lecture 1 - antibodies, T cell receptors and MHC molecules Flashcards

(48 cards)

1
Q

what are the organisms that causes disease

A

pathogens

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2
Q

examples of pathogens

A

bacteria
viruses
fungi
worms
protozoa

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3
Q

specific/adaptive response exhibits

A

memory

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4
Q

what features allow specific immune response to have memory

A
  • clonally distributed receptors
  • large repertoire (cells have lots of different receptors)
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5
Q

what is the lag phase

A

time from infection until you get your response

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6
Q

lag phase in secondary response

A

much shorter and the number of antibodies is much higher

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7
Q

when a specific lymphocyte binds to a foreign antigen that lymphocyte activate and is

A

clonally expanded

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8
Q

lymphocytes are

A

t cells and b cells

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9
Q

BCR (b cell receptor) is expressed by B lymphocyte and binds to

A

free antigens

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10
Q

when the B cell is activated the BCR is released from the cell now known as an

A

antibody

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11
Q

TCR is not dimeric, what two chains does it have

A

an alpha and beta chain

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12
Q

the TCR only binds to antigens are being displayed to it by

A

MHC molecules

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13
Q

TCR is always on the T cell and never

A

secreted

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14
Q

MHCs are expressed by

A

APC (antigen presenting cells)

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15
Q

how do antibodies interact with the complement system

A

via the constant heavy chain regions

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16
Q

complement system can cause destruction of what very quickly

A

pathogens

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17
Q

how do antibodies activate effector cells

A

the Fc region of the antibody can be recognised by activator cells via the FcR (Fc receptor)

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18
Q

antibody structure:
what chains to antibodies have

A

2 light and 2 heavy chain

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19
Q

the variable domains of the two chains form the

A

antigen binding site

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20
Q

which domain does the FcR bind to

A

the constant region

21
Q

what are the 5 antibody classes/isotypes

A

IgM, D, A, G and E

22
Q

what region determines the class

A

heavy chain constant regions

23
Q

light chains has 2 domains, how many can heavy chain have

24
Q

each domain is how many amino acids

25
how are the domains held together
by disulphide bridge
26
in variable regions we have pieces that are hypervariable in each variable region how many hypervariable regions are there
3 (HV1-3)
27
HV regions are the bits that are interacting with the
antigen
28
what part of the antigen will the antibody recognise
the epitope
29
a linear/continuous epitope
the parts that are bound are next to each other in primary structure
30
non linear epitope
parts arent close together in the primary structure but are when folded into 3D structure
31
antibody and antigen form what type of interactions
non covalent
32
what does TCR recognise on the MHC
peptide fragment of an antigen
33
how many domains does a TCR have
4
34
how many CDRs (complementary determining regions) are there in TCR
3
35
what does MHC stand for
major histocompatibility complex
36
MHC class I molecules are expressed in
nearly all cells types in the body
37
class I is how many chains
1
38
what are the subunits of the MHC class I
α1,2 and 3, β2 microglobulin
39
MHC class II has how many chains
2, alpha and beta chain
40
what are the domains in MHC class II
β1 and 2, α1 and 2
41
MHCs are every polymorphic which means there are many
alleles of MHC molecules
42
what are the 3 MHC class I molecules
HLA-A, HLA-B and HLA-C
43
what are the 3 MHC class II molecules
HLA-DP, HLA-DQ and HLA-DR
44
what cells are MHC class II molecules expressed in
APCs
45
the groove on MHC class II is more ____ that the groove on MHC class I
open meaning it can bind a different array of proteins
46
CD8 t cells binds to which MHC class
class I MHC by CD8 binding to the alpha1/alpha2 domain
47
what does this binding do
stabilises TCR/MHC interaction
48
CD4 t cells bind to which MHC class
class II by CD4 binding to the alpha2/beta2 domains