4 Antibodies - specificity and function Flashcards

1
Q

antigen origin name

A

from antibody generator

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2
Q

epitope

A

Many antibodies may bind the same antigen, each a separate site termed an antigenic determinant or epitope – antibodies recognise epitopes

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3
Q

what epitopes do antigens show

A

can also show repeated epitopes

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4
Q

what structure are antigens

A

can be diverse molecular structures

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5
Q

two effector cell types

A

B lymphocytes

T lymphocytes

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6
Q

B lymphocytes (B cells)

A
  • make antibodies (immunoglobulins) - cell surface and secreted
  • can improve the antibodies made over time
  • protection against extracellular pathogens & toxins
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7
Q

T lymphocytes (T cells)

A
  • express T cell receptors (TCR)
  • interact with other cells
  • can kill cells, or facilitate immune responses by other cells
  • Killer T cells (CD8+), Helper T cells and regulatory T cells (CD4+)
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8
Q

variable region

A

antigen-binding site

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9
Q

constant region

A

binds to cellular receptors – effector function

heavy chains have a hinge region in middle that gives a flexibility to the antibody

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10
Q

adaptive immune system

A

It changes over time!

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11
Q

immunoglobins examples

A

Serum glycoproteins also found in tissue fluids
B lymphocytes
antibodies

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12
Q

B lymphocytes

A

> surface antigen receptor (B cell receptor; BCR)

> associates with other cell surface proteins

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13
Q

Plasma cells produce

A

secretory immunoglobulin (antibody)

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14
Q

antibody classes

A

five classes of antibody: IgG, IgA, IgM, IgD & IgE

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15
Q

what is the first antibody line of defence

A

IgM

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16
Q

bonds in antiobodies

A

disulphide

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17
Q

what enzymes can be used in enzymatic cleavage

A

papain

pepsin

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18
Q

what happens if us papain enzyme for cleavage

A
  • 2x Fab, (Fragment- antigen binding)

- Fc (Fragment-crystallizable)

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19
Q

what happens if use pepsin enzyme for cleavage

A
  • Fab(2), bivalent binding

- Fc fragments

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20
Q

why is an antibody bifunctional

A
  • antigen binding

- ability to trigger effector functions

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21
Q

what light chains could be in a B cell

A

any one b cell will only use either kappa or lambda chain

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22
Q

constant region of a light chain

A

CL

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23
Q

variable region of a light chain

A

VL

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24
Q

variable domain of a heavy chain

A

CH1, CH2, CH3, sometimes CH4

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25
constant domain of a heavy chain
VH
26
antibody flexibility
Hinge regions | hinge of IgG subclasses is what makes them differ
27
Serum concentrations and half-life of IgG1
High concentration for IgG1 in serum | Half-life varies in subtypes – IgG1 usually longest
28
Serum concentrations and half-life of IgG3
IgG3 not found in serum is found in the skin = low concentration in serum
29
what makes up the domain structure of antibodies
- Variable (V) | - Constant (C)
30
what is the complementarity determining region
``` Peptide loops (hypervariable regions) are involved in interactions with antigen Hypervariable regions (loops) interact with antigen ```
31
how many complementarity determining regions does the heavy and light chains have each
3 CDRs each
32
what forms a paratope
Combination of H+L CDRs produces the unique antibody combining site
33
where is a paratope
within the antibody
34
what holds the antigen into place
non-covalent interactions of the paratope with the antigenic epitope
35
Size of antigens and area of interaction varies
Small, can fit into the antibody Lay across the antibody Globular, antibody can open up slightly and sit on it
36
Conformational specificity of an antibody
an antibody may recognise a specific 3D conformation of protein
37
primary sequence recognised by antibodies
linear epitope
38
secondary sequence recognised by antibodies
constrained secondary structure epitope (e.g. a loop or turn)
39
tertiary structure recognised by antibodies
discontinuous epitope (tertiary structure epitope) Tertiary structure gives the epitope
40
affinity
strength of a single antibody (Fab)/antigen bond
41
avidity
- Binding of a multivalent antibody to a multivalent antigen | - Avidity is likely to be the physiologically relevant affinity (functional affinity)
42
effect of bivalent antibody
equilibrium constant higher, functional ability increased as avidity higher
43
Fab binding
affinity
44
IgG bindings
affinity or functional avidity
45
IgM binding
affinity and avidity
46
how do antibody isotopes differ
hinge regions
47
IgM antibody structure
form a pentameric structure – using a joining chain protein and disulphide bonds – how circulates in body
48
why has IgM got a higher molecular weight
circulating as a pentamer
49
IgA antibody structure
dimer in the body
50
isotope physical differences
- CH1-CH2 hinge length - Interchain disulphide bond location and number - Number of CH domains - Variable glycosylation - Multimer capability
51
what is a multimeric immunoglobin
When antibodies come together some can become relatively large
52
Tissue distribution of IgG isotopes
IgG in most places
53
Tissue distribution of IgM isotopes
IgM when secreted mainly in peripheral blood
54
Tissue distribution of IgA isotopes
Dimeric IgA in mucosa – upper respiratory tract and gut
55
Tissue distribution of IgE isotopes
IgE mainly in skin, as allergic reactions take place here e.g. basophils and mast cells
56
Tissue distribution of IgD isotopes
IgD expressed in upper respiratory tract, possibly more important than IgA
57
Effects of pathogen specific antibodies
- Neutralize toxins - Block virus binding and entering cells - Opsonise pathogens - Activate complement
58
where are Antibody receptors present
Fc receptors present on phagocytic cells
59
Antibody function
Different classes have different functions
60
antibody capabilities
> Neutralisation > Complement activation > Opsonization cytotoxicity
61
what occurs at IgG
location of effector function sites