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

Jennifer Kovacs-Nolan, Erika Sasaki, Dongwan Yoo, Yoshinori Mine

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)1183-1188
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number5
StatePublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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