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Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
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Intercellular exchange of class II MHC complexes: ultrastructural localization and functional presentation of

D M Patel1, R W Dudek, M D Mannie

  • 1Department of Microbiology and Immunology, East Carolina University School of Medicine, Greenville, North Carolina 27858-4354, USA.

Cellular Immunology
|March 21, 2002
PubMed

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.

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