Enterovirus 71 induces apoptosis in a Bax dependent manner / 中华实验和临床病毒学杂志

<p><b>OBJECTIVE</b>To explore the molecular mechanism of apoptosis induced by enterovirus 71 (EV71) infection.</p><p><b>METHODS</b>The effects of EV71 on Rhabdomyosarcoma (RD) cell viability were detected by CCK8 assay. EV71-induced apoptosis on RD cells were detected by Hoechst 33342 staining and Western blot targeting Caspase 3, 8 and PARP. Bax conformational change was detected by immunoprecipitation with Bax 6A7 antibody.</p><p><b>RESULTS</b>EV71 decreased the viability of RD cells and induces the activation of Caspase 3, 8 and PARP. Bax expression increases in RD cells after EV71 infection, and Bax conformational change also can be detected after EV71 infection.</p><p><b>CONCLUSION</b>Our study reveals that EV71 induces Caspase-dependent apoptosis by Bax conformational change.</p>

Identification A novel protein TRIM38 that activate NF-kappaB signaling pathways / 中华实验和临床病毒学杂志

<p><b>OBJECTIVE</b>The tripartite motif (TRIM) proteins are a family of more than 70 human members, however only a few of them have been well studied. It has been shown that TRIM proteins are involved in various cellular processes such as cell proliferation, differentiation, apoptosis and antiviral defense. The functions of TRIM38 are largely unknown. In this study we explore the effect of TRIM38 on NF-kappaB signaling pathway.</p><p><b>METHODS</b>293T cells were transfected with NF-kappaB-Luc and plasmids expressing TRIM38 and its mutants fused to Flag. 24 h after transfection, cells were harvested and luciferase activities were measured. Data are representative of three independent experiments with triplicate samples. The expression of proteins was analyzed by Western Blot.</p><p><b>RESULTS</b>TRIM38 could activate NF-kappaB signaling pathway. The mutants of TRIM38 affected the function of TRIM38. Only the mutant of SPRY domain deletion had no obviously influence of the function of TRIM38.</p><p><b>CONCLUSION</b>Our study reveals that NF-kappaB is activated in response to TRIM38.</p>

Study on the ubiquitin ligase activity of rotavirus NSP1 protein / 中华实验和临床病毒学杂志

<p><b>OBJECTIVE</b>To confirm the activity of non structural protein 1 (NSP1) of Rotavirus (RV) as E3 ubiquitin ligase by experiments and to provide some clues for NSP1 on the pathogenic mechanisms and replication of RV.</p><p><b>METHODS</b>The whole gene and RING deleted mutation gene of NSP1 were coloned into pEGFPC1 expression plasmid, and transfected into human embryonic kidney (HEK) 293 FT cells with pBlue-Script-HA-Ubiquitin. The expression of proteins were proved by using con-focal microscope and western blotting. The ubiquination of proteins were detected by co-immunoprecite.</p><p><b>RESULTS</b>The cellular proteins of HEK293FT are ubiquinated by NSP1 protein and NSP1 protein was self-ubiquinated also.</p><p><b>CONCLUSIONS</b>It revealed that RV NSP1 had the activity of E3 ubiquitin ligase and it may play a role on the modulate mechanisms of ubiquination.</p>