Fine Structure of Antibodies Flashcards

1
Q

Which two domains of the Fc portion do not interact and why?

A

The two Ch1 portions of the heavy chain

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2
Q

Which regions of the V region actually interact with the epitope?

A

The hypervariable

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3
Q

What are hyper-variable regions also known as?

A

Complementarity-determining regions

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4
Q

How many CDRs are found per antibody?

A

12

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5
Q

How many framework regions are in each V region?

A

4

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6
Q

What are the two types of L chains?

A

kappa and lambda

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7
Q

True or False. L chains do not need to be identical in an antibody.

A

False, they do need to be identical

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8
Q

Is there effector function associated with the L chain?

A

No

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9
Q

IgG is divided into how many subclasses?

A

4

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10
Q

IgA is divided into how many subclasses?

A

2

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11
Q

What type of bond forms loops within each chain?

A

Intrachain S-S

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12
Q

Which region of the antibody determines function and anatomical location?

A

The Ch region

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13
Q

IgM is predominately present as what?

A

A monomeric membrane-bound BCR on mature B cells

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14
Q

Which isotype is the first secreted when B cells are activated by T cells?

A

IgM

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15
Q

Which isotype is the most predominant in response to T-independent antigens?

A

IgM

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16
Q

What formation is IgM commonly found in?

A

Pentamer

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17
Q

Which isotype is the most efficient in activating the classical complement pathway?

A

IgM

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18
Q

What is the major source of IgM in saliva?

A

Gengival cervicular fluid

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19
Q

Which isotype is the only kind made by the fetus?

A

IgM

20
Q

How many subclasses of IgG are found in humans?

A

4

21
Q

Which region of the antibody helps to distinguish between the classes?

A

The hinge region

22
Q

Which isotype is the most abundant in tissues and serum?

A

IgG

23
Q

Which isotype can cross the placenta?

A

IgG

24
Q

Rank the subclasses of IgG in order of effectiveness of crossing the placenta

A

IgG1 > IgG3 > IgG2 > IgG4

25
Q

Which subclasses of IgG activate the complement pathway?

A

IgG1, IgG2, and IgG3

26
Q

How can IgG be bound?

A

By Fc receptors

27
Q

What is the purpose of binding IgG on various cell types?

A

To increase opsonization

28
Q

Which isotype can participate in ADCC?

A

IgG

29
Q

How many subclasses of IgA are there?

A

2

30
Q

Which subclass of IgA is predominant in serum and in what ratio?

A

IgA1 in a 5:1 ratio

31
Q

What is the ratio of IgA1:IgA2 in mucosal secretions?

A

1:1

32
Q

What is IgA1 predominantly directed against?

A

Protein Isotopes

33
Q

What is IgA2 directed against?

A

Polysaccharide isotopes

34
Q

Which isotype is most abundant of all the isotypes?

A

IgA

35
Q

What is the most abundant isotype in secretions?

A

IgA

36
Q

Where is monomeric IgA found?

A

In serum

37
Q

Where is polymeric IgA found?

A

In secretions as in dimer form (SIgA)

38
Q

How is most IgE found?

A

Bound to Fce receptors on the surface of mast cells, basophils, and easinophils

39
Q

What happens when Fabs of IgE are cross-linked by binding antigen?

A

The cell is activated and releases contents of its granules.

40
Q

When does IgE release contents of its granules?

A

When it’s Fabs are cross-linked in antigen binding

41
Q

What is an example of immediate hypersensitivity reactions mediated by IgE?

A

Type 1 hypersensitivity or allergy

42
Q

How does IgE provide protection from parasites?

A

When repeating epitopes on the parasite cause cross-linking and granules contents from the attached cell to be released onto the parasite killing it

43
Q

Where are most IgE secreting plasma cells found?

A

In the pharyngeal tonsils.

44
Q

Where is IgD mostly found?

A

On the surface of naive mature B cells

45
Q

How does IgD function in B cell activation?

A

As a BCR

46
Q

How does IgD play a role in regulation of B cell surface?

A

If IgD is missing, self-reactive B cells can enter lymphoid organs and proliferate