Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein.

Published

Journal Article

By analogy to other retroviruses, the major envelope glycoprotein, gp120, of human T-lymphotropic virus type III (HTLV-III) is a probable target for neutralizing antibody. This antigen has been purified from H9 cells chronically infected with the HTLV-IIIB prototype strain. Several goats immunized with the gp120 produced antibodies that neutralized infection of H9 cells by the homologous virus isolate. These same sera failed to neutralize the divergent HTLV-IIIRF isolate. Individuals infected with HTLV-III commonly develop antibodies to gp120 that could be isolated by using the gp120 antigen coupled to an immunoadsorbent resin. The antibody fraction that bound tightly to such a resin was found to neutralize the IIIB but not the RF isolate in a similar fashion as the goat anti-gp120 sera. However, the nonbinding fraction (effluent) from the resin also contained neutralizing activity that was able to block infection by both virus isolates with similar efficacy. Human antibodies to the other virus envelope gene product, the transmembrane gp41, were also affinity purified by utilizing the recombinant peptide 121, but these failed to influence infection by either virus isolate.

Full Text

Duke Authors

Cited Authors

  • Matthews, TJ; Langlois, AJ; Robey, WG; Chang, NT; Gallo, RC; Fischinger, PJ; Bolognesi, DP

Published Date

  • December 1986

Published In

Volume / Issue

  • 83 / 24

Start / End Page

  • 9709 - 9713

PubMed ID

  • 2432599

Pubmed Central ID

  • 2432599

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.83.24.9709

Language

  • eng

Conference Location

  • United States