3. Antigen presentation to T cells by MHC Flashcards

1
Q

Which MHC presents viral epitopes?

A

MHC I

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2
Q

Which MHC presents cytosolic pathogens

A

MHC I

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3
Q

Which MHC presents intravesicular pathogens?

A

MHC II

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4
Q

Which MHC presents extracellular pathogens and toxins?

A

MHC II

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5
Q

Complex which transports peptides from the cytosol to the ER

A

TAP complex

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6
Q

How do cytokines change the proteasome to the immunoproteasome

A

Changes the beta subunit which alters the C terminal of the peptide which is broken down - makes C terminal into a hydrophobic AA which can bind to the MHC

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7
Q

What does the chaperone protein calnexin do?

A

Holds the alpha chains in place until beta 2 micro globulin binds

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8
Q

Which 2 chaperone proteins are involved once beta2 micro globulin binds?

A

Calreticulin holds the MHC in place in a complex with ERp57

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9
Q

How is the assembled MHC in the ER linked with the Tap complex?

A

Chaperone protein tapasin binds to the TAP complex

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10
Q

Which protein tries the peptides which enter the ER to 8-10AA length?

A

ERAAP

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11
Q

Example of virus that interfere with MHC I presentation and how

A

Adenovirus - protein 19 competes with tapasin and inhibits peptide loading into MHC I

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12
Q

Why doesn’t MHC II bind peptides going into the ER?

A

Invariant chain - sits as a trimer bound to 3 class II molecules at a time and blocks the binding grooves

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13
Q

What is the name of the fragment left behind once invariant chain is cleaved?

A

CLIP

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14
Q

What binds to MHC II and causes the CLIP to be released?

A

HLA-DM

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15
Q

Most polymorphic gene region for MHC II

A

DRB

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16
Q

Most polymorphic gene region for MHC I

A

B

17
Q

How does staphylococcus aureus cause toxic shock syndrome?

A

Cross links MHC II not in the groove, so can bind to any MHC or TCR and trigger a reaction.