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

20
Q

IgA: what is the heavy chain

21
Q

what is the 2nd most abundant Ig

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
IgM: what is the heavy chain
u
26
IgM: binding sites
multiple (10 Fab regions as large pentameric molecule joined by J chain), so compensate for low affinity
27
IgM: location
blood as large
28
IgM: function
multiple binding sites so efficient as agglutination and activating complement
29
IgE: what is the heavy chain
E
30
IgE: when is it produced
present at very low concentrations in response to parasitic infections and in allergic diseases
31
IgE: what does it bind to
high affinity Fc receptors of mast cells and basophils
32
IgE: what does cross-linking by antigen trigger
mast cell activation and histamine release
33
IgD: what is the heavy chain
d
34
IgD: concentration
very low concentration as serum (not much soluble IgD)
35
IgD: when is surface IgD expressed
early in B cell development
36
IgD: what is it involved with
B cell development and activation
37
comparison of Ig structures
diagram
38
which Ig are present in blood
IgG, IgM
39
which Ig is present in EC fluid
IgG
40
which Ig is present in secretions
dimeric IgA
41
which maternal Ig is present in foetus via placenta
IgG
42
which Ig is present with mast cells below epithelia
IgE
43
5 consequences of antibody-antigen binding
neutralisation, agglutination, opsonisation, complement activation, bound by cells expressing Fc receptors (especially innate immunity such as phagocytes and NK cells)