Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Infection and Immunity > 4 Antibodies - specificity and function > Flashcards

4 Antibodies - specificity and function Flashcards

1
Q

antigen origin name

A

from antibody generator

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

epitope

A

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

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

what epitopes do antigens show

A

can also show repeated epitopes

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

what structure are antigens

A

can be diverse molecular structures

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

two effector cell types

A

B lymphocytes

T lymphocytes

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

variable region

A

antigen-binding site

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

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

adaptive immune system

A

It changes over time!

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

immunoglobins examples

A

Serum glycoproteins also found in tissue fluids
B lymphocytes
antibodies

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

B lymphocytes

A

> surface antigen receptor (B cell receptor; BCR)

> associates with other cell surface proteins

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

Plasma cells produce

A

secretory immunoglobulin (antibody)

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

antibody classes

A

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

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

what is the first antibody line of defence

A

IgM

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

bonds in antiobodies

A

disulphide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what enzymes can be used in enzymatic cleavage

A

papain

pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what happens if us papain enzyme for cleavage

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

- Fc (Fragment-crystallizable)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what happens if use pepsin enzyme for cleavage

A
  • Fab(2), bivalent binding

- Fc fragments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

why is an antibody bifunctional

A
  • antigen binding

- ability to trigger effector functions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what light chains could be in a B cell

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

constant region of a light chain

A

CL

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

variable region of a light chain

A

VL

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

variable domain of a heavy chain

A

CH1, CH2, CH3, sometimes CH4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

constant domain of a heavy chain

A

VH

26
Q

antibody flexibility

A

Hinge regions

hinge of IgG subclasses is what makes them differ

27
Q

Serum concentrations and half-life of IgG1

A

High concentration for IgG1 in serum

Half-life varies in subtypes – IgG1 usually longest

28
Q

Serum concentrations and half-life of IgG3

A

IgG3 not found in serum is found in the skin = low concentration in serum

29
Q

what makes up the domain structure of antibodies

A
  • Variable (V)

- Constant (C)

30
Q

what is the complementarity determining region

A 
Peptide loops (hypervariable regions) are involved in interactions with antigen
Hypervariable regions (loops) interact with antigen
31
Q

how many complementarity determining regions does the heavy and light chains have each

A

3 CDRs each

32
Q

what forms a paratope

A

Combination of H+L CDRs produces the unique antibody combining site

33
Q

where is a paratope

A

within the antibody

34
Q

what holds the antigen into place

A

non-covalent interactions of the paratope with the antigenic epitope

35
Q

Size of antigens and area of interaction varies

A

Small, can fit into the antibody
Lay across the antibody
Globular, antibody can open up slightly and sit on it

36
Q

Conformational specificity of an antibody

A

an antibody may recognise a specific 3D conformation of protein

37
Q

primary sequence recognised by antibodies

A

linear epitope

38
Q

secondary sequence recognised by antibodies

A

constrained secondary structure epitope (e.g. a loop or turn)

39
Q

tertiary structure recognised by antibodies

A

discontinuous epitope (tertiary structure epitope) Tertiary structure gives the epitope

40
Q

affinity

A

strength of a single antibody (Fab)/antigen bond

41
Q

avidity

A
  • Binding of a multivalent antibody to a multivalent antigen

- Avidity is likely to be the physiologically relevant affinity (functional affinity)

42
Q

effect of bivalent antibody

A

equilibrium constant higher, functional ability increased as avidity higher

43
Q

Fab binding

A

affinity

44
Q

IgG bindings

A

affinity or functional avidity

45
Q

IgM binding

A

affinity and avidity

46
Q

how do antibody isotopes differ

A

hinge regions

47
Q

IgM antibody structure

A

form a pentameric structure – using a joining chain protein and disulphide bonds – how circulates in body

48
Q

why has IgM got a higher molecular weight

A

circulating as a pentamer

49
Q

IgA antibody structure

A

dimer in the body

50
Q

isotope physical differences

A
  • CH1-CH2 hinge length
  • Interchain disulphide bond location and number
  • Number of CH domains
  • Variable glycosylation
  • Multimer capability
51
Q

what is a multimeric immunoglobin

A

When antibodies come together some can become relatively large

52
Q

Tissue distribution of IgG isotopes

A

IgG in most places

53
Q

Tissue distribution of IgM isotopes

A

IgM when secreted mainly in peripheral blood

54
Q

Tissue distribution of IgA isotopes

A

Dimeric IgA in mucosa – upper respiratory tract and gut

55
Q

Tissue distribution of IgE isotopes

A

IgE mainly in skin, as allergic reactions take place here e.g. basophils and mast cells

56
Q

Tissue distribution of IgD isotopes

A

IgD expressed in upper respiratory tract, possibly more important than IgA

57
Q

Effects of pathogen specific antibodies

A
  • Neutralize toxins
  • Block virus binding and entering cells
  • Opsonise pathogens
  • Activate complement
58
Q

where are Antibody receptors present

A

Fc receptors present on phagocytic cells

59
Q

Antibody function

A

Different classes have different functions

60
Q

antibody capabilities

A

> Neutralisation
Complement activation
Opsonization cytotoxicity

61
Q

what occurs at IgG

A

location of effector function sites

Infection and Immunity (29 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions