Lecture 1 Flashcards

1
Q

What is specific/adaptive immunity induced by?

A

Exposure to a particular infection

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2
Q

What are some features of specific immunity?

A

Mediated by lymphocytes (B/Tcells)

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3
Q

How can self reactive lymphocytes be removed?

A

By clonal deletion

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4
Q

What forms a clone of effector cells?

A

Proliferation and differentiation of activated specific lymphocytes

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5
Q

Why are BCR expressed by?

A

B cells

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6
Q

What does the membrane bound form of Ig binds?

A

Free antigen

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7
Q

When is the antigen secreted?

A

When the B cell is activated

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8
Q

What allows for the activation of complement?

A

Opsonisation and classical pathway activation and MAC

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9
Q

What are antibodies formed by?

A

4 polypeptides

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10
Q

What is the structure for antibodies?

A

Variables V regions (heavy and light) and constant C regions

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11
Q

What do the two V regions form?

A

Antigen binding site

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12
Q

What do the C regions do?

A

Antibody effector function - FC region

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13
Q

What type of structure are antibodies?

A

Bivalent structure

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14
Q

What are the 2 identical heavy and light chains held together by?

A

Covalent and non covalent bonds

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15
Q

What does the FC region bind on the constant region?

A

Macrophages, NK cells and neutrophils

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16
Q

What are the 5 different classes of antibodies?

A

IgA, M, D, G, E

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17
Q

What is another word for antibody?

A

Isotype

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18
Q

What are antibodies determined by?

A

The heavy chain in the C region

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19
Q

What termini’s do C domains occupy?

20
Q

What C termini’s do V domains occupy?

21
Q

What domains are part of the immunoglobulin superfamily?

A

TCR, MHC class I and II

22
Q

How many hypervariable regions are there?

A

2 in the V heavy and V light

23
Q

How many HV loops?

24
Q

How many complementary-determining regions are there (CDR)?

25
What affects antibody binding?
Size and shape
26
What does a linear epitope mean ?
It s continuous
27
Non-linear?
Discontinuous
28
How are epitopes recognised?
By antibodies
29
What do antibodies and antigens form?
Non-covalent interactions
30
When might an antigen sequence be manipulated?
In a vaccine design
31
What do CDRs determine?
The specificity and affinity of an antibody for an antigen
32
What do TCR bind instead of antigens?
Peptides
33
What do TCR recognise?
Short peptide fragments bound to MHC molecules on other cells
34
What is the structure of TCRs?
They are made up of alpha and beta chains which form a heterodimer
35
What do the V domains of TCR interact with?
Peptide bound to MHC molecules
36
When were MHC molecules first identified?
In transplant rejection
37
Where are MHC I molecules expressed?
In nearly all cell types in the body
38
Where are MHC class II molecules expressed?
Restricted to specialised groups
39
Where are MHC class I molecules expressed?
On all nucleated cells
40
What are the 3 different MHC class I molecules?
HLA-A, HLA-B, HLA-C
41
What is the MW of the alpha chain in an MHC class I molecule ?
43kD
42
What is the MW of the beta-1 microglobulin chain on the MHC CLASS I molecule?
12kD
43
What do the alpha and beta domains fold to make on an MHC class I molecule?
Beta sheet - peptide binding site (groove, cleft)
44
What is the DNA encoding alpha 1 and 2 on MHC class I moelcules like?
Polymorphic
45
What is the alpha 2 chain and Beta2 domain like on MHC I MOLECULES?
Fold into Ig-like domains
46
What are the three types of MHC class II molecules?
HLA-DQ, HLA-DP, HLA-DR
47
What are the alphabeta chain domains expressed on in MHC CLASS II?
APC