Antibodies - Diebel Flashcards

(34 cards)

1
Q

Basic structure of an antibody

A
  • Fab region (basic unit) = 2 heavy chains and 2 light chains
  • Fc region = 2 heavy chains
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2
Q

H chain

A

5 kinds: gamma, alpha, mu, epsilon, delta

-defines the class of antibody to which the molecule belongs

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3
Q

L chain

A

2 varieties: kappa or lambda

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4
Q

What chain changes in class switching?

A

Heavy chain!

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5
Q

Secreted IgA structure?

A

Dimer of the basic unit (2 H’s and 2 L chains)

Basic units held together by J chain

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6
Q

IgM structure?

A

Pentamer

Basic units held together by J chain

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7
Q

Constant Region

A

Made up of 1 to 4 compact, structurally-similar domains call C domains

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8
Q

Variable Domains

A

Different in sequence between antibodies of different specificities.

-At N-terminal

Hyper variable regions make it more different

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9
Q

Valence=

A

of antigenic determinates (epitopes) an antibody molecule can theoretically bind.

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10
Q

Valence of IgG

A

2 (1 antibody with 2 Fab parts)

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11
Q

Valence of secreted IgA

A

4

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12
Q

Valence of IgM

A

10 in theory but 5 in practice b/c of puckering

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13
Q

Valence of Fab?

A

1

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14
Q

Valence of F(ab’)2:

A

2

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15
Q

Valence of isolated VL or VH?

A

0 –takes a combo of VL and VH to make antibody binding sites

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16
Q

Isotypes:

A
  • Constant domains change but variable domains stay the same
  • slight differences in the AA sequence of their H chain C regions
17
Q

10 isotypes

A
IgG 1-4
IgA 1-2
IgM 1-2
IgD
IgE
18
Q

Allotypes

A
  • minor ALLELIC differences in sequence of Igs between individuals
  • depends on if you are using your mom or dad’s genes to produce chain

Ex: two IgG1 molecules that are the same but the AA sequence is slightly different

19
Q

Idiotypes

A

=unique combining region, made up of the CDR (complementarity- determining regions) amino acids of its L and H chains

  • Antigen determinate part of Ab
  • *Antibody’s unique combining site considered as an antigen.
20
Q

CDR (complementarity-determining regions)

A

AA sequence variablity is not distributed uniformly along V domain

  • These 3 areas are called CDR or hypervariable regions
  • CDR comprise the actual antigen-binding site
21
Q

Anti-idiotype

A

Antibodies made that recognize the unique sequence of that combining site and no other.

22
Q

IgG (1000 mg/dL)

A
  • main antibody in blood and fluids
  • Neutralizes toxins and blood-borne viruses,
  • activates complement to destroy bacteria

-main antibody! - memory

23
Q

IgA (200 mg/dL)

A

Does same as IgG in blood

  • Real work is SECRETIONS
  • Forms a DIMER and secretory components protects it from proteolysis
24
Q

IgM (100 mg/dL)

A
  • same as IgG
  • FIRST antibody to appear in serum after immuniztion
  • very efficient at activating complement
25
IgD (5 mg/dL)
role uncertain - functions mainly as receptor on naive B cells - always surface bound
26
IgE (0.02 mg/dL)
Causes Type 1 immunopathology (immediate hypersensitivity) - ALLERGIES - BUT true importance is in resistance to WORMS/PARASITES
27
2 things initiated after antibody binds an antigen?
IgG or IgM binds to antigen and conformational change happens so 2 things are initiated: 1. Binding to phagocytic cells - have receptors FcR for the altered Fc of IgG 2. C1q (1st part of the complement system) now binds to 2 adjacent Fcs and is ACTIVATED
28
IgG activation of Complement
Secreted as a monomer but forms a HEXAMER to activate complement
29
IgG1 structure
Disulfide bonds hold chains together | 3 constant heavy domains
30
IgG3 structure
Monomer | -larger hinge region so it is better at binding complement than IgG1
31
IgM structure
Secreted form: - 5 antibodies linked by J chain = PENTAMER - 4 constant heavy domains
32
IgA structure
Dimer (linked by J chain) | Secretory component that helps it go through epithelial cell layers
33
IgD structure
ONLY membrane bound - only on naive B cells - monomer
34
IgE structure
- 4 constant heavy domains | - always secreted as a monomer