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9 BMD 430 lecture 9

front 1

1. What are the two major compartments of the cell?
A. Cytosol and mitochondria
B. Cytosol and nucleus
C. Cytosol and vesicular system
D. ER and Golgi

back 1

B. Cytosol and nucleus

front 2

2. Why are the cytosol and vesicular system kept separate?
A. To regulate calcium
B. To prevent viral and bacterial overlap
C. Because viruses exploit cytosol, bacteria exploit vesicular compartments
D. To maintain osmotic balance

back 2

C. Because viruses exploit cytosol, bacteria exploit vesicular compartments

front 3

3. Which type of antigen is presented by MHC class I molecules?
A. Exogenous
B. Endogenous
C. Lipid
D. Polysaccharide

back 3

B. Endogenous

front 4

4. What is the role of TAP1/2 in antigen presentation?
A. Binds peptide to MHC
B. Transports peptides into the ER using ATP
C. Degrades misfolded proteins
D. Removes CLIP from MHC class II

back 4

B. Transports peptides into the ER using ATP

front 5

5. What is the function of calnexin?
A. Transports peptides into the cytosol
B. Ensures proper folding of MHC class I before β2-microglobulin binds
C. Removes CLIP from MHC class II
D. Cuts peptides to 8 amino acids

back 5

B. Ensures proper folding of MHC class I before β2-microglobulin binds

front 6

6. Which enzyme trims peptides in the ER to the correct size for MHC class I binding?

A. Tapasin

B. ERAP

C. Calreticulin

D. ERp57

back 6

B. ERAP

front 7

7. The proteasome breaks down:

A. Damaged DNA

B. Misfolded or old proteins into small peptides

C. Cytokines

D. Lipids

back 7

B. Misfolded or old proteins into small peptides

front 8

8. The immunoproteasome is formed in response to:

A. Heat shock

B. Cytokines such as IFN-γ

C. Nutrient deficiency

D. Lipid accumulation

back 8

B. Cytokines such as IFN-γ

front 9

9. What is the purpose of the invariant chain (Ii)?

A. Loads peptide onto MHC II

B. Blocks premature peptide binding and directs MHC II to endosome

C. Removes CLIP from MHC II

D. Prevents folding of MHC I

back 9

B. Blocks premature peptide binding and directs MHC II to endosome

front 10

10. The CLIP fragment is:

A. A part of the invariant chain that remains in the peptide-binding groove

B. A transport protein

C. A cytokine

D. A TAP cofactor

back 10

A. A part of the invariant chain that remains in the peptide-binding groove

front 11

11. What does HLA-DM do?

A. Blocks CLIP binding

B. Degrades peptides

C. Removes CLIP and helps peptide loading on MHC II

D. Recycles MHC II to the ER

back 11

C. Removes CLIP and helps peptide loading on MHC II

front 12

12. What family of molecules presents lipid antigens?

A. CD3

B. CD4

C. CD1

D. TAP

back 12

C. CD1

front 13

13. CD1 molecules are structurally similar to:

A. MHC class I

B. MHC class II

C. Both A and B

D. Neither

back 13

A. MHC class I

front 14

14. Which antigen-presenting cell initiates adaptive immunity?

A. Macrophage

B. B cell

C. Dendritic cell

D. Neutrophil

back 14

C. Dendritic cell

front 15

15. Which MHC class is associated with exogenous antigen presentation?

A. MHC class I

B. MHC class II

C. CD1

D. HLA-C

back 15

B. MHC class II

front 16

ERAP

back 16

Removes amino acids from peptide N-terminus

front 17

Tapasin

back 17

Ensures high-affinity peptide binds to MHC I

front 18

Calreticulin

back 18

Chaperone protein assisting MHC folding

front 19

TAP1/2

back 19

Transports peptides into the ER using ATP

front 20

CLIP

back 20

Blocks premature peptide binding to MHC II

front 21

16. Define self-antigen vs. non-self antigen and explain why presentation of self-antigen is normal.

back 21

Self = own proteins; Non-self = foreign. Self presentation = normal immune tolerance.

front 22

17. What is ERAD, and why is it necessary for protein quality control?

back 22

ERAD = ER-associated degradation of misfolded proteins

front 23

18. What is the peptide loading complex (PLC) and what are its components?

back 23

PLC = Tapasin, TAP1/2, ERp57, Calreticulin. Loads peptide onto MHC I

front 24

19. Define peptide editing and explain the role of tapasin.

back 24

Peptide editing = Tapasin ensures tight peptide binding to MHC I.

front 25

20. What is immunodominance? Name the three strength levels of epitopes.

back 25

Immunodominance = strongest epitope response (immunodominant > subdominant > cryptic).

front 26

21. Explain the role of cross-presentation and why it’s important.

back 26

Cross-presentation = exogenous antigen presented via MHC I → activates CD8+ T cells.

front 27

22. What are the three main antigen-presenting cells (APCs)?

back 27

Dendritic cells, macrophages, B cells.

front 28

23. Describe the process by which dendritic cells activate T cells.

back 28

DCs phagocytose antigen → migrate to lymph node → present via MHC II → activate naive T cells.

front 29

24. What are the two problems the invariant chain (Ii) solves for MHC class II?

back 29

Ii blocks endogenous peptide binding and directs MHC II to endosome.

front 30

25. Explain how MHC class I and MHC class II differ in antigen origin and the T cell type they activate.

back 30

MHC I = endogenous/CD8+; MHC II = exogenous/CD4+.