| First Author | Schirmbeck R | Year | 1997 |
| Journal | Eur J Immunol | Volume | 27 |
| Issue | 12 | Pages | 3471-84 |
| PubMed ID | 9464837 | Mgi Jnum | J:45132 |
| Mgi Id | MGI:1194438 | Doi | 10.1002/eji.1830271248 |
| Citation | Schirmbeck R, et al. (1997) Processing of exogenous hepatitis B surface antigen particles for Ld-restricted epitope presentation depends on exogenous beta2-microglobulin. Eur J Immunol 27(12):3471-84 |
| abstractText | Processing of exogenous hepatitis B surface antigen (HBsAg) particles in an endolysosomal compartment generates peptides that bind to the major histocompatibility complex (MHC) class I molecule Ld and are presented to CD8+ cytotoxic T lymphocytes. Surface-associated empty MHC class I molecules associated neither with peptide, nor with beta2-microglobulin (beta2m) are involved in this alternative processing pathway of exogenous antigen for MHC class I-restricted peptide presentation. Here, we demonstrate that internalization of exogenous beta2m is required for endolysosomal generation of presentation-competent, trimeric Ld molecules in cells pulsed with exogenous HBsAg. These data point to a role of endocytosed exogenous beta2m in the endolysosomal assembly of MHC class I molecules that present peptides from endosomally processed, exogenous antigen. |
