Recognition of Invaders Flashcards

1
Q

Lymphocytes

A
B cells - act outside the cell
T cells (CD4/CD8) - attack inside the cell
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2
Q

Antibodies (also known as Ig)

A

Cell surface, produced from B cells to bind foreign bodies and mediate effector functions

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3
Q

Structure of antibodies

A

Two Fab arms, which are variable and bind the antigen

Fc region, the constant domain

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4
Q

What are antigens vs antigenic epitopes?

A

Whole molecule antibodies recognise, usually large, >4KDa, can be proteins/carbs/lipids/DNA
Antigenic epitopes - bits that antibodies recognise, smaller regions e.g. spike proteins
Many epitopes on one antigen

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5
Q

Hypervariable region of antibodies?

A

Form the complementary determining region (CDR)

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6
Q

Types of epitopes?

A

Linear - amino acids in sequence recognised

Conformational - amino acids brought close together by protein folding

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7
Q

Affinity of antigen binding?

A

Weak, non-covalent bonds = must be close together for strong interactions
Affinity refers to just one binding site and its antigen, determined by how good the fit is

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8
Q

Avidity of binding?

A

Total strength of binding - increases with number of binding sites used

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9
Q

Cross-reactivity in antibodies?

A

Antibodies bind different epitopes with differing affinities i.e. one well, one less well
Useful in mutated states

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10
Q

Antibody production?

A

Need 10^11 in 5L of blood for specificity
Protective level = 10ng per ml, i.e. 5000kg!
Therefore only produced in large amounts after infection, and then kept in low levels for the rest of the time

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11
Q

Functions of Fc fragment?

A

Effector domain - neutralise, preventing bacterial adherence to epithelium
Opsonisation = phagocytosis
Complement activation
ADCC

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12
Q

What is the humoral immune response? What are the 4 mechanisms?

A
That mediated by antibodies
Neutralisation (block pathogen binding sites, useful for viruses)
Opsonisation (flagging for phagocytosis)
Complement Activation
ADCC (extracellular pathogens)
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13
Q

5 classes of antibodies?

A

IgG, IgM, IgD, IgA1, IgE

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14
Q

IgG?

A

Most abundant, IgG1-4
Diffuses into extravascular sites
Involved in all four functions, mostly neutralisation
IgG3 strongly involved in complement

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15
Q

IgM?

A

First one produced by B cells so found across epithelium, up to 10 binding sites
Used somewhat in neutralisation and opsonisation
Mainly involved in complement

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16
Q

IgD?

A

Rare

Don’t really know what it does

17
Q

IgA?

A

Major Ig in mucosa and serum, subclasses 1 and 2
Mainly in mucosal associated lymphoid tissue (MALT)
Found as dimer in epithelium (when secretory), monomer when diffusing
Most involved in neutralisation

18
Q

IgE?

A

Produced by mast cells so involved heavily in sensitising them
Worm infections/allergy

19
Q

What form do the Igs exist in?

A

IgM and A - polymers, IgM pentameric and IgA dimeric due to cysteine residue in the constant J chain

20
Q

T cell life cycle?

A

Originate in bone marrow (common lymphoid progenitor)
Mature in thymus
Migrate to lymphoid tissues

21
Q

Thymus and aging?

A

Reduces in size with age - 30g newborns, 3g at 80

Therefore t cell populations decline over time

22
Q

Types of t-cell?

A

CD4 - helper cells, Th

CD8 - cytotoxic, Tc/CTL

23
Q

B cell antigen receptors?

A

Antibody structure - Fc regions of light and heavy chain, with CDR and signal transducing molecules (Igs) in membrane for signalling

24
Q

T cell antigen receptors? (TCR)

A

Two chains, alpha and beta, bound by disulphide bonds with carbohydrate groups.
Top variable region, lower constant region
Va and Vb have hypervariable regins with different CDRs for antigen specificity
Also have signal transducing molecules - CD3

25
Q

How do TCRs recognise antigens?

A

Antigen presented from antigen-presenting cells, via MHCs

26
Q

MHCs?

A

MHC -1 : 3 alpha chain regions, a1-3, which binds to membrane
Non-covalently linked to a 2beta chain
1 transmembrane domain
Expressed by all cells

MHC-2 : 2 alpha, 2 beta - both chains have transmembrane domains
Less expressed - e.g. in macrophages, beta cells