Purification and partial characterization of R5, R5X4, and X4 HIV-1 subtype C envelope glycoproteins expressed in insect cells

J Med Virol. 2005 Aug;76(4):459-63. doi: 10.1002/jmv.20383.

Abstract

Biological properties of four recombinant HIV-1 subtype C envelope glycoproteins from viruses with different phenotypic characteristics (CCR5 and/or CXCR4-utilizing) were investigated. The gp160 genes were cloned, expressed in Spodoptera frugiperda insect cells, purified, and their biological characteristics were examined. The conformational and functional integrity of the HIV-1 subtype C rgp160 was intact since they reacted with the A32, C11, IgG1b12, 7B2, and 17b conformational dependant monoclonal antibodies (MAb), sCD4, and patient sera. Baculovirus derived rgp160 can be used for further structural, functional, antigenic, and immunological studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Baculoviridae / genetics
  • Cell Line
  • Cloning, Molecular
  • HIV Antibodies / immunology
  • HIV Envelope Protein gp160 / chemistry
  • HIV Envelope Protein gp160 / genetics
  • HIV Envelope Protein gp160 / immunology*
  • HIV Envelope Protein gp160 / isolation & purification*
  • HIV-1 / chemistry*
  • HIV-1 / classification*
  • HIV-1 / isolation & purification
  • Neutralization Tests
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Recombinant Proteins / isolation & purification
  • Spodoptera

Substances

  • Antibodies, Monoclonal
  • HIV Antibodies
  • HIV Envelope Protein gp160
  • Recombinant Proteins