Preferential antibody recognition of structurally distinct HIV-1 gp 120 molecules

T. C. VanCott, F. R. Bethke, V. Kalyanaraman, D. S. Burke, R. R. Redfield, D. L. Birx

Research output: Contribution to journalArticle

Abstract

We have developed an assay, using a biosensor matrix and surface plasmon resonance, that rapidly and reproducibly measures antibody reactivity to human immunodeficiency virus type 1 (HIV-1) gp 120 in various structural conformations. In particular, antibodies displaying preferential reactivity to a CD4-binding competent (“native,” rgp 120) or CD4-binding incompetent (“reduced,” rcmgp 120) monomeric gp 120 molecule were distinguished. This technique has advantages over conventional enzyme-linked immunosorbent assay (ELISA) methodology in which it is difficult to control the concentration of protein adsorbed to the ELISA wells and a significant disruption of protein structure occurs on adsorption. A population of gp 120 molecules that lacked CD4 receptor binding capacity and bound antibodies specific for reduced gp 120 was found in several native gp 120 preparations. The relative amount of this CD4-binding incompetent population varied among the various preparations studied. This presence of CD4-binding incompetent molecules within various native recombinant gp 120 preparations may have implications for HIV-1 envelope vaccine development. By measuring antibody-binding ratios, several monoclonal antibodies were identified, which, although elicited by immunization with various native gp 120 preparations, bound specifically to reduced gp 120. The ability to screen antibody specificity against HIV-1 envelope proteins with different conformations will assist in determining the quality of antibodies induced by various HIV-1 envelope vaccine candidates.

Original languageEnglish (US)
Pages (from-to)1103-1115
Number of pages13
JournalJournal of acquired immune deficiency syndromes
Volume7
Issue number11
StatePublished - Nov 1994

Keywords

  • AIDS vaccines
  • Biosensors
  • Biospecific interaction analysis
  • Human immunodeficiency virus
  • gp 120 envelope

ASJC Scopus subject areas

  • Infectious Diseases
  • Pharmacology (medical)

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  • Cite this

    VanCott, T. C., Bethke, F. R., Kalyanaraman, V., Burke, D. S., Redfield, R. R., & Birx, D. L. (1994). Preferential antibody recognition of structurally distinct HIV-1 gp 120 molecules. Journal of acquired immune deficiency syndromes, 7(11), 1103-1115.