L8 - Antigen Presentation Flashcards
What is the structure of MHC I?
3 extracellular domains, α1 + α2 (peptide binding region), α3 (Ig-like region) and a β2 microglobulin
Are the peptides fixed within the MHC I molecule?
Yes
Describe MHC I Antigen Presentation
- Pathogen infection, synthesis of viral antigens
- Proteasome degrades antigen (cytoplasm)
- Peptides enter ER via TAP
- Peptides inserted onto MHC I
- MHC I / Peptide complex transported along secretory pathway to plasma membrane
What is the structure of MHC II?
2 chains, α chain (α1 and α2) and β chain (β1 and β2). The 1s are peptide binding regions, the 2s are Ig-like regions
Are the peptides fixed within the MHC II molecule?
No
Describe MHC II Antigen Presentation
- Antigen presenting cell endocytoses antigen
- Endosomal proteases degrade antigen
- Antigenic peptides contained in endosomal compartments
- MHC II molecules synthesized in the ER (must travel to endosomal compartments)
- Binds with Ii, transported to endosomes
- Binding to antigenic peptides via Ii degradation
- Transported to plasma membrane
How do the conditions change between early endosomes, late endosomes and lysosomes?
- pH decreases
- Reducing condition increases
- Proteases increases
What does MHC II associate with to prevent binding of ER components?
Invariant chain (Ii) - CLiP region of Ii occupies peptide binding site
How does MHC II associate with Ii?
Three MHC II αβ dimers associate in the ER with three Ii to form a [αβIi]3 nonamer
Do MHC II molecules bind pre-formed antigenic peptides or do they bind longer peptides that are later trimmed?
Most likely both exist