Structural and functional analysis of the NS2 protein of porcine hemagglutinating encephalomyelitis virus
Porcine hemagglutinating encephalomyelitis virus (PHEV) is one of the coronaviruses susceptible to swine populations. The non-structural protein 2 (NS2) encoded by its genome is frequently deleted during the epidemic transmission of the virus, but its biological significance remains unclear. In order to explore the structure and function of the NS2 protein, this study utilized platforms such as ProtParam, TMHMM, NetPhos3.1, and ExPASy to analyze its physicochemical properties, spatial structure, genetic evolution, and post-translational modification characteristics. Meanwhile, the NS2 protein was expressed in eukaryotes and transcriptome sequencing was performed to clarify the biological processes it participates in. The results showed that the NS2 protein consists of 233 amino acids, with a molecular weight of 26.735 kDa, and a half-life of approximately 30 hours in mammals. It includes 13 phosphorylation sites, 2 N-glycosylation sites, and 1 O-glycosylation site, with no signal peptide and strong hydrophilicity. The a-helix accounts for the highest proportion in NS2 (43.78%), followed by random coils (36.05%). The homology of the NS2 protein between the epidemic strains PHEV-CC14 and PHEV-JL/2008 in Northeast China is 99.57%. The NS2 protein is widely involved in the regulation of nerve-related functions, such as axon guidance and synaptic development. This study preliminarily clarified the biological function of the NS2 protein, providing a new perspective for understanding the pathogenic mechanism of PHEV.
