Antibodies (year 2) Flashcards

1
Q

define an antigen

A

any molecule that can bind specifically to an antibody or antigen receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

define an epitope

A

site in an antigen recognised by an antibody or antigen receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

define an antibody

A

protein that binds specifically to an antigen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is affinity?

A

binding of one antigen binding fragment (Fab) region to one epitope

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what is avidity?

A

overall attraction between antigen and antibody - able to bind to more than one epitope

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what does high avidity and affinity mean for the function of the antibody?

A

carries out its function well, if they don’t bind well to the pathogen then they won’t work properly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what immune response are antibodies apart of?

A

humoral - produced by B cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what cells produce antibodies?

A

B cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

name the 5 classes of immunoglobulin

A

IgM, IgG, IgA, IgE, IgD

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

where are the three main classes of antibody produced?

A

IgM - spleen/lymph nodes
IgG - spleen/lymph nodes
IgA - locally in mucosal systems (GI/respiratory)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what species of animal is IgD mainly found in?

A

fish

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

describe the structure of IgG

A

Y shaped structure with hinge regions and two antigen binding sites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

describe the structure of IgM

A

pentameric structure with 5 subunits joined by glycoprotein bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

describe the structure of IgA

A

2 subunit structure joined by a J chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what are the two regions of an immunoglobulin subunit?

A

constant and variable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

what is the role of the constant region of an immunoglobulin?

A

interacts with the hosts cells and can alter the effector function, delivers antibody to specific areas and helps to initiate the compliment cascade and when it changes it is known as class switching

17
Q

what triggers class switching?

A

cytokines

18
Q

what is the role of the variable region on immunoglobulins?

A

free to interact with the pathogen

19
Q

what is the main isotope of immunoglobulin produced during a primary immune response?

A

M

20
Q

what is the main isotope of immunoglobulin present during a secondary immune response?

A

IgG and IgA

21
Q

describe the length and magnitude of primary and secondary immune responses

A

primary - short lived and low magnitude

secondary - rapid and longer duration with higher magnitude

22
Q

why does class switching from IgM to IgG and IgA occur?

A

IgA and IgG have a higher affinity for antigens than IgM

23
Q

where is the primary immune response initiated?

A

local lymph nodes

24
Q

where is the secondary immune response initiated?

A

local lymphoid tissue

25
Q

what are the two cells that synthesise antibody?

A

blasting B lymphocytes

plasma cells

26
Q

where are the plasma and blasting B lymphocyte cells that synthesise antibody located?

A

in germinal centres

27
Q

what are the three main functions of antibody?

A

neutralise pathogens
activate complement
opsonisation

28
Q

what does neutralisation of pathogens prevent?

A

pathogen attachment
invasion of host cells
replication
toxin production

29
Q

IgA is a tissue specific effector, describe this process?

A

secreted locally to mucosal tissue then binds to polymeric Ig receptor and passes into the lumen of the enterocyte
the receptor is then proteolysed to leave the secretory component protecting IgA