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MIMM 214 > B Cells 3 > Flashcards

B Cells 3 Flashcards

1
Q

what is the shape of an antibody?

A

Y

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2
Q

what type of molecule are antibodies?

A

glycoproteins

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3
Q

what is immunoglobulin?

A

protein family that antibodies and BCRs are part of

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4
Q

describe the structure of antibody in terms of chains

A
  • 2 identical disulfide-linked heavy chains
  • 2 identical light chains
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5
Q

describe the structure of antibody in terms of regions

A

VARIABLE regions –> heavy and light chains both have a variable region for antibody binding (V_L, V_H)

CONSTANT regions –> heavy and light chains both have a constant region (C_L, C_H)

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6
Q

what is the function of the variable region?

A

Ag binding

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7
Q

how many variable regions are there in an antibody?

A

2 identical variable regions –> therefore 2 identical binding sites

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8
Q

what does Ag binding lead to?

A

neutralization

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9
Q

what is the function of the constant region?

A

involved in complement activation

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10
Q

what is the constant region called?

A

Fc

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11
Q

what does the constant region do? and 2 functions

A

Fc binds Fc receptors on phagocytes and other cell types to lead to intracellular signaling

  1. C1q binds to activate complement
  2. help mast cells get rid of helminth
  3. opsonization for phagocyte
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12
Q

what are the 2 fragments of antibody?

A
  1. Fab fragments
  2. Fc fragments
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13
Q

how many Fab fragments per antibody?

A

2

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14
Q

what does Fab stand for?

A

Fragment antigen binding

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15
Q

what parts of the antibody are in Fab fragments?

A

has the antigen-binding domain (variable region) and part of the constant H and L chains

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16
Q

how many Fc fragments are there?

A

1

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17
Q

what does Fc stand for?

A

Fragment crystallizable

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18
Q

what parts of the antibody are in the Fc fragment?

A

constant regions of the heavy chain

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19
Q

which fragment is recognized by receptors that bind antibodies?

A

Fc fragment

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20
Q

what type of bond holds antibody together?

A

disulfide covalent bonds

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21
Q

what type of 3D structures are antibodies folded into?

A

Beta sheets

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22
Q

what does CDR stand for?

A

Complementarity Determining Region

23
Q

what is CDR?

A

Antibody-antigen binding site –> direct contact with Ag

24
Q

what is the structure of CDR?

A

3 hypervariable loops per variable domain and are not part of the B strands

25
Q

which part of antibodies have the greatest variability in the antibody sequence? why?

A

complementarity determining region to allow binding to diff antigens

26
Q

where is CDR located on the antibody?

A

at the extremities of the antibody –> i.e. extremities are responsible for antibody:antigen binding

27
Q

what type of binding occurs between the Ig and epitope? and 4 examples

A

NON-COVALENT BINDING

  1. H bonds
  2. van der Waals
  3. Hydrophobic
  4. Ionic
28
Q

what is a way to describe specificity of the antibody:antigen binding?

A

lock and key

29
Q

what are 2 types of variability that affect antibody:antigen binding?

A
  1. variability in size of epitope
  2. variability in antibody –> CDR varies in length
30
Q

where are epitopes located on an antigen?

A

epitopes can be anywhere on an antigen –> antigen has many epitopes

31
Q

what are the 5 classes of antibody?

A
  1. IgM
  2. IgD
  3. IgG
  4. IgE
  5. IgA
32
Q

what is the main difference btwn classes of antibody?

A

different # of Ig-like domains in the constant region of the heavy chain based on diff AA sequence

33
Q

is IgM a monomer?

A

no, it is a pentamer

34
Q

describe the structure of IgM pentamer

A

5 IgM antibodies linked together via disulfide bonds

35
Q

describe the heavy chain of IgM

A

1 variable region, 4 constant regions

36
Q

describe how IgM is expressed on mature B cells vs plasma cells

A

mature B cells express transmembrane IgM (monomer) prior to activation

then B cell becomes plasma cell and forms pentamer

37
Q

IgM is part of which wave of secreted antibodies?

A

IgM is part of the first wave

38
Q

describe the heavy chain of IgD

A

1 variable region, 3 constant regions

39
Q

IgD is part of which wave of secreted antibodies?

A

IgD is part of the first wave

40
Q

describe the heavy chain of IgG

A

1 variable region, 3 constant regions

41
Q

IgG is the most abundant in ______

A

IgG is the most abundant in plasma fluid

42
Q

how many IgG subclasses are there? what is the difference btwn them

A

4 –> each with slightly diff functions

43
Q

when is IgG produced?

A

after differentiation in the germinal center –> not 1st wave

44
Q

describe the heavy chain of IgE

A

1 variable region, 4 constant regions

45
Q

when is IgE produced?

A

to help Th2 get rid of Helminth infections

46
Q

describe the heavy chain of IgA

A

1 variable region, 3 constant regions

47
Q

describe the structure of IgA in plasma

A

monomer

48
Q

describe the structure of IgA in mucous secretions in GIT and respiratory system

A

dimer

49
Q

how does IgA become a dimer?

A

linking via J chain

50
Q

IgA is important for which type of immunity?

A

mucosal immunity

51
Q

how many subclasses of IgA are there?

A

2

52
Q

why can antibodies be used as a drug? and an example?

A

antibodies can bind to any epitope –> ex. antibody against TNFalpha for rheumatoid arthritis

53
Q

how are antibodies used in research?

A

ELISA assay or WB where an antibody conjugated with fluorescence can bind the Fc region of another antibody

54
Q

why can an antibody therapy cause an immune response?

A

if the antibody is less similar to humans, your immune system can mount an immune response against it

MIMM 214 (33 decks)

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