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
what does IgG determine
(blood) (can have subfamilies; IgG1-4, Ig2a) (can cross over into the placenta) help prevent infections.
26
what does IgE do
mediates allergic reactions
27
what does IgD do
on the surface receptor of B cells; (not secreted) receptor for antigens
28
What does IgA do
found in mucus/tears protect the mucosal tissues from microbial invasion and maintain immune homeostasis with the microbiota.
29
what does IgM do
(first secretions of antibodies) (form pentomers) (high avidity) binding to antigen and activating complement system
30
how are chains in antibody connected
disulfide bonds
31
what is at the middle of the Y for antibodies
a hinge
32
what are two enzymes that can cleave antibodies
papain and pepsin
33
how does papain cleave
Cleaves at the disulfide bond Creates 3 fragments 2 Fabs (top of Y) and 1 Fc (stem of Y)
34
how does pepsin cleave
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
which antibodies have complement protein recognition
IgG
36
what are the globular heads of antibodies
tips (binding region)
37
what are the globular heads made up of
beta strands that are repeated
38
what are the hypervariable regions
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
what do the HV loops recognize
the epitope of antigen
40
can multiple and different antibodies bind to the same antigen
yes; An antigen can be bound to multiple different antibodies depending on different antigenic determinants.
41
what types of epitopes are there
continuous, discontinuous, and conformational
42
what is the difference between continuous and discontinuous
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
what does conformational mean
shape
44
types of bonds antibodies form
Hydrogen, van der waals, electrostatic, hydrophobic forces
45
how can bonds between antibody and antigen be disrupted
salt ratio, pH, temperature.
46
what are cdr
cluster determining region
47
how many cdrs bind to epitope
6 CDRs that bind the epitope (3 on each side)
48
what is a hapten
an antigen that is too small to be recognized by itself
49
difference TCR and antibody
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
how is the epitope exposed before it is presented on MHC
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
how is MHC II presented on CD4 cells
by the APC
52
how is MHC II expressed on CD8 cells
by the infected cell
53
what are TAP proteins functions
take expressed viral protein fragments and express them on MHC I.
54
what cells express mhc i
expressed on the cell surface of all nucleated cells and present peptide fragments derived from intracellular proteins
55
what cells express mhc ii
antigen-presenting cells (APC) including dendritic cells (DC), macrophages, and B cells
56
what do exopeptidases do
chop up viral amino acids in order to be fit on MHC
57
which mhc cleft is deeper
mhc i
58
which mhc cleft is wider
mhc ii
59
how many residues can mhc i hold
8-10
60
how many residues can mhc ii hold
13-17
61
what is the cleft made up of for mhc i
alpha 1 and 2
62
what is the cleft made up of for mhc ii
beta 1 and alpha 1
63
how does the epitope fit for mhc i if too big
exonucleases
64
which mhc is double bound
mhc ii
65
why is there an invariant protein bound to mhc if no epitope exposed
because mhc is unstable in not bound
66
how is mhc ii expressed when a pathogen is phagocytized
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
which residues are optimum for mhc expression
Prefers amino acids to be hydrophobic and basic for carboxylic ends
68
which mhc recognizes more variation
MHC II has a lot more variation and can recognize a lot more residues than class I
69
what does the TCR recognize
both the epitope and parts of the MHC in order to have sufficient binding.
70
what makes epitope and MHC binding and signal stronger
CD4 and CD8 proteins
71
how does CD4 interact with MHCII
CD4 D1 and D2 interact with MHC II B1 and B2h
72
how does CD8 interact with MHCI
CD8 B and A interact with the MHC I A1 and A2 CD8 are heterodimers
73
what kinase brings in the CD8 or CD4 to MHC
Lck
74
which MHC can T cells express
both I and II
75
which cells don't express MHC
RBCs, brain, sperm and egg
76
Why bother determining the structure of TCR proteins?
T cell repertoire is large, not all TCR may be structurally the same * New structures may indicate novel functions
77