[DISCUSSION] MODULE 1 UNIT 3 Flashcards

1
Q

•Glycoproteins (gamma globulins) present in serum/ plasma

A

ANTIBODIES

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2
Q

•Produced by plasma cells in response to exposure to antigen

A

ANTIBODIES

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3
Q

•React specifically with that antigen in vivo or in vitro

A

ANTIBODIES

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4
Q

•Part of adaptive immunity or humoral immune response

A

ANTIBODIES

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5
Q

•As glycoprotein: consist of:

polypeptide
carbohydrate

A

82 – 96%
4 – 18%

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6
Q

•Antigen receptors on the surface of B cells

A

Immunoglobulins

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7
Q

•Ability of the host to produce this is genetically endowed

A

Immunoglobulins

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8
Q

• The property of Immunoglobulins in vivo is determined by genes

A

specific recognition

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9
Q

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

A

transmembrane sequence

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10
Q

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

A

transmembrane sequence

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11
Q

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

A

secreted into the plasma

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12
Q

TWO (2) HALLMARK PROPERTIES OF ANTIBODY

A
  1. SPECIFICITY
  2. DIVERSITY AND HETEROGENEITY
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13
Q

• Able to recognize and bind its particular antigen

A
  1. SPECIFICITY
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14
Q

• Complementariness of the antigenic epitope and antibody-combining site

A
  1. SPECIFICITY
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15
Q

• is based on a physical and chemical
reaction

A
  1. SPECIFICITY
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16
Q

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

A
  1. DIVERSITY AND HETEROGENEITY
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17
Q

• Extensive gene rearrangements

A
  1. DIVERSITY AND HETEROGENEITY
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18
Q

DISTRIBUTION OF ANTIBODIES

A

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

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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)
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20
Q

STRUCTURE OF ANTIBODIES

A

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

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21
Q

STRUCTURE OF ANTIBODIES

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

A

Gerald Edelman
Rodney Porter

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22
Q

The Immunoglobulin Domain

A
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23
Q

•localized between the CH2 domains of the two H chains

A

CARBOHYDRATES

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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
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25
Q

Ag binding

A

Fab

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26
Q

Valence= 1

A

Fab

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27
Q

Specificity determined by VH and VL

A

Fab

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28
Q

Effector functions

A

Fc

29
Q
A

F(ab’)2

30
Q

Pentamer

A

IgM

31
Q

Monomer

A

IgG
IgE
IgD

32
Q

Dimer

A

Secretory IgA

33
Q

Monomer (7s)

A

IgG

34
Q

IgG subclasses

A

IgG1
IgG2
IgG3
IgG4

35
Q

Pentamer (19s)

A

IgM

36
Q

Extra domain (CH4)

A

IgM

37
Q

J chain

A

IgM

38
Q

Third highest serum immunoglobulin

A

IgM

39
Q

First immunoglobulins made by fetus and b cells

A

IgM

40
Q

Fixes complement

A

IgM

41
Q

Agglutination immunoglobulin

A

IgM

42
Q

Binds to fc receptors

A

IgM

43
Q

B cell surface immunoglobulin

A

IgM

44
Q

Serum - monomer

A

IgA

45
Q

Secretions (sIgA)

A

Dimer (11s)
J chain
Secretory component

46
Q

Monomer
Tail piece

A

IgD

47
Q

Monomer
Extra domain (CH4)

A

IgE

48
Q

Action of IgE on Mast cells

A
49
Q

*PROPERTIES OF THE DIFFERENT IMMUNOGLOBULIN CLASSES

A

•Tabulate as many properties as you can
•Differences among IgG subclasses and IgA subclasses

50
Q

CLASSIFICATION OF ANTIBODIES

A

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
Q

A. According to HOST

A
  1. Autoantibody
  2. Homologous / alloantibody
  3. Isoantibody/ isoagglutinins
  4. Heterophil(e) antibodies
52
Q

B. According to Production in the Immune response

A
  1. Naturally-occurring
  2. Immune
53
Q

C. According to Serologic Behavior

A
  1. Agglutinin
  2. Precipitins
  3. Blocking antibody
  4. Complete antibody
54
Q

D. According to Temperature of Reaction

A
  1. Cold-reactive antibody
  2. Warm agglutinin/ warm-reactive antibody
55
Q

E. According to Complement Fixation

A
  1. Complement-fixing
  2. Non-complement fixing
56
Q

F. According to Monoclonal production

A
  1. Monoclonal antibody
  2. Polyclonal antibody
57
Q

VARIABILITY OF ANTIBODIES

A

A. ISOTYPES
B. ALLOTYPES
C. IDIOTYPES

58
Q

• Refer to the different classes of immunoglobulins

A

A. ISOTYPES

59
Q

• Based on the heavy chain (g, m, a, d, e)

A

A. ISOTYPES

60
Q

• Refer to genetic markers on the heavy chain of the Ig present on some individuals but not in others

A

B. ALLOTYPES

61
Q

• Follows a simple Mendelian heredity

A

B. ALLOTYPES

62
Q

• 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

A

C. IDIOTYPES

63
Q

• All antibody molecules share the same (?) but display remarkable variability in the (?)

A

basic structural characteristics
regions that bind antigens

64
Q

• An antibody molecule has a symmetric core structure composed of

A

two identical light chains and two identical heavy chains

65
Q

• Antibody heavy chains and light chains both consist of (?) that participate in antigen recognition and (?)

A

amino-terminal variable (V) regions
carboxy-terminal constant (C) regions

66
Q

help mediate some of the protective or effector functions of antibodies

A

C regions of the heavy chains

67
Q

• The antigen-binding portion of an antibody molecule is the

A

Fab region

68
Q

the C-terminal end that is involved in effector functions is the

A

Fc region