Attachment of an oligopeptide epitope to the C-terminus of recombinant SIV gp160 facilitates the construction of SMAA complexes while preserving CD4 binding

T. Hanke, D. F. Young, C. Doyle, I. Jones, R. E. Randall*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

A small 14 amino acid oligopeptide tag (termed SV5-Pk) was fused onto the carboxy-terminus of simian immunodeficiency viras gp160 expressed from a recombinant baculovirus. The presence of the Pk tag had no obvious effect on the expression and glycosylation of gp160 and did not interfere either with CD4 binding or with cleavage at its maturation site by the protease furin. The presence of the Pk tag did, however, facilitate the simplified purification of full-length gp160 and its incorporation into immunogenic solid matrix-antibody-antigen (SMAA) complexes.

Original languageEnglish
Pages (from-to)149-156
Number of pages8
JournalJournal of Virological Methods
Volume53
Issue number1
DOIs
Publication statusPublished - 1 Jan 1995

Keywords

  • gp160
  • Purification
  • SIV

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