Bombyx mori has become an important model organism for many fundamental studies. Bombyx mori nucleopolyhedrovirus (BmNPV) is a significant pathogen to Bombyx mori, yet also an efficient vector for recombinant protein production. A previous study indicated that acetylation plays many vital roles in several cellular processes of Bombyx mori while global phosphorylation pattern upon BmNPV infection remains elusive. Employing tandem mass tag (TMT) labeling and phosphorylation affinity enrichment followed by high-resolution LC-MS/MS analysis and intensive bioinformatics analysis, the quantitative phosphoproteome in Bombyx mori cells infected by BmNPV at 24 hpi with an MOI of 10 was extensively examined. Totally, 6480 phosphorylation sites in 2112 protein groups were identified, among which 4764 sites in 1717 proteins were quantified. Among the quantified proteins, 81 up-regulated and 25 down-regulated sites were identified with significant criteria (the quantitative ratio above 1.3 was considered as up-regulation and below 0.77 was considered as down-regulation) and with significant p-value (p < 0.05). Some proteins of BmNPV were also hyperphosphorylated during infection, such as P6.9, 39 K, LEF-6, Ac58-like protein, Ac82-like protein and BRO-D. The phosphorylated proteins were primary involved in several specific functions, out of which, we focused on the binding activity, protein synthesis, viral replication and apoptosis through kinase activity.

As the main pathogen associated with enzootic pneumonia (EP), Mycoplasma hyopneumoniae (Mhp) is globally prevalent and inflicts huge financial losses on the worldwide swine industry each year. However, the pathogenicity of Mhp has not been fully explained to date. Mhp invasion usually leads to long-term chronic infection and persistent lung colonization, suggesting that Mhp has developed effective immune evasion strategies. In this review, we offer more detailed information than was previously available about its immune evasion mechanisms through a systematic summary of the extant findings. Genetic mutation and post-translational protein processing confer Mhp the ability to alter its surface antigens. With the help of adhesins, Mhp can achieve cell invasion. And Mhp can modulate the host immune system through the induction of inflammation, incomplete autophagy, apoptosis, and the suppression of immune cell or immune effector activity. Furthermore, we offer the latest views on how we may treat Mhp infections and develop novel vaccines.

Background: Porcine reproductive and respiratory syndrome is caused by PRRSV. Modified live vaccines (MLVs) are widely used to control PRRSV infection, but their efficacy against the emerging NADC30-like variant remains unclear. This study aimed to evaluate the efficacy of a VR-2332-based MLV against the NADC30-like PRRSV strain HNjz15. Methods: Forty piglets were randomized into a vaccination group (MLV group), negative control group (NC group), and sentinel group. MLV group piglets were immunized with a commercial MLV at 3 weeks of age and challenged with HNjz15 (10^6.6 TCID₅₀/mL) at 21 days post-immunization. Clinical symptoms, viral load, antibody responses, cytokine levels, and lung lesions were monitored for 14 days post-challenge. Results: Although fever and respiratory symptoms were more pronounced in the NC group pigs than those of the MLV group (average percent occurrence: 65.2% vs. 52.9%), there was no statistical difference (p > 0.05) in the occurrence of respiratory symptoms between the two groups from 5 dpc. Reduced weight gains (by 40–53%) were also observed in the MLV and NC groups compared with the sentinels. The MLV and NC groups exhibited severe lung lesions, while there was no marked difference in viral RNA loads in serum and tissue samples between the MLV and NC groups (p > 0.05). The MLV vaccine induced a significant high level of N protein-specific antibodies compared to the NC group. There was also no significant difference in IFN-γ or TNF-α response to the HNjz15 challenge in both groups (p > 0.05). Conclusions: The VR-2332-based MLV does not provide adequate protection against challenge with the PRRSV-2 NADC30-like strain HNjz15.