Liposome-mediated peptide loading of MHC-DR molecules in vivo

FEBS Lett. 1997 Jun 2;409(1):91-5. doi: 10.1016/s0014-5793(97)00493-6.

Abstract

Amino acid residues 3-15 of mycobacterial HSP60 define a dominant T-cell epitope for HLA-DR3+ve humans and Mamu-DR3+ve rhesus monkeys. Our results show that Mamu-DR3 molecules on PBMC can be efficiently loaded in vivo with the above-mentioned peptides when they are intravenously injected encapsulated in liposomes, but not in the free form. Mamu-DR3 loading is abolished by encapsulation of a nonstimulatory peptide. These results have implications for the delivery of therapeutic peptides in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding, Competitive / drug effects
  • Binding, Competitive / immunology
  • Drug Carriers
  • Female
  • Histocompatibility Antigens Class II / administration & dosage*
  • Histocompatibility Antigens Class II / drug effects
  • Histocompatibility Antigens Class II / metabolism
  • Injections, Intravenous
  • Liposomes / administration & dosage
  • Liposomes / pharmacology*
  • Lymphocyte Activation / drug effects
  • Macaca mulatta
  • Male
  • Peptides / administration & dosage*
  • Peptides / immunology*
  • Peptides / metabolism
  • Protein Binding / drug effects
  • Protein Binding / immunology
  • T-Lymphocytes / immunology

Substances

  • Drug Carriers
  • Histocompatibility Antigens Class II
  • Liposomes
  • Peptides