Use of TrpE fusion protein to identify antigenic domains within the BIV envelope protein

Ping Chen, Zhen Qian Liu, Charles Wood

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Nine different recombinant clones spanning various regions of the bovine immunodeficiency-like virus (BIV) envelope gene open reading frame were generated. These clones span the entire external glycoprotein as well as the transmembrane glycoprotein region. These proteins were expressed as fusions to the TrpE protein in E. coli. The levels of recombinant protein expressed varied, some clones expressed enough protein that can be detected in a Coomassie blue-stained gel, whereas other proteins could only be detected by Western blot analyses. A recombinant env protein representing the extracellular domain of the env protein was detected by BIV-infected bovine sera. In addition, a 134 amino acid peptide which may represent a major immunoreactive epitope was identified. This peptide is located at the amino terminus of the transmembrane glycoprotein and was specifically recognized by all BIV-infected calf sera tested. The identification of this epitope and the use of recombinant envelope protein will enable us to develop a more effective screening test to study the epidemiology of BIV infection.

Original languageEnglish (US)
Pages (from-to)331-343
Number of pages13
JournalJournal of Virological Methods
Volume47
Issue number3
DOIs
StatePublished - May 1994

Keywords

  • (E. coli)
  • Bovine immunodeficiency-like virus
  • Envelope protein
  • Fusion protein
  • TrpE

ASJC Scopus subject areas

  • Virology

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