Antibody interaction with antigen Flashcards

(45 cards)

1
Q

What does the Ab recognise?

A

Conformational antigens composed of several sequentially discontinuous segments brought together by folding of the molecule

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2
Q

What is the epitope?

A

The part of the antigen which is recognized by the antibody

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3
Q

What is the paratope?

A

The complimentary part of the antibody

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4
Q

What is each V region made of?

A

3 hypervariable regions

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5
Q

What are complimentary determining regions?

A

6 hypervariable regions of light and heavy chains

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6
Q

Describe the hypervariable region

A

CDR loops interact with antigen
Poke out of the beta sheets of Ig domain

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7
Q

How does the binding happen?

A

Neither the antibody nor the antigen is changed by binding
One antibody binding site binds to one epitope on the antigen
The binding is non-covalent and is reversible

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8
Q

What bonds are involved in the binding?

A

Non-covalent interaction due to Ionic bonds
H-bonds
Hydrophobic bonds
Van der Waals forces
Lots of small forces add up to a strong interaction.
All critically dependent on the distance apart

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9
Q

What forces are present in antibody-antigen binding?

A

Electrostatic
Hydrogen bonds
Hydrophobic bonds
Van der Waals

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10
Q

What is the strength of interaction?

A

Each force acts over short distance that can be measured (affinity)

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11
Q

What is meant by avidity?

A

Avidity = total binding strength
Different from affinity (binding strength at a single binding site)
Avidity functionally more important than affinity

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12
Q

What else is required for antibody production?

A

Additional signals from the B cell once BCR is ligated and IgAlpha and IgBeta signal is sent

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13
Q

How do T cells contribute to Ab production?

A

Cytokine production

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14
Q

What does neutralisation of viruses depend on?

A

type of virus, target cell and class of Ab

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15
Q

What is the importance of antibodies in neutralisation?

A

May be important in limiting viral infectivity - bind to a virus to block infection
Vaccine efficacy often assessed by measuring circulating, neutralising Abs

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16
Q

Why is neutralisation important?

A

May inhibit virus-cell interaction
Prevent endocytosis of virus
Prevent uncoating inside endosome

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17
Q

What makes neutralisation more effective?

A

Complement

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18
Q

How are toxins neutralised?

A

Abs bind bacterial exotoxins: neutralise their effect by preventing attachment to cellular receptors (e.g. binding of cholera toxin to ganglioside GM1)

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19
Q

What antibodies are important in neutralisation?

20
Q

What receptor mediates toxin clearance?

21
Q

What is opsonisation?

A

The coating (binding) of particles by either Ab,
complement or APP (eg CRP)
Ab bind microorganisms via the Fab and to cells
by the Fc

22
Q

What does opsonisation do?

A

Increases the efficiency of the
phagocytic process, allowing the organism to be
cleared more effectively

23
Q

What is complement?

A

The complement system is a collection of circulating membrane-associated proteins
Important in defence against microbes

24
Q

What are the pathways of complement?

A

Classical and alternate pathways

25
What are the functions of complement?
Chemotaxis Opsonisation Lysis of target cells Priming of adaptive immune response
26
How do antibodies interact with cells?
Via Fc receptors
27
What do Fc receptors associate with?
G-chain
28
How does activation of Fc receptors occur?
Due to aggregation of receptors and signalling via Immunoreceptor Tyrosine- based Activation or Inhibition Motifs
29
What does Fc receptor activation cause?
ADCC (antibody-dependent cellular cytotoxicity) Phagocytosis Apoptosis Mediator release Can enhance antigen presentation
30
What does CD64 bind?
Monomeric IgG1 and IgG3 with high affinity and IgG4 with low affinity No binding to IgG2
31
Where is CD64 expressed?
On mononuclear phagocytes
32
What is CD64 involved in?
Phagocytosis of immune complexes and mediator release
33
What is the structure of CD64?
3 extracellular Ig domains Associated with gamma chain ITAM
34
Describe CD32
2 types = FcgRIIa and FcgRIIb
35
Describe FcgRIIa
Wide cellular distribution Moderate affinity for monomeric IgG1 and IgG3. High affinity for complexed IgG Has ITAM
36
Describe FcgRIIb
Same specificity for Ig but has ITIM
37
How is the antibody response inhibited?
Secreted antibody forms complex with antigen Antigen-antibody complex binds to B cell Ig and Fc receptor Block in B cell receptor signalling due to ITIM -ve signal Inhibition of B cell response
38
Describe CD16
Has FcgRIIIa and FcgRIIIb
39
Describe FcgRIIIa
Transmembrane molecule with moderate affinity for monomeric IgG Associated with g-, b-, z- h- chains of the CD3 complex as ITAMs Expressed on monocytes, macrophages, NK cells and some T cells ADCC
40
Describe FcgRIIIb
GPI (glycophosphatidilelinositol) linked with low affinity for monomeric IgG Expressed on neutrophils and basophils Activates by lipid raft formation and associates
41
Describe CD89
Associated with g-chain Expressed on myeloid cells Can trigger phagocytosis, cell lysis and the release of inflammatory mediators Binds both IgA1 and IgA2
42
Describe Fc-epsilon-RI
Very high affinity receptor for IgE Associates with g-chains and b-chain (abg2 receptor unit) Expressed on mast cells and basophils. Receptors always saturated (low serum IgE) X-linking of these Ab molecules bound to FceRI leads to mediator release e.g histamine
43
Describe CD23
Low affinity receptor for IgE Expressed on leukocytes and lymphocytes. Not a member of the Ig-Superfamily, similar to C-type lectins (eg mannose binding lectin)
44
Where is CD23a expressed?
B cells and involved in IgE production
45
Where is CD23b expressed?
Many cell types and induced by IL-4