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IMMUNE 1 LEC > CHAPTER III – ANTIBODIES > Flashcards

CHAPTER III – ANTIBODIES Flashcards

1
Q

Glycoproteins that recognize and bind to a particular antigen with very high specificity.

A

ANTIBODIES

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2
Q

Made in response to exposure to the antigen.

A

ANTIBODIES

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3
Q

One virus or microbe may have several (?), to which different antibodies may bind.

A

antigenic determinant sites

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4
Q

Each antibody has at least two identical sites that bind

A

antigen: Antigen binding sites.

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5
Q

Belong to a group of serum proteins called

A

Immunoglobulins (Igs).

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6
Q

Electrophoresis at pH 8.6, immunoglobulins appear primarily in the

A

gamma band

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7
Q

GENERAL FUNCTIONS OF IMMUNOGLOBULINS

A

Neutralize toxic substances

Facilitate phagocytosis and kill microbes

Combine with antigens on cellular surfaces and thereby cause the destruction of these cells either extravascular (outside of the blood vessels within the mononuclear-phagocyte system or reticuloendothelial system) or intravascularly (within blood vessels though the action of complement)

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8
Q

postulated that certain cells had specific surface receptors for antigen

A

Paul Ehrlich

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9
Q

Occurred once antigen was introduced, it would select the cell with proper receptor, combination would take place and receptors would break off and enter the circulation as antibody molecules

A

EHRLICH’S SIDE-CHAIN THEORY

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10
Q

New receptors would form in place of those broken off and enter the circulation as antibody molecules

A

EHRLICH’S SIDE-CHAIN THEORY

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11
Q

Receptors are located on the surface of the Ab-producing cell

A

EHRLICH’S SIDE-CHAIN THEORY

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12
Q

Felix Haurowitz

A

TEMPLATE THEORY

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13
Q

Antibody producing cells are capable of synthesizing a generalized type of antibody, and when contact with an antigen occurs, the antigen serves as a mold or template and alters protein synthesis so that antibody with a specific fits is made

A

TEMPLATE THEORY

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14
Q

This now specific antibody enters the circulation, while the antigen remains behind to direct further synthesis

A

TEMPLATE THEORY

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15
Q

MOST ACCEPTED

A

CLONAL SELECTION

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16
Q

Niels Jerne and Macfarlane Burnet independently supported the idea of clonal selection process for antibody formation

A

CLONAL SELECTION

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17
Q

The key premise is that individual lymphocytes are genetically programmed to produce one type of immunoglobulin and that a specific antigen finds or selects those particular cells capable of responding to it, causing to proliferate

A

CLONAL SELECTION

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18
Q

A flexible Y-shaped molecule with four protein chains

A

Monomer

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19
Q

Monomer four protein chains

A

 2 identical light chains
 2 identical heavy chains
 1 LC, 2 HC = 4 Protein Chains

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20
Q

Two sections at the end of Y’s arms – Antigen binding sites (Fab).

A

Variable Regions

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21
Q

Identical on the same antibody, but vary from one antibody to another.

A

Variable Regions

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22
Q

Stem of monomer and lower parts of Y arms.

A

Constant Regions

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23
Q

For Complement fixation, Skin Fixation and Placental transfer

A

Fc region

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24
Q

first approximately 110 amino acids at the amino-terminal end the remaining amino acids can typically be divided up into three or more constant regions with very similar sequences, designated CH1, CH2, and CH3.

A

Variable domain of the H chain

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25
Q

are unique to each class and give each immunoglobulin

A

Constant regions of the H chain

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26
Q

: IgG
: IgA
: IgE
: IgD
: IgM

A

gamma H chain: IgG
alpha H chain: IgA
epsilon H chain: IgE
delta H chain: IgD
mu H chain : IgM

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27
Q

ANTIBODY VARIATIONS

A

ISOTYPE

ALLOTYPES

IDIOTYPE

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28
Q

Refers to the heavy chain that determine the Ig class

A

ISOTYPE

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29
Q

most common type

A

ISOTYPE

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30
Q

Minor variations of in the constant region

A

ALLOTYPES

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31
Q

E.g occur in the four IgG subclasses, in one IgA subclass, and in the kappa light chain.

A

Allotypes

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32
Q

Variations in variable regions

A

IDIOTYPE:

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33
Q

The aminoterminal ends of both L and H chains contain these regions, which are essential to the formation of the antigen-binding site.

A

IDIOTYPE

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34
Q

Possess both constant and variable regions

A

LIGHT CHAINS

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35
Q

o Kappa (65%)
o Lambda (35%)
o 2:1

A

LIGHT CHAINS

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36
Q

discovered through Bence Jones Proteins which are light chains produced by a malignant plasma cell from the urine of Multiple Myeloma pts

A

LIGHT CHAINS

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37
Q

Connect heavy and light chains
Connect light chains and light chains
Connect heavy chains and heavy chains

A

DISULFIDE BONDS

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38
Q

Between CH1 and CH2

A

HINGE REGION

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39
Q

Flexible region

A

HINGE REGION

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40
Q

Amino acid: PROLINE

A

HINGE REGION

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41
Q

Regions or sections in an Ig molecule

A
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42
Q

DOMAINS

A

A. 1 Light Chain

B. 1 Heavy Chain

C. IgM and IgE: with Extra CH4

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43
Q

1 Light Chain

A

2 domains: 1 VL and 1 CL

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44
Q

1 Heavy Chain

A

4 domains: 1 VH and 3 CH

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45
Q

: with Extra CH4

A

IgM and IgE

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46
Q

cleaves the Ig above the hinge region

A

Papain digestion

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47
Q

3 fragments

2 Fab + 1 FC

A

Papain digestion

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48
Q

cleaves Ig below the hinge region

A

Pepsin digestion

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49
Q

2 fragments

F(ab)2 + Fc

A

Pepsin digestion

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50
Q

BASIC Ig Structure

A

MONOMER

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51
Q

IgG, IgD, IgE, IgA (most)

A

MONOMER

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52
Q

2 binding site (2 valence)

A

MONOMER

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53
Q

Secretory component or piece of IgA2

A

DIMER

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54
Q

prevents the enzymatic degeneration of enzyme among secretions

A

DIMER

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55
Q

4 valence

A

DIMER

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56
Q

With J chain

A

DIMER

POLYMER

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57
Q

> 2 monomer

A

POLYMER

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58
Q

IgM

A

POLYMER

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59
Q

10 valence

A

POLYMER

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60
Q

Predominant type of immunoglobulin in humans

A

IgG

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61
Q

Greatest in serum concentration

A

IgG

(followed by IgM, IgA, IgD, IgE)

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62
Q

Longest half-life of any immunoglobulin class

A

IgG

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63
Q

Predominant in chronic phase of infection and in recovery

64
Q

Its subclasses are differentiated in the number of disulfide bonds

65
Q
  • predominant (67%); 2 disulfide bonds
66
Q
  • 22%; 4 disulfide bonds
67
Q
  • 7%; 15 disulfide bonds
68
Q
  • 4%; 2 disulfide bonds
69
Q

FUNCTIONS OF IgG

A

Provides immunity to the newborn by crossing thru the placenta (Most Efficient: IgG1)

Fixes or activates complement (Best: IgG3)

Opsonization

Neutralization of toxins and viruses

Participation in agglutination and precipitation reaction

70
Q

crossing thru the placenta (Most Efficient:)

71
Q

Only Ig to cross the placenta

72
Q

First Ab present/found in newborns

73
Q

Fixes or activates complement (Best:)

74
Q

FUNCTIONS OF IgM

A

Complement fixation: Most efficient in triggering the classical complement pathway

Best agglutinin

Opsonization

Neutralization of toxins

75
Q

FUNCTIONS OF IgD

A

Responsible for IMMUNOREGULATION

76
Q

DISEASE ASSOCIATIONS OF IgG

A

o Infectious diseases, such as hepatitis, rubella, and infectious mononucleosis
o Collagen disorders, such as rheumatoid arthritis and systemic lupus erythematosus
o Hematologic disorders, such as polyclonal gammopathies, monoclonal gammopathies, monocytic leukemia, and Hodgkin’s disease

77
Q

DISEASE ASSOCIATIONS OF IgM

A

o Infectious diseases, such as subacute bacterial endocarditis, infectious mononucleosis, leprosy, trypanosomiasis, malaria, and actinomycosis
o Collagen disorders, such as scleroderma
o Hematologic disorders, such as polyclonal gammopathies, monocytic leukemia, and monoclonal gammopathies (e.g., Waldenström’s macroglobulinemia)

78
Q

DISEASE ASSOCIATIONS OF IgA

A

o Infectious diseases, such as tuberculosis and actinomycosis
o Collagen disorders, such as rheumatoid arthritis
o Hematologic disorders, such as polyclonal gammopathies,
o Monocytic leukemia, and monoclonal gammopathy (e.g., IgA myeloma)
o Liver disease, such as Laennec’s cirrhosis and chronic active hepatitis

79
Q

Pentamer in serum; Monomer as a surface marker

80
Q

Free state: Star-like appearance

81
Q

Combined with Ag: crab-like appearance

82
Q

Known as the macroglobulin

83
Q

Most primitive

84
Q

First to appear in phylogeny and the last to leave in senescence

85
Q

First to appear/be made by infants

86
Q

FIRST to appear after a primary antigenic stimulus

87
Q

IgM GRAM NEGATIVE bacteria Example:

A

Wasserman antibodies, heterophile antibodies, RF (Rheumatoid factor), cold agglutinins and allohemagglutinins belong under this type of antibody

88
Q

Formed in response to stimulus by GRAM NEGATIVE bacteria

89
Q

Monomeric in (IgA1)

90
Q

Occurs as a dimer (IgA2) in

A

secretions

91
Q

Secretory Component provides:

A

Mucosal Immunity

92
Q

Mucosal Immunity

A

Prevents attachment of pathogen to mucosal surface
Prevent enzymatic degradation of IgA

93
Q

Found on unstimulated but immunocompetent cell

94
Q

Postulated as anti-idiotypic antibody involved in a feedback mechanism to switch off B-CELLS

95
Q

Location: on the surface of a B lymphocyte in association with IgM

96
Q

Least abundant immunoglobulin in the serum

97
Q

Heat-labile antibodies, originally called as Reagin antibody

98
Q

Binds strongly to a receptor on mast cells and basophils and together with antigen, mediates the release of histamine and heparin from these cells

99
Q

Mediates hypersensitivity reactions, such as allergies, and anaphylaxis, and generally responsible for an individual’s immunity to invading parasites

100
Q

Eosinophil recognizes the IgE attached to parasite to release Major Basic protein and Eosinophil Cationic Protein

101
Q

Multiple epitopes per

A

one antigen

102
Q

Depends on the (?) to which an epitope is more specific

103
Q

Apply electricity in the serum to check for migration at pH 8.6 (alkaline)

A

Electrophoresis

104
Q

Electrophoresis proteins

A
  1. Albumin – primary
  2. Alpha-proteins
  3. Beta-proteins
  4. Gamma-proteins – Immunoglobulins
105
Q

Once Ab binds with Ag, Ag cannot create a toxic effect

A

Neutralize toxic substances

106
Q

Some Ig can act as an opsonin

A

Facilitate phagocytosis and kill microbes

107
Q

extravascular (outside of the blood vessels within the)

A

mononuclear-phagocyte system or reticuloendothelial system

108
Q

intravascularly (within blood vessels though the)

A

action of complement

109
Q

– antigen-binding site

110
Q

fragment crystallizable or fragment constant

111
Q

not capable of antigen-binding but can bind to cells (immune cells – B and T cells)

112
Q

capable of binding or fixing the complement

113
Q

each Ag has an Ab which alerts the immune system

114
Q

T cell attaches to Ab → reticuloendothelial system

A

Extravascular

115
Q

organs under RES:

A

o spleen – primary cell  Apoptosis
o liver

116
Q

Toxic and immediate destruction of the Ag

A

Intravascular

117
Q

Stimulation of complement attaches to Fc portion leading to lysis

A

Intravascular

118
Q

Receptors are located on the surface of the Ab-producing cell

A

EHRLICH’S SIDE-CHAIN THEORY

119
Q

Different studies, the same idea

A

CLONAL SELECTION

120
Q

Example: Hematopoiesis – formation of blood cells

A

CLONAL SELECTION

121
Q

HSC – able to produce different CFUs

A

CLONAL SELECTION

122
Q

Erythroid – rbc
Myeloid – granulocytes, monocytes, platelets
Lymphoid – B and T lymphocytes (B cell matures into a plasma cell once Ag is encountered; plasma cell produces Ab)

A

CLONAL SELECTION

123
Q

1 LC, 2 HC =

A

4 Protein Chains

124
Q

can filter urine

A

Bence Jones Proteins

125
Q

Bence Jones Proteins

heated at 50-60oC →
heated at 100oC →

A

precipitates

dissolves

126
Q

2 mols of sulfide

A

DISULFIDE BONDS

127
Q

Complete antibody =

A

12 domains (2 LC [2x2] x 2 HC [4x2])

128
Q

IgE =

A

14 domains (+2)

129
Q

Cutting parts of Igs through enzyme treatment

A

FRAGMENTATION

130
Q

Ags and Ig are monomer in nature

131
Q

can bind 10 Ags at the same time

132
Q

– larger complexes; particulate ag and ab

A

Agglutination

133
Q

– smaller complexes, soluble ag, best precipitin or best Ab

A

Precipitation

134
Q

Monomer
Too small to cause an agglutination rx
Participates with the use of an additional reagent – incomplete antibody

135
Q

– smaller complexes, soluble ag, best precipitin or best Ab

A

Precipitation

136
Q

↑ WBCs – abnormal in function

A

monocytic leukemia

137
Q

Counterpart: Neutrophil

138
Q

(counterpart: mast cells and basophils)

A

IgE Allergic reactions

139
Q

(counterpart: eosinophils)

A

IgE Parasitic infections

140
Q

Early onset or acute phase infection

141
Q

More efficient than IgG3

142
Q

Has a large structure – only needs 1 molecule of IgM to activate the complement (2 mols for IgG)

143
Q

Best agglutinin – larger complexes

144
Q

() – predominant type of IgA

145
Q

Additional Ig for newborns and infants

146
Q

Breastfeeding mother can transfer (?) thru breastmilk to the baby (placenta for IgG)

147
Q

Unknown function at first

148
Q

control of immune response between lymphocyte and macrophages; has something to do with maturation of T cells

149
Q

has surface markers of IgM and IgD

A

mature T cell

150
Q

did not encountered and Ag

A

unstimulated cell

151
Q

can interact w/ an Ag

A

immunocompetent B cell

152
Q

To maintain homeostasis or balance

Excess = autoimmune disorder (attacking of own cells, hyperactive, oversensitive)

A

Postulated as anti-idiotypic antibody involved in a feedback mechanism to switch off B-CELLS

153
Q

2nd to greatest conc in serum

154
Q

easily destroyed by heat

A

Heat-labile

155
Q

mast cells and basophils granules

A

histamine and heparin

156
Q

Eosinophil granules

A

Major Basic protein and Eosinophil Cationic Protein

IMMUNE 1 LEC (28 decks)

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