Lecture 6 Flashcards

(45 cards)

1
Q

Where do T cells develop and mature?

A
  • develop in the bone marrow
  • mature in the thymus
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2
Q

Where do B cells develop and mature?

A

develop AND mature in the bone marrow

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3
Q

What is an antigen?

A
  • a macromolecule (protein, polysaccharide, glycoproteins)
  • recognized by the body as foreign
  • stimulates an immune response
  • can be foreign or self
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4
Q

What is an epitope?

A

region or site of antigen that are recognized by the immune system (they bind to Igs or TCRs)

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5
Q

What are B cell receptors also known as?

A

Immunoglobulins (antibodies)

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6
Q

What is the membrane-bound form of the B-cell receptor called and what is it bound to?

A

BCR; bound on the B-cell surface

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7
Q

What is the secreted form of B-cell receptors called? Where do they bind pathogens?

A

antibody; in the extracellular spaces

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8
Q

What is the structure of an antibody?

A
  • Y-shaped
  • Two hinged heavy chains
  • Two light chains
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9
Q

What joins the chains in an antibody together?

A

disulphide bonds

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10
Q

What is avidity?

A

The total strength of the interaction between an antibody and an antigen

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11
Q

What is affinity?

A

The strength of the interaction between a single antigen-binding site and antigen

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12
Q

What are the two types of immunoglobulin domains in an antibody?

A

variable and constant

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13
Q

What do the variable regions of immunoglobulins determine?

A

antigen-binding specificity

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14
Q

What do the constant immunoglobulin domains of an antibody determine?

A

the different Ig classes: ie: IgM, IgG, IgD, IgA, IgE

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15
Q

What is the hinge region of an antibody?

A
  • lies within the C region
  • allows flexibility in binding multiple antigens
  • differs between isotypes
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16
Q

What are distinct characteristics in the C region?

A
  1. number and location of disulphide bonds
  2. number of attached carb groups
  3. number of C domains
  4. length of hinge regions
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17
Q

How many subclasses of IgG exist? List them in decreasing order

A

IgG1, IgG2, IgG3, IgG4

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18
Q

How many subclasses of IgA exist?

A

2; IgA1, IgA2

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19
Q

What is the most abundant Ig in serum?

20
Q

What is the first Ig produced after B-cell activation?

21
Q

In what form is IgM secreted and where?

A

pentamer; normally in bloodstream but not in tissues

22
Q

Which Igs activate the classical pathway of complement?

A

most IgGs and IgM; IgA, IgG and IgD do not activate complement

23
Q

Which Ig is the heaviest?

24
Q

Where and how does IgA act?

A

at mucosal surfaces; secreted into gut and respiratory tract and breast milk

25
What does IgE do?
acts in parasite immunity and allergic reactions; high-affinity binding to mast cells and basophils
26
What does IgD do?
has an unknown role; present on the surface of mature B cells as a marker
27
What Ig participates in placental transfer?
IgG
28
How do the IgM and IgA molecules form polymers?
by interacting with the J chain
29
How many antigen-binding sites do IgM molecules in plasma have
10
30
IgA is found as ____ in mucous secretion but as ____ in plasma
dimers; monomers
31
____ are regions within the variable regions of H and L chains
hypervariable regions
32
Do the hypervariable regions of antibodies directly or indirectly make contact with the antigen?
- directly - actually contact the antigen - makeup the antigen-binding site - also called complementarity-determining regions
33
How many hypervariable regions are there? What are their names?
3; HV1, HV2, HV3
34
Where is the most variable part of the domain?
HV3
35
What are the regions between hypervariable regions called? How many are there?
framework regions; 4 (FR1-FR4)
36
The immune system generates antibodies of different specificities. How does it do this?
- by creating various combinations of H-chain and L-chain V regions - process known as combinatorial diversity - formation of VH and VL region genes from smaller DNA segments
37
When does combinatorial diversity occur?
during development of B cells in the bone marrow
38
What is the general structure / characteristics of a T-cell Receptor?
- Transmembrane proteins with an almost entirely extracellular structure - two protein chains (a and B) - each chain has C and V region - V region of a and B chains make the antigen-binding site - Each T cell expresses one type of TCR which can offer protection against only one pathogen
39
Most TCRs can only recognize ____
small peptides
40
Peptides must be presented via cell-surface receptors called ____ to T cells
MHC / HLA family
41
How do the structures of MHC class I and MHC class II differ?
**MHC class I **: - three alpha subunits and a beta macroglobulin - alpha 1 and 2 form the peptide-binding groove - alpha 3 is the only subunit that anchors MHC to the plasma membrane **MHC class II** - two alpha and two beta subunits - alpha 1 and beta 1 form the peptide-binding groove - alpha 2 and beta 2 anchor MHC to the plasma membrane
42
the MHC presenting the antigen binds to both the ____ and the ____
TCR and a co-receptor expressed on the T-cell surface
43
What are the two co-receptors of T cells? What MHC do they bind to and do they target extracellular or intracellular pathogens?
1. CD4: binds MHC-II, targets EXTRACELLULAR pathogens 2. CD8: binds to MHC-I, targets INTRACELLULAR pathogens
44
TCR is not expressed without ____ because:
CD3; it is required to bring TCR to surface
45
What does the CD3 complex do?
Recruits the signaling molecules that are activated upon TCR engagment which drives T cell activation