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Immunology > Part 4 > Flashcards

Part 4 Flashcards

1
Q

how does immunotherapy work

A

antibodies from immune system target cancer cells

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2
Q

what cells secrete antibodies

A

B cells

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3
Q

what are the functions of antibodies

A

neutralize, opsonize, and destroy

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4
Q

why are antibodies unique

A

specific to antigen and create specific effector functions.

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5
Q

what does immunocompetence refer to

A

the ability for T cells being able to recognize the antigen presented on the MHC with the TCR.
positive

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6
Q

what does immunotolerance refer to

A

the process of eliminating any developing T or B lymphocytes that are autoreactive, i.e. reactive to the body itself.
negative

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7
Q

what can an antobody refer to

A

a B cell receptor or it can detach and be an antibody.

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8
Q

how many binding sites does an antibody have

A

2

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9
Q

what does affinity mean for antibodies

A

antibody is bound to B cell`

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10
Q

what does avidity mean for antibodies

A

antibody is soluble

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11
Q

what are the regions of antibodies

A

varible and constant regions

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12
Q

what are the regions of T cell Receptors

A

Va and Ca; Vb and Cb.
left side is alpha and right is beta

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13
Q

what are the chains of antibodies

A

light and heavy

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14
Q

how many parts is made up of the light chain

A

2

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15
Q

how many parts of the heavy chain

A

4

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16
Q

where is the Fab region of antibody

A

the two Y branches

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17
Q

what does the Fab region do

A

The fragment antigen-binding region (Fab region) is a region on an antibody that binds to antigens. It is composed of one constant and one variable domain of each of the heavy and the light chain.

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18
Q

where is the Fc region of antibody

A

the Y stem

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19
Q

what does the Fc region do

A

the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system

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20
Q

what genes encode for the light chain

A

Kappa and Lambda

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21
Q

what is the ratio of kappa and lambda

A

2 K for 1 L

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22
Q

how is B cell leukemia indentfied

A

kappa and lambda ratio is thrown off

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23
Q

what is the function of the heavy chain

A

determines the effector function of the antibody

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24
Q

what are the 5 classes of genes in the antibody

A

IgG, E, D, A, M

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25
Q

what does IgG determine

A

(blood) (can have subfamilies; IgG1-4, Ig2a) (can cross over into the placenta)
help prevent infections.

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26
Q

what does IgE do

A

mediates allergic reactions

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27
Q

what does IgD do

A

on the surface receptor of B cells; (not secreted)
receptor for antigens

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28
Q

What does IgA do

A

found in mucus/tears
protect the mucosal tissues from microbial invasion and maintain immune homeostasis with the microbiota.

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29
Q

what does IgM do

A

(first secretions of antibodies) (form pentomers) (high avidity)
binding to antigen and activating complement system

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30
Q

how are chains in antibody connected

A

disulfide bonds

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31
Q

what is at the middle of the Y for antibodies

A

a hinge

32
Q

what are two enzymes that can cleave antibodies

A

papain and pepsin

33
Q

how does papain cleave

A

Cleaves at the disulfide bond
Creates 3 fragments
2 Fabs (top of Y) and 1 Fc (stem of Y)

34
Q

how does pepsin cleave

A

Cleaves at the half of Y.
Creates two fragments
F(ab’)2 and pFc’
F(ab’)2 is the V of the Y
pFc’ is the stem of Y

35
Q

which antibodies have complement protein recognition

A

IgG

36
Q

what are the globular heads of antibodies

A

tips (binding region)

37
Q

what are the globular heads made up of

A

beta strands that are repeated

38
Q

what are the hypervariable regions

A

form the antigen-binding site and are found on both light and heavy chains. They also contribute to the specificity of each antibody.
loops

39
Q

what do the HV loops recognize

A

the epitope of antigen

40
Q

can multiple and different antibodies bind to the same antigen

A

yes; An antigen can be bound to multiple different antibodies depending on different antigenic determinants.

41
Q

what types of epitopes are there

A

continuous, discontinuous, and conformational

42
Q

what is the difference between continuous and discontinuous

A

A continuous, linear, or sequential, epitope is a fragment of the protein sequence. A discontinuous epitope is composed of several small fragments that are scattered in the protein sequence, but are close when the protein is structured.

43
Q

what does conformational mean

A

shape

44
Q

types of bonds antibodies form

A

Hydrogen, van der waals, electrostatic, hydrophobic forces

45
Q

how can bonds between antibody and antigen be disrupted

A

salt ratio, pH, temperature.

46
Q

what are cdr

A

cluster determining region

47
Q

how many cdrs bind to epitope

A

6 CDRs that bind the epitope (3 on each side)

48
Q

what is a hapten

A

an antigen that is too small to be recognized by itself

49
Q

difference TCR and antibody

A

Antibodies are soluble; TCRs are membrane bound.
Antibodies have two binding sites; TCRs only have one.
Antibodies can bind directly to the antigen; TCRs need antigen to be presented to them.
TCRs have four hypervariable (CDR loops) regions; three in antibodies

50
Q

how is the epitope exposed before it is presented on MHC

A

Epitope fragments are buried, so when a pathogen is digested/broken down, the epitope is then exposed.
The epitope then is bound and expressed by the MHC.

51
Q

how is MHC II presented on CD4 cells

A

by the APC

52
Q

how is MHC II expressed on CD8 cells

A

by the infected cell

53
Q

what are TAP proteins functions

A

take expressed viral protein fragments and express them on MHC I.

54
Q

what cells express mhc i

A

expressed on the cell surface of all nucleated cells and present peptide fragments derived from intracellular proteins

55
Q

what cells express mhc ii

A

antigen-presenting cells (APC) including dendritic cells (DC), macrophages, and B cells

56
Q

what do exopeptidases do

A

chop up viral amino acids in order to be fit on MHC

57
Q

which mhc cleft is deeper

A

mhc i

58
Q

which mhc cleft is wider

A

mhc ii

59
Q

how many residues can mhc i hold

A

8-10

60
Q

how many residues can mhc ii hold

A

13-17

61
Q

what is the cleft made up of for mhc i

A

alpha 1 and 2

62
Q

what is the cleft made up of for mhc ii

A

beta 1 and alpha 1

63
Q

how does the epitope fit for mhc i if too big

A

exonucleases

64
Q

which mhc is double bound

A

mhc ii

65
Q

why is there an invariant protein bound to mhc if no epitope exposed

A

because mhc is unstable in not bound

66
Q

how is mhc ii expressed when a pathogen is phagocytized

A

MHC II is produced in the ER when needed and travels to the membrane through a vesicle where it converges with the membrane to be expressed on the surface.

67
Q

which residues are optimum for mhc expression

A

Prefers amino acids to be hydrophobic and basic for carboxylic ends

68
Q

which mhc recognizes more variation

A

MHC II has a lot more variation and can recognize a lot more residues than class I

69
Q

what does the TCR recognize

A

both the epitope and parts of the MHC in order to have sufficient binding.

70
Q

what makes epitope and MHC binding and signal stronger

A

CD4 and CD8 proteins

71
Q

how does CD4 interact with MHCII

A

CD4 D1 and D2 interact with MHC II B1 and B2h

72
Q

how does CD8 interact with MHCI

A

CD8 B and A interact with the MHC I A1 and A2
CD8 are heterodimers

73
Q

what kinase brings in the CD8 or CD4 to MHC

A

Lck

74
Q

which MHC can T cells express

A

both I and II

75
Q

which cells don’t express MHC

A

RBCs, brain, sperm and egg

76
Q

Why bother determining the structure of TCR
proteins?

A

T cell repertoire is large, not all TCR may be structurally the same
* New structures may indicate novel functions

77
Q
A

Immunology (11 decks)

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