[DISCUSSION] MODULE 1 UNIT 3 Flashcards

1
Q

•Glycoproteins (gamma globulins) present in serum/ plasma

A

ANTIBODIES

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

•Produced by plasma cells in response to exposure to antigen

A

ANTIBODIES

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

•React specifically with that antigen in vivo or in vitro

A

ANTIBODIES

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

•Part of adaptive immunity or humoral immune response

A

ANTIBODIES

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

•As glycoprotein: consist of:

polypeptide
carbohydrate

A

82 – 96%
4 – 18%

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

•Antigen receptors on the surface of B cells

A

Immunoglobulins

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

•Ability of the host to produce this is genetically endowed

A

Immunoglobulins

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

• The property of Immunoglobulins in vivo is determined by genes

A

specific recognition

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

• The expression of immunoglobulins on a B cell surface require the presence of

A

transmembrane sequence

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

• Permits insertion and anchorage of the immunoglobulins into the cell membrane

A

transmembrane sequence

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

•In the absence of this transmembrane sequence as occurs in plasma cells, the antibodies become

A

secreted into the plasma

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

TWO (2) HALLMARK PROPERTIES OF ANTIBODY

A
  1. SPECIFICITY
  2. DIVERSITY AND HETEROGENEITY
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

• Able to recognize and bind its particular antigen

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

• Complementariness of the antigenic epitope and antibody-combining site

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

• is based on a physical and chemical
reaction

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

• Able to recognize and respond to a vast array of antigen challenge in nature

A
  1. DIVERSITY AND HETEROGENEITY
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

• Extensive gene rearrangements

A
  1. DIVERSITY AND HETEROGENEITY
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

DISTRIBUTION OF ANTIBODIES

A

•Blood plasma / serum (in vitro)
•Saliva
•Tears
•Mucous secretions
•Milk colostrums
•Other body fluids

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

BIOLOGIC ACTIVITIES

  1. Primary:
  2. Secondary:
A
  1. Primary:
    bind antigens specifically
  2. Secondary:
    a. Opsonization
    b. Neutralization of toxins and virus
    c. Complement fixation
    d. Antibody-dependent cell-mediated cytotoxicity (ADCC)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

STRUCTURE OF ANTIBODIES

A

•BASIC UNIT
•DISULFIDE BONDS
•REGIONS
•DOMAINS
• FRAGMENTS
•HINGE REGION
• S -VALUE

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

STRUCTURE OF ANTIBODIES

1950s by (?) - (USA)
1960s by (?) - (England)

A

Gerald Edelman
Rodney Porter

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

The Immunoglobulin Domain

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

•localized between the CH2 domains of the two H chains

A

CARBOHYDRATES

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

•Functions of the carbohydrate include:

A
  1. increasing the solubility of immunoglobulin
  2. providing protection against degradation
  3. enhancing functional activity of the FC domains
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Ag binding
Fab
26
Valence= 1
Fab
27
Specificity determined by VH and VL
Fab
28
Effector functions
Fc
29
F(ab')2
30
Pentamer
IgM
31
Monomer
IgG IgE IgD
32
Dimer
Secretory IgA
33
Monomer (7s)
IgG
34
IgG subclasses
IgG1 IgG2 IgG3 IgG4
35
Pentamer (19s)
IgM
36
Extra domain (CH4)
IgM
37
J chain
IgM
38
Third highest serum immunoglobulin
IgM
39
First immunoglobulins made by fetus and b cells
IgM
40
Fixes complement
IgM
41
Agglutination immunoglobulin
IgM
42
Binds to fc receptors
IgM
43
B cell surface immunoglobulin
IgM
44
Serum - monomer
IgA
45
Secretions (sIgA)
Dimer (11s) J chain Secretory component
46
Monomer Tail piece
IgD
47
Monomer Extra domain (CH4)
IgE
48
Action of IgE on Mast cells
49
*PROPERTIES OF THE DIFFERENT IMMUNOGLOBULIN CLASSES
•Tabulate as many properties as you can •Differences among IgG subclasses and IgA subclasses
50
CLASSIFICATION OF ANTIBODIES
A. According to HOST B. According to Production in the Immune response C. According to Serologic Behavior D. According to Temperature of Reaction E. According to Complement Fixation F. According to Monoclonal production
51
A. According to HOST
1. Autoantibody 2. Homologous / alloantibody 3. Isoantibody/ isoagglutinins 4. Heterophil(e) antibodies
52
B. According to Production in the Immune response
1. Naturally-occurring 2. Immune
53
C. According to Serologic Behavior
1. Agglutinin 2. Precipitins 3. Blocking antibody 4. Complete antibody
54
D. According to Temperature of Reaction
1. Cold-reactive antibody 2. Warm agglutinin/ warm-reactive antibody
55
E. According to Complement Fixation
1. Complement-fixing 2. Non-complement fixing
56
F. According to Monoclonal production
1. Monoclonal antibody 2. Polyclonal antibody
57
VARIABILITY OF ANTIBODIES
A. ISOTYPES B. ALLOTYPES C. IDIOTYPES
58
• Refer to the different classes of immunoglobulins
A. ISOTYPES
59
• Based on the heavy chain (g, m, a, d, e)
A. ISOTYPES
60
• Refer to genetic markers on the heavy chain of the Ig present on some individuals but not in others
B. ALLOTYPES
61
• Follows a simple Mendelian heredity
B. ALLOTYPES
62
• Refer to the unique specificity of the antibody conferred at the paratope on the basis of a.a. on the variable sequence of the Ig
C. IDIOTYPES
63
• All antibody molecules share the same (?) but display remarkable variability in the (?)
basic structural characteristics regions that bind antigens
64
• An antibody molecule has a symmetric core structure composed of
two identical light chains and two identical heavy chains
65
• Antibody heavy chains and light chains both consist of (?) that participate in antigen recognition and (?)
amino-terminal variable (V) regions carboxy-terminal constant (C) regions
66
help mediate some of the protective or effector functions of antibodies
C regions of the heavy chains
67
• The antigen-binding portion of an antibody molecule is the
Fab region
68
the C-terminal end that is involved in effector functions is the
Fc region