[Objective] Using the characteristics of MS2 phage coat protein that can self-assemble and encapsulate exogenous nucleic acid in vitro, prepare RT-PCR quality control materials for detection of porcine epidemic diarrhea virus, and study its stability and resistance to Rnase degradation. [Method] Select the highly conservative N protein gene of porcine epidemic diarrhea virus as the target sequence, insert it into the downstream of the gene carrying the MS2 phage coat protein and PAC locus, construct a recombinant vector, express the recombinant protein through the prokaryotic expression system, and the target protein is subjected to sulfuric acid Purification by ammonium and gel filtration chromatography, as well as Benzonase nuclease digestion, physical characterization of the chimeric protein using electron microscopy, and Taqman fluorescence RT-PCR to verify the thermal stability of armor RNA and Rnase resistance. [Result] Successfully constructed MS2 containing MS2 Recombinant vector of phage coat protein, PAC site and porcine epidemic diarrhea virus target gene. After prokaryotic expression and purification, uniform MS2 virus-like particles with a diameter of 23-28 nm are obtained. The particles are digested with nuclease and extracted with RNA And fluorescent RT-PCR confirmed that it formed armor RNA encapsulating the target gene. The armor RNA can withstand the degradation of Rnase, and can exist stably at 37°C for 15 d under aseptic conditions. [Conclusion] MS2 phage coat protein body The virus-like particles prepared by outsourcing the PEDV N protein target sequence can be used as a quality control product (armor RNA) for the detection of porcine epidemic diarrhea virus by RT-PCR. It has good thermal stability and resistance to Rnase attack, and can monitor the entire detection process throughout the process. [ABSTRACT FROM AUTHOR]