Immunoglobulins Flashcards
What is another name for antibodies?
Where is it present? Product of which system?
Secreted by?
- immunoglobulins
- present in plasma, tissues, secretions and lymphatics
- product of humoral immune system
- secreted by activated B cells - plasma cells
How many classes of immunoglobulin are there?
What are their names?
Function?
There are 5 classes of immunoglobulin:
- IgG
- IgM
- IgA
- IgD
- IgE
Provide recognition function and trigger effector functions
What region is at the N-terminus of an antibody?
C-terminus?
What are the regions of an antibody?
- Upper:
- Lower:
- Inbetween:
- N-Terminus: variable region
- C-Terminus: constant region
- Upper region: Fab arms
- Lower: Fc region
- Inbetween is a flexible region, part of the heavy chain: hinge
Where do we have disuphide bridges?
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- Hinge - site of inter-heavy chain disulphide bonds
- Between light and heavy chains
What is the dual function of antibodies?
- Recognition function: binding to antigen by Fab arms
- Effector function: clearance mechanisms to get rid of foreign material, occurs through interaction of Fc with effector molecules
What are the two types of light chains in humans?
Can light chains be different in an individual antibody?
What are the two globular domains
- Lambda and kappa chains
- No, both light chains are the same in any individual antibody molecule
- Variable light domain (VL) and Constant light (CL)
Which chain determines the class of antibody?
Why?
The heavy chain determines class of antibody because the light chains are the same in all classes
Name the heavy chain for each type of immunoglobulin:
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How many globular domains do these heavy chains fold up into?
Name them:
- IgG: gamma heavy chain
- IgA: alpha
- IgM: mu
- IgE: epsilon
- IgD: delta
Fold up into 4 or 5 globular domains:
- Variable heavy (VH), constant heavy (CH) 1, CH2, CH3 and (CH4)
Name the key effector molecules:
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- Fc receptors
- Complement
What are CDRs?
Complementarity determining regions are key parts that determine which antigen they are going to bind to.
How many CDRs are their?
What do they create?
There are 6 CDRs, 3 from VH and 3 in VL domains
They create the antigen binding site
Where is the anitgen binding site found?
What is it formed from?
What do they form?
- At the tip of each Fab arm
- Formed from 6 hypervariable regions: 3 in VH and 3 in VL
- A unique 3D structure, site for binding antigen, only allowing the complementary antigen to bind, therefore high specificity and high affinity for binding
IgG
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- most abundant Ig in plasma (10mg/ml)
- Y shaped, 2 heavy chains, 2 light chains
- 4 subclasses: IgG1, IgG2, IgG3, IgG4
- very efficient at triggering complement and phagocytosis via Fc receptors
- only Ig class to cross placenta from mother to foetus - protects baby in first months of life
- predominant antibody of secondary response
IgM
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- Only in plasma and secretions: too large to enter tissues
- 5 Y shaped units held together by J chain and disulphide bridges
- heavy chain has 5 globular domains
- 10 antigen binding sites for antigen - good at clumping viruses together
- very efficient at activating complement
- predominant antibody of primary response
What does agglutinating mean?
- clumping virus particles together