Objective: To investigate the relationship between the EBV-induced liver injury and caspase-3/6 in children. Methods: Data of 249 patients seen from July 2016 to June 2017 who got infection with EBV were collected in second affiliated hospital of Wenzhou Medical University and the patients were divided into two groups; 168 patients who were diagnosed with hepatitis were selected for abnormal liver function group, laboratory tests were performed in acute phase and convalescent phase. Meanwhile the 81 patients, whose liver function were normal were selected for normal liver function group. Two ml of blood plasma was collected from each patient from both groups at the beginning and after a week’s treatment of the abnormal liver function group. The patients were aged from 1 to 14 years. The abnormal liver function group was further divided into four groups: young children (1-3 years old), preschool children (4-6 years old), school children (7-10 years old), teenagers (10-14 years old). Firstly, we recorded their alanine aminotransferase (ALT), aspartate aminotransferase (AST), total bilirubin (TBIL), gamma glutamyl transpeptidase (GGT) and direct bilirubin (DBIL), then by the use of enzyme linked immunosorbent assay (ELISA) we measured the protein level of caspase-3 and caspase-6. Results: In the group of abnormal liver function group, in the acute phase of the teenagers the level of ALT, caspase-3 and caspase-6 are improved significantly(927.2±82.5 vs. 158.5±41.4, P<0.001, 169.8±52.8 vs. 91.5±10.1, P<0.001, P<0.05, 82.2± 2.6, P<0.001, 965.8±31.5, P<0.001, 184.8±14.3, P<0.001), while the AST, TBLL, GGT and DBLL had no significant difference. Conclusions In the process of EBV-induced liver injury, there was a linear correlation between the increase of caspase-3/6 and ALT in the acute stage, suggesting that EBV-induced liver injury is closely related to caspase-3/6.

To develop Senecavirus A (SVA) virus-like particles (VLPs), a recombinant prokaryotic expression plasmid pET28a-SVA-VP031 was constructed to co-express SVA structural proteins VP0, VP3 and VP1, according to the genomic sequence of the field isolate CH-FJ-2017 after the recombinant proteins were expressed in E .coli system, and purified by Ni+ ion chromatographic method. The SVA VLPs self-assemble with a high yield in vitro buffer. A typical VLPs with an average diameter of 25-30 nm which is similar to native virions by using TEM detection. Animals immunized by SVA VLPs shown that the VLPs induced high titers neutralizing antibodies in Guinea pigs. This study indicated that the VLPs produced with co-expressing SVA structural proteins VP0, VP3 and VP1 in prokaryotic system is a promising candidate and laid an important foundation for the development of a novel SVA VLPs vaccine.
Animals ; Antibodies, Neutralizing ; Escherichia coli/genetics* ; Genomics ; Guinea Pigs ; Picornaviridae/genetics*