Lecture 3 Flashcards

1
Q

How are T cell receptors encoded?

A

By rearranging genes

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2
Q

What regions of the T cell receptors are encoded?

A

Variable regions are encoded by V,D,J segments

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3
Q

Where do b cells develop?

A

In the bone marrow

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4
Q

Where to T cells go once they have left the bone marrow?

A

Thymus

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5
Q

When do T cells rearrange?

A

When in the thymus, don’t turn on until they are in the thymus

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6
Q

When do B cells rearrange?

A

When in the Bone marrow

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7
Q

What are some similar mechanisms that are seen in in TCR that are also in BCR?

A

Multiple V,D and J gene segments, combinatorial diversity and junctional diversity

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8
Q

Unlike a BCR what is never done in a TCR?

A

It is never secreted it is always found on the surface of the cell

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9
Q

What else is not found in the T cell?

A

Hyper mutation

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10
Q

What happens randomly in T cells?

A

An individual T cell will breaks its DNA randomly during the alpha D and V region

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11
Q

What to alpha and beta chains do?

A

Pair up to combine together to make a unique T cell receptor in the cell

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12
Q

What is T cell alpha chain similar to?

A

Light chain

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13
Q

What is the T cell beta chain similar to?

A

Heavy chain

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14
Q

Why do T cells not have hyper mutation?

A

Because the don’t contain AID (activation induced cytidine deaminase

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15
Q

On the beta chain what binds first?

A

D and J chain then they combine with a v chain

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16
Q

Where does splicing occur on a T cell?

A

Constant region

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17
Q

Where do TCR recognise antigens?

A

In grooves of MHC molecules

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18
Q

Where is the single alpha chain located?

A

On chromosome 14

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19
Q

What will T cells generate?

A

Either alpha beta cell receptors or gamma delta cell receptors

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20
Q

What are the gene segments found in a TCRbeta?

A

V,D,J,C

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21
Q

What are the gene segments found on TCRalpha?

A

V,J,C

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22
Q

Where is HLA found?

A

On chromosome 6

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23
Q

How are MHC expressed?

A

Co-dominantly

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24
Q

What do class I MHC molecules express?

A

All nucleated cells

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25
What do class II MHC molecules express?
Expressed on only particular cell types
26
What are the specific types of cells that MHC class II molecules express?
B cells, macrophages, dendritic cells
27
What are MHC molecules induced by?
Interferons (inflammation)
28
How many MHC molecules will a single gene contain?
12 MHC molecules
29
What is the gene structure of class I MHC molecules?
HLA-A, HLA-B, HLA-C
30
What is the gene structure for class II MHC molecules?
HLA-DP, HLA-DQ, HLA-DR
31
What do class II molecules contain?
Maternal and paternal expression
32
If there is one heterozygous gene at each loci how many class I molecules can be expressed?
6 different class I molecules
33
What is the co-dominant expression of MHC molecules?
Polymorphism and polygeny
34
Where do polymorphism occur?
In clusters
35
Where does the variability of MHC molecules occur?
Occur where the MHC forms the peptide binding groove
36
What are regions for such high levels of MHC polymorphism?
Binding of a vast range of peptides that be presented to T cells
37
What is the downside of high levels of MHC polymorphism?
Increased immune-mediated disease e.g. increases the likelihood of presenting self antigens (could state an immune response on yourself)
38
Where are antigens from?
Either from inside the cell or from a pathogen that has hijacked a cell
39
Endogenous?
Inside the cell - will end up on the source of the cells by class I
40
Exogenous?
Outside the cell - bacteria that float around outside cells get taken up by the cells - MHC class II
41
What do macrophages do?
They eat antigens and display them on its surface
42
How do peptides end up on the surface of the cells bound to MHC molecules?
The are PROCESSED into small peptide fragments suitable for binding to and presentation by MHC I and II
43
What does the proteasome do to antigens?
Degrade and chop up the antigens in the cytoplasm
44
Where are class I molecules found?
In the ER
45
What does the proteasome allow the fragments in the ER to do?
Bind to peptide binding grooves which allows class I molecules to go out of the ER into the cell surface
46
Where is the viral protein synthesised in class I?
In the cytoplasm
47
How are the peptides transported in class I?
By the TAP transporter - to ER
48
What happens once the peptides bind to the class I molecules?
Transported to the cell surface
49
What can the proteasome change?
Can change its behaviour depending on what happens outside the cell
50
What is TAP TRANSPOTER?
A component of multi protein assembly
51
What does the TAP component contain?
Contains tapasin and calreticulin
52
Where is the bacteria (antigen) found in the MHC II molecule?
Endocytosed into intracellular vesicles inside the cell
53
How is the protein cleaved to peptides in MHC II?
By acid proteases in vesicles
54
Where is class II targeted?
Targeted in the endocydic pathway
55
Why aren’t class II molecules loaded into the ER?
Because the invariant chains stops this from happening
56
What does the invariant chain do?
Binds to the class II peptide binding groove blocking the peptides from getting into the ER
57
What happens to the lysosomal enzymes in the endocydic pathways (MHC class II)
They get degraded leaving the CLIP peptide associated with the binding groove
58
What can displace the CLIP?
Peptides from the antigen
59
What is HLA-DM required for?
Loading peptides into the groove
60
What happens in normal healthy uninfected cells?
MHC I and II will bind and present peptides from self proteins
61
What are LMPs?
They are molecules part of the proteasome - change change the features of the proteasome
62
What can class I molecules be killed by?
CD8+ (cytotoxic cells)
63
What are MHC II cells also known as?
APC (antigen presenting cells)
64
What are some example of antigen presenting cells?
Macrophages, dendritic cells and B cells
65
What cells can express MHC class II cells?
CD4 T helper cells