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|標題:||Expression of recombinant envelope protein of Japanese encephalitis virus YL strain in Escherichia coli possesses hemagglutination activity||作者:||Chen, S.O.
|關鍵字:||envelope glycoprotein;hemagglutination;Japanese encephalitis virus;YL;strain;phylogenetic analysis;swiss-model;in-vitro;flavivirus;virulence;cloning;mutants;genome;cdna;mice||Project:||Virus Genes||期刊/報告no：:||Virus Genes, Volume 28, Issue 2, Page(s) 215-221.||摘要:||
The nucleotide sequence of glycoprotein E of YL vaccine strain was cloned, sequenced and expressed in E. coli. Phylogenetic analysis of envelope ( E) amino acid sequences of 18 JEVs in GenBank showed that the vaccine strain YL closer to the virulent strain HVI which is a Taiwanese isolate. We found only two amino acid mutations (K-138 and G-389) of E protein might lead viral attenuation in YL. In this study, we used pRSET vector system to construct three recombinant plasmids (pRSET/F1R1, pRSET/ F2R2 and pRSET/F1R2), which encoded and expressed different or overlapping amino acid region of E protein. The antigenicity and hemagglutination activity of these recombinant proteins were examined by western blotting and hemagglutination test, respectively. Our results demonstrated that the recombinant protein of pRSET/F1R2 possesses predominant antigenicity and hemagglutination activity.
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