Intercellular Exchange of Class II MHC Complexes: Ultrastructural Localization and Functional Presentation of Adsorbed I-A/Peptide Complexes

Abstract

Activated rat T cells, like human T cells, synthesize class II MHC glycoproteins (MHCII) and absorb MHCII from neighboring T cells. This study focused on interactions of myelin basic protein (MBP)-specific T cells that either synthesized MHCII or absorbed MHCII during activation to assess cellular structures associated with presentation of functional MHCII/peptide complexes. Synthesis of MHCII by CD4+TCR+ T cells involved I-A+ multivesicular MHC class II-like compartments (MIIC), release of MHCII+ vesicles, and expression of MHCII on a dendritic arborization. T-cell-mediated adsorption of MHCII was a saturable process that required close cell proximity, actin polymerization, and a permissive temperature. Adsorbed MHCII existed on vesicles that were intimately associated with the responder cell membrane. T cells bearing adsorbed vesicular MHCII presented antigen and were specifically lysed by CD4+ T cell responders, but when labeled with anti-MHCII antibody were not susceptible to complement-mediated lysis. In summary, this study reveals vesicular compartments associated with synthesis and intercellular exchange of functional MHCII/peptide complexes.