Week 3 Antibodies

Front 1

• Explain the roles of antibodies in immunity
[LO]

Back 1

1. Binding - binding and identifying Ag and foreign substances
2. recruitment and activation of effector molecules to eliminate antibody bathed material

Front 2

Name each of the antibody classes and their role in immunity [LO]

Back 2

Front 3

Draw a diagram of each of the antibody classes and be able to
identify:
• The heavy and light chains
• Domains
• Hinge region
• Presence of J chain

[LO]

Back 3

[LO]

Front 4

Know the relative concentrations of the Ig classes in serum and secretions [LO]

Back 4

[LO]

Front 5

Explain how antibodies attach to antigens and Fc receptors [LO]

Back 5

[LO]
IgG antibodies are Y-shaped protein structures made up of different regions. The two arms of the Y are known as Fab regions, where Fab stands for fragment, antigen-binding. Fc is the tail region, with Fc standing for fraction, crystallizable. Fab regions attach to antigens while the Fc region binds to Fc receptors on the surface of a cell.

Front 6

What role do antibodies and Fc receptors play in immunity? [LO]

Back 6

Binding of antibody via Fc receptors activates other cells to
up- or down-regulate immune response

Front 7

What is the approximate weight of an Ab?

Back 7

150kDa

Front 8

What are the two different kinds of polypeptide chain that create an Ab?

Back 8

heavy and light chains

Front 9

What bond unites the heavy chains?

Back 9

disulfide bonds

Front 10

What are the light chains bonded to?

Back 10

identicle L chains are linked to the H chain by the disulfide bond

Front 11

What are the 5 classes of antibody determined by the constant region of the heavy chain?

Back 11

Front 12

What are the two types of light chain?

Back 12

Front 13

Draw and identify the antigen binding site on an igG

Back 13

Front 14

Locate the disufide bonds on your diagram of an IgG

Back 14

Front 15

What is the Fab site?

Back 15

Antigen binding site

Front 16

What is an Fc site?

Back 16

effector functions - complement triggering, cell receptor binding

Front 17

Describe light chain configuration

Back 17

Front 18

Describe heavy chain configurations

Back 18

Front 19

Describe AbAg binding in the Fab section

Back 19

16 aa contact 16aa in Ag

Front 20

Describe the hinge function and morphology

Back 20

Front 21

Describe the domain functions of CL

Back 21

Front 22

Describe the domain fn of CH1

Back 22

Front 23

Describe the domain function of CH2

Back 23

Front 24

Describe the domain function of Ch3

Back 24

Front 25

Describe hypervariable regions

Back 25

Front 26

What are the amino acid positions of hypervariable regions?

Back 26

Front 27

What are CDRs

Back 27

Complementarity determining regions

Front 28

How long is the light chain in IgG?

Back 28

212

Front 29

How long is the heavy chain in IgG?

Back 29

450

Front 30

describe how one can attain pepsin and other fragments

Back 30

Front 31

What is the valency of IgG?

Back 31

divalent -> 2

Front 32

How many subclasses exist for IgG?

Back 32

1,2,3,4

Front 33

Describe the Fc region of an IgG

Back 33

Front 34

What can IgG4 do that other IgG subclasses cannot

Back 34

Front 35

Describe IgM

Back 35

Front 36

Which Ig is a pentameter?

Back 36

Front 37

Describe IgM heavy chains

Back 37

Front 38

dEscribe location and bonding of J chain

Back 38

Front 39

Describe formational capabilities of IgM molecule

Back 39

Front 40

Which Ig can bind complement

Back 40

Front 41

What is the main Ab of primary immune response?

Back 41

Front 42

Describe IgA molecule with diagram

Back 42

Front 43

What are the relative concentrations of each of the Ig classes in serum?

Back 43