Characterization and kinetics of MHC class I-restricted presentation of a soluble antigen delivered by liposomes.
We describe in this report the characterization and kinetics of MHC class I-restricted presentation of a soluble antigen delivered by liposomes. pH-sensitive liposomes delivered ovalbumin (OVA) to the class I pathway more efficiently than pH-insensitive liposomes; the latter showed competence in the class I-restricted sensitization only when a large antigen loading dose was used. Such sensitization of EL4 cells resulted from substantial delivery of the ingested liposomal OVA to the cytosolic compartment as revealed with immunogold electron microscopy. Most of the ingested liposomal OVA were rapidly catabolized and released into the extracellular medium. The residual processed antigen took about 2 h to egress to the cell surface for recognition by CTL. The liposome-mediated antigen presentation exhibited a transient kinetics which was manipulable with antigen dose. Brefeldin A, an ER-to-Golgi transport inhibitor, strongly inhibited such presentation. The antigens displayed on the cell surface could also be removed by a brief acid wash of the cells and subsequently reappeared on the surface if an intracellular pool of antigen existed at the time of acid wash.
Zhou
F
F
Department of Pharmacology, University of Pittsburgh School of Medicine, PA.
Watkins
S C
SC
Huang
L
L
D000818:Animals; D000938:Antigen-Presenting Cells / Q000276:immunology*; D000941:Antigens / Q000008:administration & dosage* / Q000378:metabolism; D003601:Cytotoxicity Tests, Immunologic; D005260:Female; D015395:Histocompatibility Antigens Class I / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D008081:Liposomes; D051379:Mice; D008810:Mice, Inbred C57BL; D016253:Microscopy, Immunoelectron; D010047:Ovalbumin / Q000008:administration & dosage / Q000276:immunology / Q000493:pharmacokinetics; D012995:Solubility; D014407:Tumor Cells, Cultured
D000941:Antigens; D015395:Histocompatibility Antigens Class I; D008081:Liposomes; D010047:Ovalbumin