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BIOSCI 107 Part Two > Blood and Immune: Adaptive immunity, antibodies and your immune repertoire > Flashcards

Blood and Immune: Adaptive immunity, antibodies and your immune repertoire Flashcards

1
Q

What is adaptive immunity?

A

Your immunity that has memory. The secondary response is stronger and more rapid than the primary response

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2
Q

Does affinity of B cells towards antigens increase over time and with persistence?

A

yes

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3
Q

What is persistence of an antigen

A

antigen is taken up in specialized tissue, lymph nodes, and make germinal centres and lymphoid follicles . They produce lots of progeny that have similar but developing antibody molecules

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4
Q

When is your immune repertoire developed?

A

before birth (develop as many combinations of antigen binding molecules as possible)(10^11 different antigen binding molecules)

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5
Q

What is on each B and T lymphocyte

A

Each lymphocyte represents a different antigen specificity randomly produced by rearrangement of the genes coding for the antigen receptors.

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6
Q

are the receptors the same on all B cells

A

no, each carry an individual receptor that is different from every other B cell

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7
Q

What is a transposases

A

DNA cutting and repair enzyme

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8
Q

What causes high number of antigen specificities

A

Gene rearrangement/recombination is
important for the production of the
vast number of antigen specificities

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9
Q

What gene regions use the same mechanism of rearrangment as transposons

A

Immunoglobulin (Ig) and T cell Receptor (TcR)

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10
Q

Transposase’s in the genome

A

RAG1 and RAG2 (Recombination Activation Genes)

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11
Q

Where are recognition sequences (RS) found

A

are located at the ends of all the Ig and TcR gene segments

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12
Q

What is transposase able to do

A

moved away from the receptor gene enabling it to operate in trans i.e. it can rearrange other genes without affecting its own position in the genome

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13
Q

What are recognition sequences (RS)

A

These are base pair sequences found at the ends of any gene segments that rearranges – RS are the substrate for RAG1 and RAG2 directed recombination

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14
Q

Are RS palindromic

A

yes, read in the same direction, 3’ to 5’ or 5’ to 3’

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15
Q

What type of formation do RS form

A

hairpin formation

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16
Q

What species contain RS and RAG 1 and 2

A

The Recognition Sequences and RAG1 and RAG2 are identical in all species that possess adaptive immunity

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17
Q

What is the Ig fold

A

most basic component of a immunoglobulin protein

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18
Q

Where are antibodies formed from?

A

repeated Ig domains. Ig domains are found in hundreds of different proteins.

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19
Q

What is Ig protein domain fold called

A

β-barrel

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20
Q

How many amino acids in a β-barrel

A

~110 amino acids

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21
Q

How is a Ig fold structured

A

Two antiparallel β-pleated sheets joined in the middle by a disulphide bond

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22
Q

What can the loops at the end of strands in an Ig fold do

A

not constrained so they can vary their amino acid sequences without affecting the stability of the fold

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23
Q

How many loop regions are in a Ig fold

A

3

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24
Q

Where is the antigen binding site

A

the 3 loop regions

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25
Q

How many protein chains are in an antibody

A

4

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26
Q

What makes up each chain in an antibody

A

repeating Ig domains

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27
Q

How many domains are in the light chain in an antibody

A

2

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28
Q

How many domains are in the heavy chain in an antibody

A

4-5

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29
Q

Size of IgG

A

150kD

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30
Q

How is a heavy and light chain linked together

A

through a disulphide bond

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31
Q

How are heavy chains bonded together

A

disulphide bonds

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32
Q

Are all antibodies immunoglobins

A

yes

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33
Q

What are at the top of the two “arms” on an antibody

A

antigen binding sites

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34
Q

What forms the antigen-binding sites

A

N terminal domains of the L and H chains

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35
Q

can the effector region of an antibody change

A

no (invariant)

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36
Q

What binds the effector region of an antibody

A

Fc receptors and complement component C1

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37
Q

why are both the antigen-binding sites identical

A

because they came from the same B lymphocyre

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38
Q

What domain carries the antigen-binding site

A

FaB

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39
Q

Number of residues in the light chain

A

212

40
Q

Number of residues in the heavy chain

A

450

41
Q

What is the default Ig produced by naive B cells

A

IgM

42
Q

Types of IgM

A

It can be membrane bound (monomer) or soluble (pentamer)

43
Q

What is the name of the membrane bound form of IgM

A

B-cell antigen receptor (BCR)

44
Q

How many binding sites does the soluble form of IgM have

A

10

45
Q

What causes IgM to react strongly to surfaces such as microbes

A

avidity binding

46
Q

What binds 5 IgG molecules together

A

J chain

47
Q

Affinity and avidity in IgM

A

low affinity and high avidity

48
Q

Relationship between IgM and B lymphocytes

A

It is a membrane bound receptor on the surface of B cells. As soon as B cell recognises antigen it triggers to produce IgM

49
Q

What is affinity

A

When the sum of the attractive forces is greater than the sum of the repulsive forces
fewer molecules

50
Q

What does a higher affinity mean

A

Higher affinity means that it takes fewer molecules per unit volume to associate and dissociate slowly.

51
Q

What is the antibody binding constant

A

no. of antibody and antigen to give 50% bound as a complex

52
Q

What is the dissociation constant

A

is how long the complex to dissociate away before you move away from reactants/equilibrium

53
Q

What happens when an antibody and antigen come together

A

(affinity) there is a molecular interaction in the surface which is governed by both repulsive and attractive forces. They come together and stay together for a certain period of time

54
Q

types of attractive forces between antigen and antibody

A

electrostatic, sharing electron clouds, hydrophobic, van der waals

55
Q

What is avidity

A

Multiple affinity contacts, strength of binding is much greater than the strength of the individual affinities

56
Q

What two factors govern avidity

A

the concentration required to get antigen and antibody to come together and also how long it takes the antigen and antibody complex to dissociate away from equilibrium

57
Q

how many classes of Ig are there

A

5

58
Q

What determines the function of different Ig molecules

A

the genes in its heavy chain

59
Q

After being activated, what type of Ig does a B cell switch too (due to different heavy chain gene)

A

IgG

60
Q

Properties of IgG

A

activates complement, can be transferred through the placenta

61
Q

Properties of IgM

A

Activates complement, has a membrane-bound form

62
Q

Properties of IgA

A

Secreted at mucosal surfaces

63
Q

Properties of IgD

A

Has a membrane-bound form

64
Q

Properties of IgE

A

Has a high affinity receptor on mast cells

65
Q

Which types of Ig molecules bind with avidity

A

IgM and IgG bind with avidity, exposing Fc region allowing them to bind well with complement

66
Q

Where is IgA found

A

in secretory sites like tears, saliva and breast milk - babies need IgA from mother which is long lasting in gut (gives them strong gut immunity)

67
Q

Which two types of Ig are membrane-bound

A

IgM and IgD

68
Q

What is complementarity

A

a measure of how well to molecules interact with each other

69
Q

When is complementarity formed between an antigen and an antibody

A

if the sum of the attractive forces exceeds of the sum of the repulsive forces

70
Q

When does affinity increase?

A

when the sum of the attractive forces exceeds the sum of repulsive molecular forces

71
Q

Why are there so many different antibody molecules in the body from a limited amount of genes

A

somatic hypermutation

72
Q

What are Complementarity Determining Regions (CDR)

A

3 regions/loops (that connect the strands in the 1st domains of the Heavy and Light chains ) where amino acids sequences are different between each antibody molecule

73
Q

Area of the antigen-binding site

A

800-1000 square Angstroms

74
Q

How many identical antigen-binding sites are there

A

2

75
Q

Names of clusters that germlines are separated into

A

Variable, diversity, joining, constant

76
Q

What segment does a light chain NOT contain

A

D (diversity) segment

77
Q

What is responsible for rearrangement in B and T lymphocytes

A

RAG1 and RAG2 (Recombination activation gene)

78
Q

Most variable region in Ig molecules

A

CDR3

79
Q

What is the order of rearrangement in heavy chains

A

D to J, V to D

80
Q

Why is joining imprecise in the recombination of the Ig locus

A

so that base pairs are changed during repair. This leads to huge variation at the VDJ join ( results in massive amino acid diversity in the CDR3 loop on the antigen receptor)

81
Q

Number of variable (V) segments in H-chains

A

100

82
Q

Number of diversity (D) segments in H-chains

A

27

83
Q

Number of joining (J) segments in H-chains

A

6

84
Q

Number of variable (V) segments in L-chains

A

35

85
Q

Number of joining (J) segments in L-chains

A

5

86
Q

What is clonal selection

A

The process by which an antigen selectively binds to and activates only those lymphocytes bearing receptors specific for the antigen. The selected lymphocytes proliferate and differentiate into a clone of effector cells and a clone of memory cells specific for the stimulating antigen.

87
Q

What happens if a B cell encounters the antigen it has an affinity for

A

it produces plasma cells which produce highly affinity soluble IgG

88
Q

Where are B cells found

A

B cells are in lymph nodes throughout the body

89
Q

What is within the lymphoid follicle

A

germinal centres where B cell that has encountered pathogen is undergoing somatic hypermutation - generating B cell progeny which will become high affinity cells

90
Q

What does stochastically mean

A

occurring randomly

91
Q

When is the massive repertoire of naïve B cells generated stochastically

A

before birth each with a unique B cell Receptor

92
Q

What does somatic hypermutation result in

A

B cell clones with higher antigen receptor affinity

93
Q

What is a plasma cell

A

A fully differentiated B cell that produces a single type of antibody.

94
Q

What allows vaccinations to work

A

affinity maturation

95
Q

The function of memory cells

A

they reside in lymphoid tissue ready to respond rapidly to re-challenge.

BIOSCI 107 Part Two (17 decks)

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