Purification and application of C-terminally truncated hepatitis C virus E1 proteins expressed in Escherichia coli.

ABSTRACT:

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. coli as hexa-histid

SUBMITTER: Liu J 

PROVIDER: S-EPMC4250799 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature