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		题名	作者	年代	出处	被引量
	1	丙肝病毒E2包膜糖蛋白研究进展显示文摘	许可张云	2005	中国公共卫生2005，21，10：	1
	2	Purification and application of C-terminally truncated hepatitis C virus El proteins expressed in Escherichia coli显示文摘AIM: To explore the possibility of expressing hepatitis C virus (HCV) envelope protein 1 (E1) in Escherichia coli (E. coli)and to test the purified recombinant E1 proteins for clinical and research applications.METHODS: C-terminally truncated E1 fragments were expressed in E. coli as hexa-histidine-tagged fusion proteins. The expression products were purified under denaturing conditions using immobilized-metal affinity chromatography. Purified E1 proteins were used to immunize rabbits. Rabbit anti-sera thus obtained were reacted with both E. coli- and mammalian cell-expressed E1 glycoproteins as detected by Western blot.RESULTS: Full-length E1 protein proved difficult to express in E. coli. C-terminally truncated E1 was successfully expressed in E. colias hexa-histidine-tagged recombinant fusion protein and was purified under denaturing conditionson Ni^2+-NTA agarose. Rabbit anti-sera raised against purified recombinant E1 specifically reacted with mammalian cell-expressed E1 giycoproteins in Western blot. Furthermore, E. coli-derived E1 protein was able to detect animal antibodies elicited by El-based DNA immunization.CONCLUSION: These results demonstrate that the prokaryotically expressed E1 proteins share identical epitopes with eukaryotically expressed E1 glycoprotein. The E. coli-derived E1 proteins and corresponding antisera can become useful tools in anti-HCV vaccine research.	JingLiu Li-XinZhu Yu-YingKong Guang-DiLi YuanWang	2005	World Journal of Gastroenterology2005，11，4：	0

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