Ig Structure Flashcards

1
Q

List the classes of Ig and their conc. in serum

A

IgM, IgG, IgE, IgA, IgD

IgG (12mg/ml) > IgA (2.5mg/ml) > IgM (1.5mg/ml) > IgD (.03mg/ml) > IgE (5x10(-5)mg/ml)

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2
Q

Describe the major biological characteristics of IgM

A

Predominant Ab induced in primary response (elicited by T-independent polysaccharide)

pentameric in secreted form, appears as a monomer on B cells (part of B cell receptor (BCR)) - IF A CELL HAS IG ON THE SURFACE, PARTICULARLY IGM, IT IS A B CELL

J chain joins subunits

Activates complement

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3
Q

Describe the major biological characteristics of IgG

A

Predominant Ab induced in secondary response (T dependent)

Three classes, IgG1, IgG2, IgG3, IgG4, with slightly different characteristics, monomeric in membrane bound and secreted form

All are good at neutralization and are particularly good at diffusion into extravascular sites

1 and 3 are especially good at opsonization, sensitization for killing by NK cells, crossing the placenta, and activating compement

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4
Q

Describe the major biological characteristics of IgE

A

Involvement in allergic hypersensitivities

Sensitization of Mast Cells (IgE fixes to mast cells and basophils via an Fc receptor on the cells)

secreted as a monomer, low serum concentrations

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5
Q

Describe the major biological characteristics of IgA

A

Two subclasses, IgA1, IgA2

Predominant Ab in external secretions, occurs as a dimer joined by a J chain (it appears in serum as a monomer)

can fix complement via alternative pathways (non-classical)

key role in mucosal immunity

Transport across epithelium (dimer), neutralization, diffusion into extravascular sites (monomer)

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6
Q

Describe the major biological characteristics of IgD

A

Found predominantly on some B cells (membrane bound, generally not found in blood)

Functions as a B cell Ag receptor along with IgM

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7
Q

Describe three mechanisms by which Ab protects the host from microorganisms

A

Neutralization: Ab prevents bacterial adherence

Opsonization: Ab promotes phagocytosis

Activation of complement: Ab activates complement, which enhances opsonization and lyses some bacteria

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8
Q

What is a polyclonal Ab?

A

Ab from multiple clones of B cells are polyclonal

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9
Q

What is a monoclonal Ab?

A

Ab from a clone of B cells are monoclonal

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10
Q

What is the difference between monoclonal and polyclonal Ab?

A

Individual B cells make Ab against a single epitope. If that B cell proliferates and produces Ab, it will all be against that one epitope on the Ag - monoclonal. If multiple B cells encounter the same Ag, they will all produce Ab against various epitopes on the Ag - polyclonal. They are all specific for the Ag, but for different Epitopes.

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11
Q

What are some examples of monoclonal and polyclonal Ab used clinically?

A

polyclonal - IVIG against many different diseases

monoclonal - tumor-specific monoclonal Ab

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12
Q

State the approximate half-life of antibody titers after tetanus vaccination and after infection-caused measles

A

Tetanus (ppl immunized for tetanus): 11yrs even though recommendation is 5-10 yrs

Measles (people who got measles): 3014yrs

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13
Q

What part of the heavy an light chains are considered the variable domain? The constant domain?

A

For both, the N terminus is considered the variable domains. The remainder is considered the constant domain

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14
Q

What are some functions of the Constant domain?

A

ability to cross placenta

sites of attachment for Fc receptors of macrophages, monocytes, and mast cells

binding of complement

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15
Q

What is the function of the variable domain, and why are complementarity-determining regions (CDR) important?

A

The variable domain is the site of antigen binding, and is responsible for the specificity of Ag binding. Each heavy and light chain has three CDRs, which are sites of greatest AA variability. The 6 CDRs (3 from heavy, 3 from light) are projecting loops that are in close proximity, and form the Ag binding groove.

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16
Q

How are Ig classes defined?

A

by the C(onstant) regions of the heavy chain

17
Q

How do Ab facilitate uptake of pathogen?

A

via uptake by macrophages either through binding of Fc region or activation of complement receptors

18
Q

How does Ab aggregation lead to phagocytosis

A

Free Ig do not stimulate the cross linking of Fc receptors. However, aggregation of Ig on bacterial surfaces allows cross linking of Fc receptors which stimulates phagocytosis

19
Q

What makes an Ab binding site?

A

The V region of the heavy chain and the V region of the light chain –> where the Ag specificity lies

20
Q

How are the chains held together?

A

disulfide bonds

21
Q

If you proteolytically cleave an Ab, what do you get?

A

Fab region (Ab binding (and part of constant)) and Fc region (lower part of constant)

22
Q

How large is an epitope?

A

6-8 AA long

23
Q

How many binding sites do you have on secreted IgM?

A

10 total

24
Q

What is the total protein concentration in the blood?

A

100 mg/ml

25
Q

How much albumin is in blood?

A

50 mg/ml

26
Q

What percent of serum protein is IgG?

A

about 10%

27
Q

If someone has been infected very recently, what Ig would you find? (what is the first one that is made during an immune response?)

A

IgM

28
Q

If someone had been infected a while ago, what Ig would you find? (what is the second Ig produced during an immune response?)

A

IgG

29
Q

As a baby ages, what is the order that Ab is produced?

A

Maternal IgG (drops at birth, gone by few months after birth), IgM builds at birth, IgG builds a few months after birth, IgA builds slowly over years

30
Q

How do you get IVIG?

A

take the serum from 10,000 people, pool it all together, which gives you a huge population of polyclonal Ab, which can treat immune deficiency and inflammatory diseases

31
Q

how can you tell if a drug uses monoclonal antibody?

A

any drug that ends in -mab means it is a monoclonal antibody