lecture 3 - TCR and MHC Flashcards

1
Q

T celld come out the bone marrow and go to the

A

thymus where the gene segments are rearranged

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2
Q

generation of diversity of TCR

A

multiple V, D and J gene segments
combinational diversity between V, D and J
junction diversity

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3
Q

does somatic hypermutation happen in TCR

A

no

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4
Q

TCR alpha chain formation (similar to Ig light chain):
DNA breaks between V and J

A

random V and J join, then they join to a constant region

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5
Q

TCR beta chain formation (similar to Ig heavy chain):
VD and J regions join and then to a

A

constant region

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6
Q

what chromosome are TCRalpha genes on

A

14

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7
Q

what chromosome are the TCRbeta genes on

A

7

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8
Q

what chromosome is the Ig heavy chain on `

A

14

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9
Q

what chromosome if the Ig light chain on

A

2 for kappa
22 for lamda

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10
Q

TCRgamma and YCRdelta form a slightly different receptor.
so a TCR will either be TCR alpha and beta or

A

TCR gamma and delta

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11
Q

what chromosome is TCR gamma on

A

7

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12
Q

what chromosome is TCR delta on

A

14

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13
Q

differences between MHC and TCR/BRC

A

there no gene rearrangement in MHC molecules
MHC molecules are expressed co-dominantly (MHCs from both chromosomes are expressed)

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14
Q

APC examples

A

B cells, macrophages, dendritic cells

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15
Q

MHC is located on what chromosome

A

6

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16
Q

class I MHC molecules are

A

HLA-A, B and C

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17
Q

class II MHC molecules are

A

HLA-DP, DQ and DR

18
Q

HLA-DR has 2

A

beta chains

19
Q

MHC are the most polymorphic genes known meaning there’s lots of

A

alleles

20
Q

a single cell can have up to how many different MHC molecules

A

12 (if they are heterozygous for all 6 MHC loci)

21
Q

where is most of the polymorphism

A

in the part of the MHC molecule that forms peptide binding groove (alpha 1 and 2)

22
Q

high levels of polymorphism allows

A

binding of vast range of peptides that can be presented to T cells

23
Q

downside with high polymorphism

A

increase risk of many auto immune mediated disease (e.g. presenting self antigens)
also makes donor organs for transplantation very complex

24
Q

how do peptides end up bound to MHC molecules

A

antigen processing and presentation

25
Q

peptides from antigens inside the cell (e.g virus) are usually presented by which MHC

A

class I

26
Q

peptides from exogenous antigens (e.g bacteria) are presented by which MHC

A

class II

27
Q

presentation by MHC class I:
intracellular antigen is broken down into peptides by

A

proteasome

28
Q

peptides transport into endoplasmic reticulum and peptide binds to

A

MHC class I

29
Q

MHC is then presented at cell surface with the

A

peptide

30
Q

what are the peptides transported to ER by

A

TAP transporter

31
Q

what complex holds the MHC in the ER until peptide is bound

A

PLC (peptide loading complex)

32
Q

presentation by class II:
takes up antigen into a

A

endocytic vesicle

33
Q

peptides are produced and what fuses with the endocytic vesicle

A

vesicle containing MHC class II

34
Q

peptides bind to MHC class II and MHC is

A

presented at the surface

35
Q

what does the invariant chain do

A

forms a complex with MHC class II

36
Q

what does this complex do

A

blocks the binding of peptides when class II is being made

37
Q

when is the invariant chain is the cleaved

A

when it fuses to the endosome as its acidic

38
Q

what does this cleavage leave bound to the MHC class II

A

CLIP (a short peptide fragment)

39
Q

what binds to the MHC class II releasing CLIP

A

HLA-DM allowing peptides to bind and the MHC goes to the cell surface

40
Q

in normal healthy cells MHC I and II will present peptides from self proteins to show what it looks like when its healthy so can see changes if its infected

A
41
Q

HLA-DM and TAP are coded for within the

A

MHC