B subunit of cholera toxin fused with VP7 from GCRV (grass carp reovirus) was expressed in E. coli and folds into an active protein.
作者： Yan Zhao , Binglian Xu , Borun Zhu , Xue Liu , Dongchun Yan
DOI: 10.1016/J.IJBIOMAC.2020.02.215
关键词:
摘要: Abstract Grass carp reovirus (GCRV) is one of the most serious pathogens threatening grass (Ctenopharyngodon idella) production and results in high mortality China. To obtain a genetically engineered oral vaccine against GCRV, cholera toxin B subunit (CTB) Vibrio cholerae was fused to VP7 (CTB-VP7) transformed into BL21(DE3) for expression. SDS-PAGE Western blotting showed that purified rCTB-VP7 fusion protein (rCTB-VP7) approximately 49.0 kDa. The monomeric nature through multistage purification binding affinity GM1, receptor biologically active CTB. not vulnerable disassembly by SDS but 2-mercaptoethanol. stable highly at room temperature. experiment between GM1 also confirms effects acid alkalinity solution on structure rCTB-VP7. bound with different affinities under temperatures pH values. Prokaryotic expression characterized easy had strong force 37 °C pH 7.4. Our suggest has potential as an protection GCRV aquaculture.
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