antibodies and B lymphocytes Flashcards

antigen binding: explain how antibodies bind to antigen, and the consequences of such antigen binding

1
Q

how many hypervariable regions in the Fab

A

3

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2
Q

what are complementarity determining regions (hypervariable regions)

A

loops of amino acis which bind to epitope of antigen, lining up at end of V domains

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3
Q

what is the structure of the constant region

A

barrel-shaped B-pleated sheets with internal disulphide bridges

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4
Q

why is a large number of interactions between antibody and epitope important

A

forces are non-covalent so are weak

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5
Q

define antibody affinity

A

strength of total non-covalent interactions between a single Fab and single epitope on antigen

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6
Q

define antibody avidity

A

overall strength of multiple interactions between an antibody with multiple binding sites and a complex antigen with multiple epitopes

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7
Q

antibody avidity vs affinity

A

avidity is a better measure of binding capacity

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8
Q

define antibody cross-reactivity

A

antibodies elicit in response to one antigen can sometimes recognise a different antigen of similar structure (e.g. smallpox and cowpox, ABO blood group antigens)

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9
Q

what are the 5 classes of antibodies (Ig)

A

G, A, M, E, D

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10
Q

which 2 classes of antibodies have subclasses, and what does this mean

A

IgG, IgA; subtly differeny functions and body locations

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11
Q

what is different and the same in the 5 classes of antibodies

A

different heavy chains and CH domains, same light chains (K, λ)

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12
Q

what is the most abundant Ig

A

IgG

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13
Q

IgG: what is the heavy chain

A

y

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14
Q

IgG: how many monomer subclasses

A

4

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15
Q

IgG: where is variability mainly located

A

hinge region, effector function domains

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16
Q

which Ig is actively transported across the placenta

A

IgG

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17
Q

IgG: where is it located

A

blood, EC fluids

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18
Q

IgG: what subsets are the major activators of classical complement pathway

A

IgG1, IgG3

19
Q

what is the major secretory Ig

A

IgA

20
Q

IgA: what is the heavy chain

A

a

21
Q

what is the 2nd most abundant Ig

A

IgA

22
Q

IgA: where does it occur as monomers, and dimers

A

monomer: blood; dimer: secretions

23
Q

IgA: function

A

protects mucosal surfaces from bacteria, viruses, protozoa

24
Q

what is the first Ig synthesised after exposure to anigen

A

IgM (acts in primary antigen response)

25
Q

IgM: what is the heavy chain

A

u

26
Q

IgM: binding sites

A

multiple (10 Fab regions as large pentameric molecule joined by J chain), so compensate for low affinity

27
Q

IgM: location

A

blood as large

28
Q

IgM: function

A

multiple binding sites so efficient as agglutination and activating complement

29
Q

IgE: what is the heavy chain

A

E

30
Q

IgE: when is it produced

A

present at very low concentrations in response to parasitic infections and in allergic diseases

31
Q

IgE: what does it bind to

A

high affinity Fc receptors of mast cells and basophils

32
Q

IgE: what does cross-linking by antigen trigger

A

mast cell activation and histamine release

33
Q

IgD: what is the heavy chain

A

d

34
Q

IgD: concentration

A

very low concentration as serum (not much soluble IgD)

35
Q

IgD: when is surface IgD expressed

A

early in B cell development

36
Q

IgD: what is it involved with

A

B cell development and activation

37
Q

comparison of Ig structures

A

diagram

38
Q

which Ig are present in blood

A

IgG, IgM

39
Q

which Ig is present in EC fluid

A

IgG

40
Q

which Ig is present in secretions

A

dimeric IgA

41
Q

which maternal Ig is present in foetus via placenta

A

IgG

42
Q

which Ig is present with mast cells below epithelia

A

IgE

43
Q

5 consequences of antibody-antigen binding

A

neutralisation, agglutination, opsonisation, complement activation, bound by cells expressing Fc receptors (especially innate immunity such as phagocytes and NK cells)