Wang, Q., … Tang, Y.-D. (2025). The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2. Journal of Virology, 99(1). https://doi.org/10.1128/jvi.01821-24

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