Porcine Mx1 protein inhibits porcine deltacoronavirus replication in vitro by disturbing the N-Nsp12 interaction

This result is strongly supported by a predicted interaction complex structural model generated using AlphaFold 3, and this domain is indispensable for pMx1's antiviral function. We further revealed a crucial synergistic interaction between the PDCoV N protein and the viral RNA-dependent RNA polymerase Nsp12, a core component of the replication-transcription complex (RTC), and demonstrated that pMx1 protein effectively disrupts this interaction, thereby impeding viral genome replication.

In summary, this study elucidates the mechanism by which the pMx1 protein, as a host antiviral factor, inhibits PDCoV infection. These findings provide novel insights into the innate immune defense against coronaviruses and highlight the pMx1 gene as a promising host-derived immune factor with potential as a therapeutic target or gene editing tool for combating PDCoV.