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A new strategy for full-length Ebola virus glycoprotein expression in E.coli.

Abstract：

:Ebola virus (EBOV) causes severe hemorrhagic fever in humans and non-human primates with high rates of fatality. Glycoprotein (GP) is the only envelope protein of EBOV, which may play a critical role in virus attachment and entry as well as stimulating host protective immune responses. However, the lack of expression of full-length GP in Escherichia coli hinders the further study of its function in viral pathogenesis. In this study, the vp40 gene was fused to the full-length gp gene and cloned into a prokaryotic expression vector. We showed that the VP40-GP and GP-VP40 fusion proteins could be expressed in E.coli at 16 °C. In addition, it was shown that the position of vp40 in the fusion proteins affected the yields of the fusion proteins, with a higher level of production of the fusion protein when vp40 was upstream of gp compared to when it was downstream. The results provide a strategy for the expression of a large quantity of EBOV full-length GP, which is of importance for further analyzing the relationship between the structure and function of GP and developing an antibody for the treatment of EBOV infection.

journal_name

Virol Sin

journal_title

Virologica Sinica

authors

Zai J,Yi Y,Xia H,Zhang B,Yuan Z

doi

10.1007/s12250-016-3845-y

subject

Has Abstract

pub_date

2016-12-01 00:00:00

pages

500-508

issue

6

eissn

1674-0769

issn

1995-820X

pii

10.1007/s12250-016-3845-y

journal_volume

31

pub_type

杂志文章

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