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Cloning and expression of human rotavirus spike protein, VP8*, in Escherichia coli.

Abstract：

:A system for the expression and purification of soluble VP8*, part of the human rotavirus (HRV) spike protein, was established by expressing VP8* as a fusion protein with glutathione S-transferase (GST). VP8 cDNA, from the Wa strain of HRV, was prepared by RT-PCR, cloned into a pUC18 plasmid, and inserted into a pGEX-4T-2 GST fusion vector. The GST-VP8* fusion protein was expressed in Escherichia coli, and the VP8* was purified by Glutathione Sepharose 4B affinity chromatography, yielding 1.8 mg VP8*/L culture. The purified VP8* was used to vaccinate chickens, eliciting antibodies which displayed high neutralization activity against the Wa strain of HRV, suggesting its use for the induction of specific neutralizing antibodies for potential immunotherapeutic applications for the prevention of HRV infection.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kovacs-Nolan J,Sasaki E,Yoo D,Mine Y

doi

10.1006/bbrc.2001.4717

subject

Has Abstract

pub_date

2001-04-20 00:00:00

pages

1183-8

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94717-5

journal_volume

282

pub_type

杂志文章

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