Lecture 29 Flashcards

1
Q

Structure of Antibody

A
  • Y shaped glycoprotein
  • A part of Immunoglobulin family
  • 2 identical disulfide linked heavy chains and 2 identical light chains
  • 4 chains total
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2
Q

Where are Variable regions

A

At tip/top of Y
Both heavy and light chain have a variable region
Light chain–>VL
Heavy chain–> VH

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3
Q

Where is constant region

A

Base and cross of Y
Both heavy and light chains have a constant region
Light chain–>CL
Heavy chain–>CH

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4
Q

Function of Variable region

A

Antigen Binding
VL and VH forms antigen-binding sites (2 identical sites per antibody, one at each tip of Y)
Binding can result in neutralization

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5
Q

Function of Constant regions

A

Involved in complement activation
Constant region (Fc) can bind to Fc receptors on phagocytes and other cell types (mast cells and eosinophils)

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6
Q

Fab fragment contents

A

2 Fab fragments per antibody
Each fragment has an antigen-binding domain AND part of CH and CL chains
Each Fork of Y
Fab= fragment antigen binding

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7
Q

Fc fragment contents

A

1 Fc fragment
Constant region of heavy chain
Receptors that bind antibodies recognize the Fc region
Base of Y
Fc= fragment crystallizable

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8
Q

Immunoglobulin contents

A

2 Heavy chains (each with variable and constant regions)
2 Light chains (each with variable and constant regions)

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9
Q

How are heavy and light chains held together

A

By intra/interchain disulfide covalent bonds
Both constant and variable regions are folded in complex 3D structures including beta strands

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10
Q

Where is the Complementarity determining region (CDR)

A

In Variable region of light chain at extremities (very tip of fork)

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11
Q

CDR contents

A

6 Hypervariable loops (3 loops per variable domain)
Not part of the beta strands

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12
Q

Function of CDR

A

Allows for antigen specificity
Has direct contact with antigen (being part of the antigen binding site)
Greatest variability in antibody sequence

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13
Q

Types of bonds for antigen binding

A

Involves non-covalent bonding between the immunoglobulin and antigen epitope
Ex. Hydrogen bonds, Van der Waals, Hydrophobic, Ionic bonds

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14
Q

Saying for antigen binding specificity

A

Lock and key specificity
- involves extremities of antibody (CDR)
Location of epitopes can be anywhere on the antigen

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15
Q

5 Major classes of antibody

A

IgG, IgA, IgM, IgE, IgD

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16
Q

How are antibody classes different

A

1)Different number of Ig-like domains
2) Different length of constant region in heavy chains (different amino acid sequence)
3) Different functions during immune response

17
Q

Overall structure of IgM

A

1) Pentameric (5 antibodies linked together via disulphide bonds)
2) Heavy chain has 4 constant regions and 1 variable region

18
Q

When are IgM expressed

A

Mature B cells prior to activation (transmembrane expression)

19
Q

Which immunoglobulins are part of the first wave of secreted antibodies

A

IgM, IgD

20
Q

What is immunoglobulin the most effective initiator of the complement cascade

A

IgM

21
Q

IgD structure

A

Heavy chain has 3 constant regions and 1 variable region

22
Q

IgG structure

A

Heavy chain has 3 constant regions and 1 variable region
4 subclasses in humans IgG (1-4)

23
Q

Which immunoglobulin is most abundant in plasma

A

IgG

24
Q

When are IgG produced

A

Following differentiation in the Germinal Center

25
Q

IgE structure

A

Heavy chain has 4 constant regions and 1 variable region

26
Q

When are IgE produced

A

In response to Helminth infections
IgE role in TH2 response

27
Q

Structure of IgA

A

Heavy chains has 3 constant regions and 1 variable region
In plasma–>monomer
In mucous secretions through the J chain–>dimer
2 subclasses: IgA1 and IgA2

28
Q

Which immunoglobulin is important for mucosal immunity

A

IgA

29
Q

Treatment for rheumatoid arthritis

A

Antibody against TNF-alpha (pro-inflammatory cytokine)

30
Q

Clinical use of antibodies

A

1) Antibodies made to bind virtually any epitope
2) Antibody made to bind to another antibody