Antibodies Flashcards

1
Q

What are the two regions of an antibody?

A

Constant region and variable region

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2
Q

What are the two fragments of an antibody?

A
Fab fragments (bind to antigens)
Fc Fragments (constant region)
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3
Q

How many chains are there in an antibody? Describe them:

A

4:
2 Heavy chains (middle)
2 Light chains (outer)
Each is the same

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4
Q

What holds together the chains in antibodies?

A

Disulphide bridges

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5
Q

What allows for flexible binding of antibodies to antigens?

A

Hinge region

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6
Q

Which parts of an antibody are constant?

A

Constant region to allow membrane integration

Lower half of variable region

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7
Q

How does an antibody bind to an antigen?

A
They have many attractions to each other:
H bonds
Ionic
VDW
Hydrophobic
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8
Q

What is antibody affinity?

A

Strength of total non-covalent attractions between single antibody binding site and antigen epitope.

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9
Q

What is antibody avidity?

A

The overall strength of binding between multiple antibody binding sites (e.g. in a multimer) and multiple antigen epitopes

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10
Q

What is antibody cross-reactivity?

A

When an antibody elicited in response to one antigen can recognise a similar antigen
E.g. Smallpox and cowpox

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11
Q

What are immunoglobulins?

A

A class of soluble glycoproteins, which antibodies are a part of.

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12
Q

Name the classes of Immunoglobulins in order of abundance:

A
IgG
IgA
IgM
IgD
IgE
(GAMDE)
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13
Q

Which classes of immunoglobulins have subclasses?

A

IgG and IgA

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14
Q

How are immunoglobulin classes named?

A

Based on their Heavy chain (thank fuck!)

E.g. IgG = gamma

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15
Q

Describe what each __mer each Immunoglobulin is

e.g. dimer

A

IgG: Monomer
IgA: Monomer in blood, dimer in secretions
IgM: Pentamer

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16
Q

What does IgG do?

A

Major activator of classical complement pathway.

Moves across placenta to give passive immunity

17
Q

What does IgA do?

A

Major secretory goblin to protect mucosal surfaces

18
Q

Descrive the dimerisation of IgA

A

Binds to basolateral surface of epithelial cells (onto Poly-Ig receptor), allowing endocytosis to vesicle where receptor is cleaved, yet part remains that forms a dimer secretory IgA with a longer half life to neutralise pathogens in lumen upon release

19
Q

What does IgM do?

A

Agglutination
Activates complement
Multiple binding sites to compensate for low affinity

20
Q

Where is IgM found?

A

80% in blood

21
Q

What is IgD?

A

Basically barely there…

Involved in B cell development and activation

22
Q

What does IgE do?

A

Produced to fight parasites

Active in allergic reaction

23
Q

How does an allergen cause a reaction?

A

IgE binds to mast cell.
Allergen binds to 2 antibodies on mast cell
Cross link triggers mast cell activation.
Causes degranulation and histamine release