Immunology 6 Flashcards

1
Q

MHC class 1 is expressed in ..?

A

All nucleated cells

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2
Q

MHC class2 is expressed in …?

A

professional APCs

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3
Q

What domain of MHC class 2 binds CD4?

A

beta domain

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4
Q

What domain of MHC class 1 binds CD8?

A

alpha domain

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5
Q

TCR binds both the antigen and MHC molecule. True or False?

A

True

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6
Q

Which of MHC Class-1 and Class-2 has a relatively closed groove so the binding occurs in pockets at the ends of the groove?

A

Class-1

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7
Q

Describe the MHC class-2 antigen binding groove.

A

The groove is much more open so can accommodate bigger peptides and bind all along the length of the binding site.

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8
Q

Where are peptides for MHC class-2 derived from?

A

Extracellular peptides.
(MHC-2 Synthesised in cell, translocate to ER, vesicles bud off and bind with peptides in antigen-processing compartment)

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9
Q

Where are peptides for MHC class-1 derived from?

A

Intracellular peptides.

Often from when a cell is infected with a virus.

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10
Q

Where are viral antigen broken down for presentation on MHC class-1?

A
proteasome
(peptide then binds to class 1 molecule in golgi and transported to surface.)
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11
Q

What does interferon-gamma turn the proteasome into?

A

The immunoproteosome.

This contains additional subunits.

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12
Q

What additional subunits does immunoproteosome contain that proteasome doesn’t?

A

LMP2, LMP7, MECL1

These change specificity of cleavage.

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13
Q

What is the difference in function between immunoproteosome and proteasome?

A

There is an increased cleavage after hydrophobic residues so there are more peptides with C terminal hydrophobic residues which favours binding to MHC class 1.

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14
Q

What is TAP?

A

Transporter for antigen processing. Transport degraded peptides from proteasome to endoplasmic reticulum

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15
Q

What does Calnexin do?

A

Stabilises MHC class 1 heavy chain until beta-globulin binds and releases calnexin.

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16
Q

In the endoplasmic reticulum what is the function of the chaperone proteins that interact with the MHC class 1?

A

Interact with MHC class I to hold it in open configuration so peptides can bind. They then dissociate.

17
Q

When a MHC class-1 molecule is loaded with a peptide that has too long an N-terminus what cleaves the peptide?

A

ERAP - an aminopeptidase

18
Q

What cleaves the invariant chain from the MHC class-2?

A

cathepsin S cleaves invariant chain forming CLIP (class-2 associated invariant peptide)

19
Q

What is the molecule that facilitates the release of CLIP called?

A

HLA-DM

20
Q

Is the Li-MHC 2 transported to the antigen processing compartment intact?

A

Yes

21
Q

What is the rare event cross-presentation?

A

When macrophages ingest an infected cell and degrade it. Peptides of the infected cells enter the endoplasmic reticulum and form MHC I complexes and are presented on the outside

22
Q

What is the major histomcompatibility complex?

A

A cluster of genes associated with antigen processing and presenting. This codes for the MHC molecules

23
Q

What is the histomcompatibility complex called in humans?

A

HLA (human leukocyte antigen)

24
Q

What is the histomcompatibility complex called in mice?

A

H2 complex

25
Q

Each MHC will have more than one major locus. True or False?

A

True
In the example given there were 3, in fact there are more than this. As you have two chromosomes complexity is increased.

26
Q

Why is your complement of MHC unique to you?

A

These gene regions are highly polymorphic

27
Q

Why is it important to type donor tissue in transplant?

A

Otherwise cytotoxic T cells will recognise MHC class I on transplanted organ as foreign and will amount an immune respond against it.

28
Q

Why are differences in our alleles retained in the population?

A

Heterozygosity is an advantage.
Certain alleles are associated with resistance to specific diseases. If we had the same sets a pathogen could and knock out a species.

29
Q

New MHC alleles are generated by …?

A

Interalleic conversion between the same or different genes.

30
Q

B27 gives you a WHAT fold risk of developing Ankylosing spondylitis?

A

90

31
Q

which part of the TCR binds the peptide?

A

CDR3

32
Q

which part of the TCR binds the MHC?

A

CDR1 and CDR2