2006, Number S2
Processing and presentation of antigen by MHC molecules classes I and II
Pérez RM
Language: Spanish
References: 7
Page: 7-10
PDF size: 312.81 Kb.
ABSTRACT
The major histocompatibility complex molecules (MHC) bind self or foreign antigens and present them to T lymphocytes. Newly synthesized alpha chain of MHC class I is associated with calnexin protein in the endoplasmic reticulum (ER). The alpha chain then binds with β2-microglobulin and calnexin is substituted by calreticulin. This complex has association with other chaperone proteins, ERp57 and tapasin. MHC class I molecules are loaded with peptides of length 8-11 aminoacids derived from intracellular proteins, which were hydrolyzed by proteasomes. These peptides are translocated into the lumen of the ER by TAP (transporter associated with antigen processing), where they can proceed to bind MHC class I groove. The newly synthesized MHC class II heterodimer is escorted by the invariant protein (Ii) from the ER into the MCII and prevents premature association of any antigenic peptide by insertion of CLIP (class II-associated invariant chain peptide) within the peptide-binding site. After Ii is degraded by proteolytic enzymes, CLIP is removed by HLA-DM molecule and a peptide of 25 aminoacids is loading into the MHC class II groove. Finally the MHC class II molecules, on the surface of antigen presenting cells, present antigenic peptides to CD4+ T cells.REFERENCES