Various coronaviruses have emerged as a result of cross-species transmission among humans and domestic animals. Porcine epidemic diarrhea virus (PEDV; family Coronaviridae, genus Alphacoronavirus) causes acute diarrhea, vomiting, dehydration, and high mortality in neonatal piglets. Porcine small intestinal epithelial cells (IPEC-J2 cells) can be used as target cells for PEDV infection. However, the origin of PEDV in pigs, the host range, and cross-species infection of PEDV remain unclear. To determine whether PEDV has the ability to infect human cells in vitro, human small intestinal epithelial cells (FHs 74 Int cells) were inoculated with PEDV LJX and PEDV CV777 strains. The results indicated that PEDV LJX, but not PEDV CV777, could infect FHs 74 Int cells. Furthermore, we observed M gene mRNA transcripts and N protein expression in infected FHs 74 Int cells. A one-step growth curve showed that the highest viral titer of PEDV occurred at 12 h post infection. Viral particles in vacuoles were observed in FHs 74 Int cells at 24 h post infection. The results proved that human small intestinal epithelial cells are susceptible to PEDV infection, suggesting the possibility of cross-species transmission of PEDV.

This study evaluated the prevalence of BRV infection and its impact on the health of dairy cows at different growth stages, with a particular focus on milk-fed calves. BRV was detected in rectal swabs via RT–qPCR. In the total sample of 2400 dairy cows examined at three farms, 103 (4.29%) were found to be positive for BRV. Similarly, of the 480 milk-fed calves, 70 (14.58%) were also found to be positive for BRV. Negative binomial regression analysis revealed that older farms had higher average BRV positivity rates than new farms did and that the BRV positivity rate was higher in autumn than in the other three seasons. Additionally, BRV positivity rates gradually decreased as calf age increased. In milk-fed calves, BRV positivity was positively correlated with morbidity and mortality and negatively correlated with ADG and ADGPR. These findings provide valuable insights for farm management, particularly for older farms, highlighting the detrimental effects of BRV infection on milk-fed calves and underscoring the importance of targeted control strategies to reduce BRV prevalence and optimize dairy production efficiency.

The objective of this study was to elucidate the mechanism of action of the active components of Coptidis rhizoma against porcine epidemic diarrhea and to provide a theoretical foundation for further development of novel anti-PED therapeutic agents based on Coptidis rhizoma. The potential targets of Coptidis rhizoma against PEDV were identified through a comprehensive literature review and analysis using the TCMSP pharmacological database, SwissDrugDesign database, GeneCards database, and UniProt database. Subsequently, the STRING database and Cytoscape 3.7.1 software were employed to construct a protein–protein interaction (PPI) network and screen key targets. Gene Ontology (GO) function and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analysis were conducted on the identified targets. Molecular docking studies were performed using AutoDock 1.5.7 software to analyze the binding energy and modes of interaction between the active components of Coptidis rhizoma and the target proteins. The PyMOL 2.5.0a0 software was employed to visualize the docking results. Through comprehensive analysis, 74 specific targets of active components of Coptidis rhizoma against PEDV were identified. The core gene targets were screened, and an interaction network diagram was subsequently generated. Ultimately, 14 core targets were identified, with STAT3, ESR1, CASP3, and SRC exhibiting the most significant interactions. GO enrichment analysis revealed a total of 215 molecular items, including 48 biological function items, 139 biological process items, and 28 cellular component items. KEGG enrichment analysis identified 140 signaling pathways. Molecular docking analysis demonstrated that epiberberine and palmatine exhibited high binding affinity with STAT3 protein, worenine showed high binding affinity with ESR1 protein, obacunone exhibited high binding affinity with CASP3 protein, and epiberberine, obacunone, berberine, and berberruine exhibited high binding affinity with SRC protein. A network pharmacology and molecular docking technology approach was employed to screen six important active components of Coptidis rhizoma and four important potential targets against PEDV infection. The findings indicated that the active components of Coptidis rhizoma could serve as promising pharmaceutical agents for the prevention and control of PEDV, with significant potential for clinical application.

Peste des petits ruminants virus (PPRV), a single‐stranded negative‐sense RNA virus with an envelope, belongs to the Morbillivirus in the Paramyxoviridae family and is prevalent worldwide. PPRV infection causes fever, stomatitis, diarrhoea, pneumonia, abortion and other symptoms in small ruminants, with a high mortality rate that poses a significant threat to the sustainability and productivity of the small ruminant livestock sector. The PPRV virus particles have a diameter of approximately 400–500 nm and are composed of six structural proteins: nucleocapsid protein (N), phosphoprotein (P), envelope matrix protein (M), fusion protein (F), haemagglutinin protein (H) and large protein (L). Each protein has a distinct role in the virus's life cycle. Although the life cycle activities of PPRV have been widely reported, they are still limited. Research has demonstrated that PPRV has distinct adhesion factors on various cell surfaces, such as the epithelial cell adhesion factor nectin‐4 or the lymphocyte adhesion factor SLAM. After attaching to the cell, the F and H proteins on the PPRV membrane interact with each other, resulting in a conformational change in the F protein. This change allows the F protein to enter the cell through direct fusion with the host cell membrane. The virus enters the host cell via the outer vesicle endocytosis strategy and replicates and proliferates through the role of caveolin, actin, dynein and cholesterol on the host cell membrane. This review summarises the viral structure, attachment mechanism and transmembrane internalisation mechanism of PPRV. The aim of this review is to provide theoretical support for the development of PPRV inhibitors and the prevention and control of PPR.