Lecture 1 Flashcards

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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?

A

Carboxyl

20
Q

What C termini’s do V domains occupy?

A

Amino

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?

A

6

24
Q

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

A

CDR1-3

25
Q

What affects antibody binding?

A

Size and shape

26
Q

What does a linear epitope mean ?

A

It s continuous

27
Q

Non-linear?

A

Discontinuous

28
Q

How are epitopes recognised?

A

By antibodies

29
Q

What do antibodies and antigens form?

A

Non-covalent interactions

30
Q

When might an antigen sequence be manipulated?

A

In a vaccine design

31
Q

What do CDRs determine?

A

The specificity and affinity of an antibody for an antigen

32
Q

What do TCR bind instead of antigens?

A

Peptides

33
Q

What do TCR recognise?

A

Short peptide fragments bound to MHC molecules on other cells

34
Q

What is the structure of TCRs?

A

They are made up of alpha and beta chains which form a heterodimer

35
Q

What do the V domains of TCR interact with?

A

Peptide bound to MHC molecules

36
Q

When were MHC molecules first identified?

A

In transplant rejection

37
Q

Where are MHC I molecules expressed?

A

In nearly all cell types in the body

38
Q

Where are MHC class II molecules expressed?

A

Restricted to specialised groups

39
Q

Where are MHC class I molecules expressed?

A

On all nucleated cells

40
Q

What are the 3 different MHC class I molecules?

A

HLA-A, HLA-B, HLA-C

41
Q

What is the MW of the alpha chain in an MHC class I molecule ?

A

43kD

42
Q

What is the MW of the beta-1 microglobulin chain on the MHC CLASS I molecule?

A

12kD

43
Q

What do the alpha and beta domains fold to make on an MHC class I molecule?

A

Beta sheet - peptide binding site (groove, cleft)

44
Q

What is the DNA encoding alpha 1 and 2 on MHC class I moelcules like?

A

Polymorphic

45
Q

What is the alpha 2 chain and Beta2 domain like on MHC I MOLECULES?

A

Fold into Ig-like domains

46
Q

What are the three types of MHC class II molecules?

A

HLA-DQ, HLA-DP, HLA-DR

47
Q

What are the alphabeta chain domains expressed on in MHC CLASS II?

A

APC