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

J Virol Methods. 1995 May;53(1):149-56. doi: 10.1016/0166-0934(95)00003-d.

Abstract

A small 14 amino acid oligopeptide tag (termed SV5-Pk) was fused onto the carboxy-terminus of simian immunodeficiency virus 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.

MeSH terms

  • Animals
  • Antigen-Antibody Complex / metabolism*
  • Baculoviridae
  • CD4 Antigens / metabolism*
  • Epitopes / genetics
  • Epitopes / metabolism*
  • Gene Products, env / genetics
  • Gene Products, env / metabolism*
  • Oligopeptides / genetics
  • Oligopeptides / metabolism*
  • Protein Binding
  • Protein Processing, Post-Translational
  • Recombinant Fusion Proteins / metabolism

Substances

  • Antigen-Antibody Complex
  • CD4 Antigens
  • Epitopes
  • Gene Products, env
  • Oligopeptides
  • Recombinant Fusion Proteins
  • SIV envelope glycoprotein gp160