Antibodies induced by liposomal protein exhibit dual binding to protein and lipid epitopes

Nicos Karasavvas, Zoltan Beck, James Tong, Gary R. Matyas, Mangala Rao, Francine E. McCutchan, Nelson L. Michael, Carl R. Alving*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Natural polyreactive antibodies can accommodate chemically unrelated epitopes, such as lipids and proteins, in a single antigen binding site. Because liposomes containing lipid A as an adjuvant can induce antibodies directed against specific lipids, we immunized mice with liposomes containing lipid A together with a protein or peptide antigen to determine whether monoclonal antibodies generated after immunization would be specifically directed both to the liposomal lipid (either cholesterol or galactosylceramide) and also to the accompanying liposomal protein or peptide. Monoclonal antibodies were obtained that bound, by ELISA, to cholesterol and to recombinant gp140 envelope protein from HIV-1, or to galactosylceramide and to an HIV-1 envelope peptide. Surface plasmon resonance studies with the former antibody showed that the liposomal cholesterol and liposomal gp140 each contributed to the overall binding energy of the antibody to liposomes containing cholesterol and protein.

Original languageEnglish
Pages (from-to)982-987
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 22 Feb 2008
Externally publishedYes


  • Antibodies to cholesterol
  • Antibodies to galactosylceramide
  • Antibody binding specificity
  • Lipid A
  • Liposomes
  • Monoclonal antibodies
  • Natural antibodies
  • Polyreactive antibodies
  • Surface plasmon resonance


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