Immunoglobulin structure Flashcards

(45 cards)

1
Q

IgG

A

Predominant antibody in the secondary immune response

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2
Q

IgA

A

Predominant antibody in external secretions

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3
Q

IgM

A

Predominant antibody in primary response

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4
Q

IgD

A

Found mainly on the surface of B cells

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5
Q

IgE

A

Involvement in allergic hypersensitivities

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6
Q

Common core structure of all antibodies

A

Two identical light chains and two identical heavy chains, where each light chain is attached to a heavy chain and the heavy chains are attached to each other

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7
Q

Immunoglobulin domain

A

Where all the chains, each of about 110 amino acids in length, all fold independently

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8
Q

Isotypes of light chain

A

Either kappa or lambda

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9
Q

N-terminal region of the heavy and light chains

A

Variable regions; the rest of them are all constant regions

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10
Q

Variable region

A

Combination of the heavy chain variable and light chain variable regions make up the antigen binding region

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11
Q

Constant region

A

Carries out other effector functions of the antibody (crossing the placenta, sites for attachment of Fc receptor, complement binding)

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12
Q

CDRs

A

Complementarity determining regions - three sites on the variable region above all else determine what will bind

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13
Q

How are the CDRs exposed?

A

When they fold, the portions of the CDR in the amino acid sequence stick out as projecting loops

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14
Q

How is IgM secreted?

A

In its pentameric form, with a molecular weight of 900,000 daltons

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15
Q

What joins the subunits of IgM?

A

The J chain

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16
Q

IgM is the primary antibody for antigen administered __

A

parenterally.

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17
Q

IgM is also the primary antibody elicited by __

A

T-independent antigen

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18
Q

How is IgM expressed on B cells?

A

As a monomer

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19
Q

Can IgM cross the placenta?

20
Q

Approximate serum concentration of IgM

21
Q

IgG is the antibody most characteristic for ___

A

secondary response

22
Q

What is the difference in structure between IgG’s secreted and membrane form?

A

Nothing significant; both monomeric, both ~150,000 daltons

23
Q

How does IgG recruit complement fixation?

A

Varies based on subclass

24
Q

Can IgG cross the placenta?

A

Yes, due to presence of FcRn

25
Approximate serum concentration of IgG
1200 mg/dL
26
Typical form of IgD
Membrane form
27
Function of IgD
B cell antigen receptor along with IgM
28
Serum concentration of IgD
3 mg/dL
29
To what types of cells does IgE bind?
Mast cells and basophils due to Fc receptor
30
How is IgE secreted?
As a CHO-rich monomer of 190,000 daltons
31
Serum concentration of IgE
30 mcg/mL
32
How does predominant IgA occur?
As a dimer
33
How are the subunits of IgA joined?
By the J chain
34
How does serum IgA occur?
As a monomer (function is unclear)
35
Can IgA cross the placenta?
No
36
How does it fix complement?
Through alternative pathway
37
Serum concentration of IgA
300 mg/dL
38
IgA plays a crucial role in __
mucosal immunity
39
How do antibodies contribute to the immune response?
By binding to and neutralizing pathogens, as well as signalling for destruction by other cells
40
Fc-receptor mediated killing
If antibodies don't neutralize the pathogen, the Fcs on the antibodies will signal to FcRs on macrophages, eosinophils, NK cells, basophils, and mast cells, and they'll kill it
41
Neonatal antibody production
IgG: maternal IgG for the first few months, then reaches adult levels at age 4 IgM: adult levels reached at age 10 months IgA: adult levels reach at 10 years old
42
Clinical use of immunoglobulins: polyclonal and monoclonal antibodies
Polyclonal is found in immunized individuals. Monoclonal can be used in vitro to keep passive antibodies
43
Examples of polyclonal antibody uses
IVIG treatment for inflammatory diseases
44
Examples of monoclonal antibody therapy
Tumor-specific antibodies to treat cancer
45
Immunoglobulin classes are distinguished based on __
the constant region of the heavy chain.