Recognition of Extra Cellular Pathogens Flashcards

(26 cards)

1
Q

Discuss pattern recogntion receptors’ distribution

A

The body has probably around 100, and different cells (e.g. macrophages) can express multiple different PRRs to act on foreign substances

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2
Q

Antigen

A

Component of an infectious agent for which the body contains a lymphocyte which can recognise it

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3
Q

Epitope

A

Part of an antigen molecule to which an antibody attaches itself

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4
Q

Surface immunoglobulins vs secreted

A

B Lymphocytes have many surface immunoglobulins which are all identical; bound to the membrane via a transmembrane region. Once they specialise into plasma cells, these new cells focus on secreting immunoglobulins but have the same exact structure

Only difference is attachment via transmembrane region

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5
Q

Describe clonal selection

A

It is a competitive process

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6
Q

Describe polypeptide chain distribution in immunoglobulins

A

2 identical Light Chains, 2 identical Heavy Chains

Each immunoglobulins has identical antigen binding sites since each has a heavy and light chain

Those thick black lines are disulfide bonds (e.g. between the two heavy chains, base of a domain or between heavy and light chain)

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7
Q

VH and VL

A

Variable domains (heavy and light); region that allows variation between antigen combining sites and different antibodies

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8
Q

Hypervariable region

A

As the name suggests, the parts of the variable regions that have the most amino acid variation between different antbodies

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9
Q

CH and CL

A

Constant regions between different immunoglobulins

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10
Q

Hinge Region

A

Region halfway down the heavy chain that has some flexibility which means that the two arms can move relative to each other

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11
Q

Fab Region and Fc Region (of immunoglobulins)

A

Fab - region above hinge region that contains light chain, Vh and CH1 of heavy chain

Fc - region below hinge region that contains CH2 and CH3

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12
Q

What are Immunoglobulin classes/subclasses/isotypes and how do they vary from each other

A

IgM; IgG (1, 2, 3, 4); IgA (1, 2); IgE; IgD

They vary from their constant regions so have different genes that code for each other

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13
Q

Genes that encode different types of light chains

A

Kappa κ or Lamda λ (B cells can use different genes to make its light chain

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14
Q

What gene are B cells programmed to use to form the constant regions of their surface antibodies

A

The mu gene to make IgM class for heavy chain

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15
Q

Class switching of immunoglobulins

A

When activated, the B cell changes the genes it expresses to form the constant domains of the newly synthesised heavy chains of new antibodies (e.g. going from mu to epsilon gene [IgM → IgE])

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16
Q

Compare the different immunoglobulin isotypes

A

IgE has 4 constant domains in the heavy chain

IgM always exists as a pentamer connected by a Joining chain with all antibodies having identical binding sites; can bind up to 10 epitopes

17
Q

Which Ig Subtypes are concerned with complement activation (C1q binding)

18
Q

Which Ig Subtypes are concerned with Phagocyte Binding (via Fc)

19
Q

Which Ig Subtypes are concerned with Mast Cell Binding

20
Q

Which Ig Subtypes are concerned with Natural Killer Cell Binding

21
Q

Where can IgM pentamers be found

22
Q

Where can IgG monomers be found

A

Blood, Tissues, placental transfer - much of foetal immunity comes from this maternal IgG

23
Q

Where can IgA monomers be found

A

Blood/Tissues

24
Q

Where can IgA dimers be found

A

Mucosal secretion, Milk - can give protection to newborns

25
Where can IgE monomers be found
Tissues (bound to mast cells)
26
Where can IgD be found
Mucosa of upper aerodigestive tract (mouth, nose, throat)