The expression and purification of VP8* core protein of the rotavirus P 6 Genotype LL4260 / 中华实验和临床病毒学杂志

ABSTRACT

Objective@#The VP8* core protein of rotavirus P[6] genotype LL4260 was purified by prokaryotic expression, which is important for further study of protein structure and function.@*Methods@#The P[6] genotype LL4260 strain was obtained by PCR.The recombinant plasmid pET30 a-LL4260VP8*core was inserted into pET30 a vector and transformed into BL21 (DE3) competent cells with the correct recombinant plasmid. The expressed protein is purified by affinity chromatography and molecular sieve chromatography.@*Results@#The pET30 a-LL4260VP8* core region protein is soluble in the supernatant and proteins of approximately 22 kDa are identified by electrophoresis using purified proteins.@*Conclusions@#In this study, LL4260 containing pET30 a-LL4260VP8* core plasmid was successfully constructed and LL4260 strain VP8* protein was expressed.