'Empty' Ld molecules capture peptides from endocytosed hepatitis B surface antigen particles for major histocompatibility complex class I-restricted presentation.

Peptides recognized by CD8+ cytotoxic T lymphocytes in the context of major histocompatibility complex (MHC) class I molecules are usually derived from endogenous proteins synthesized within the cell. Exogenous 22-nm hepatitis B surface antigen (HBsAg) particles are taken up by many cells, and are processed in a novel peptide-transporter-independent, endosomal or lysosomal pathway for class I (Ld)-restricted epitope presentation. Here, we present evidence that 'empty' Ld molecules derived from the cell surface are involved in presenting antigenic peptides from endocytosed HBsAg particles. Intracellular assembly of presentation-competent, trimeric Ld molecules required endocytosis of the exogenous antigen and 'empty' Ld molecules. These data assign a functional role to surface-associated, 'empty' MHC class I molecules.