T-lymphocytes recognize short peptide antigens bound stably to polymorphic
major histocompatibility complex (MHC)-encoded glycoproteins expressed on t
he surface of antigen-presenting cells (APC). Two general pathways have evo
lved to generate peptide-MHC complexes. The MHC class II antigen processing
pathway provides a mechanism for sampling proteins present in endosomal co
mpartments. CD4+ regulatory T-cells recognize peptides bound to MHC class I
I molecules, which are selectively expressed in specialized APC that have e
fficient mechanisms for uptake of microbial antigens, and express costimula
tory molecules required for activating naive T-cells. CD8+ T-cells recogniz
e peptides bound to MHC class I molecules. Class I molecules are widely exp
ressed and bind peptides derived from the normal turnover of cellular prote
ins, providing a mechanism to display a sampling of cellular components to
be monitored for abnormalities by cytotoxic T-cells. Specialized accessory
proteins influence the efficiency of antigen presentation and the specifici
ty of immune responses through their roles in generating peptides, targetin
g antigen and MHC glycoproteins to selected intracellular compartments, and
by direct participation in the peptide-loading mechanism. It has recently
been discovered that some viruses have evolved ways to inhibit or subvert d
iscrete steps in antigen processing, providing a mechanism to evade immune
recognition.