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IMMUNOLOGY AND SEROLOGY LECTURE > C3 - LESSON 2: ANTIBODIES > Flashcards

C3 - LESSON 2: ANTIBODIES Flashcards

1
Q

Specific proteins referred to as immunoglobulins

A

Antibodies

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2
Q

Antibodies Composition:

A

86%-98% polypeptide; 2%-14% carbohydrate

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3
Q

Considered to be the humoral branch of immune response

A

Antibodies

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4
Q

can be found in blood plasma and in many body fluids such as tears, saliva and colostrum.

A

Antibodies

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5
Q

The primary function of an antibody in body defenses is to (?), which may be enough to neutralize bacterial toxins or some viruses.

A

combine with antigen

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6
Q

A secondary interaction of an antibody molecule with another (?) (e.g., complement) is usually required to dispose of larger antigens (e.g., bacteria).

A

effector agent

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7
Q

5 Major Classes (basis: heavy chain)

A
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8
Q

IgG-
IgM-
IgA-
IgD-
IgE-

A

IgG- gamma
IgM- mu
IgA- alpha
IgD- delta
IgE- epsilon

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9
Q

Each immunoglobulin is made up of a number of regions called

A

domains

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10
Q

All immunoglobulin molecules are made up of a basic (?) (TETRAPEPTIDE) that consists of two large chains called (?) and two smaller chains called (?).

A

four-chain polypeptide unit

heavy or H chains

light or L chains

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11
Q

Tetrapeptide Structure of Immunoglobulins is held together by

A

noncovalent forces and disulfide interchain bridges

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12
Q

The basic structure of immunoglobulins was elucidated in the 1950s and 1960s by the efforts of two men:

A
  1. Gerald Edelman
  2. Rodney Porter
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13
Q

N

A
  1. Gerald Edelman
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14
Q

used proteolytic enzyme which cleaved IgG into 3 pieces.

A
  1. Rodney Porter
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15
Q

For their contributions, these men shared the Nobel Prize in physiology and medicine in 1972.

A
  1. Gerald Edelman
  2. Rodney Porter
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16
Q

They chose to work with immunoglobulin G.

A
  1. Gerald Edelman
  2. Rodney Porter
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17
Q

Tips of the heavy and light chains

A

Variable Region

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18
Q

Antigen-binding site

A

Variable Region

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19
Q

Recognizes and attaches specifically to a particular antigen

A

Variable Region

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20
Q

Number of binding sites = valence

A

Variable Region

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21
Q

Responsible for the type and antigen-antibody reaction that occurs

A

Constant Region

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22
Q

Constant region of heavy chain differs from one antibody class to the other

A

Constant Region

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23
Q

Structure serves as a basis for distinguishing the 5 different classes: IgG, IgA, IgM, IgD and IgE

A

Constant Region

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24
Q

segment of H chain located between the CH1 and CH2 regions

A

Hinge Region

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25
Q

Has high proline and hydrophobic residue

A

Hinge Region

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26
Q

Allows bending of antibody

A

Hinge Region

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27
Q
  • proteolytic enzyme
A

Papain

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28
Q

used to cleave IgG into three pieces of about equal size

A

Papain

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29
Q

Carboxymethyl cellulose ion exchange chromatography separated this material into two types of fragments:

A
  1. Fc fragment (fragment crystallizable)
  2. Fab fragment (fragment antigen-binding)
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30
Q

spontaneously crystallized at 4 degrees Celsius

A
  1. Fc fragment (fragment crystallizable)
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31
Q

no antigen-binding ability

A
  1. Fc fragment (fragment crystallizable)
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32
Q

known to represent the carboxy-terminal halves of two H chains that are held together by S-S bonding

A
  1. Fc fragment (fragment crystallizable)
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33
Q

Important in effector functions- opsonization and complement fixation

A
  1. Fc fragment (fragment crystallizable)
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34
Q

Have antigen-binding capacity

A
  1. Fab fragment (fragment antigen-binding)
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35
Q

Each fragment represented one antigen-binding site

A
  1. Fab fragment (fragment antigen-binding)
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36
Q

Each Fab fragment thus consists of one L chain and one-half of an H chain, held together by disulfide bonding.

A
  1. Fab fragment (fragment antigen-binding)
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37
Q
  • used pepsin to obtain additional evidence for the structure of immunoglobulins.
A

Alfred Nisonoff

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38
Q
  • proteolytic enzyme was found to cleave IgG at the carboxy-terminal side of the interchain disulfide bonds yielding one single fragment with a molecular weight of 100,000 d and all the antigenbinding ability, known as F(ab).
A

Pepsin

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39
Q

An additional fragment called (?) was similar to FC except that it disintegrated into several smaller pieces

A

FC

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40
Q

Discovered in 1845 by Dr. Henry Bence-Jones

A

Bence-Jones proteins

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41
Q

L chains that were being secreted by malignant plasma cells

A

Bence-Jones proteins

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42
Q

60ºC- they precipitate from urine

A

Bence-Jones proteins

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43
Q

further heating to 80ºC- they re-dissolve

A

Bence-Jones proteins

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44
Q

Two main types of L chains:

A
  1. Kappa
  2. Lambda
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45
Q

each type had essentially the same sequence

A

Lambda

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46
Q

Constant region

A

Lambda

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47
Q

Variable region (amino-terminal end)

A

Lambda

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48
Q

Constant regions of the (?) are unique to each class and give each immunoglobulin type its name.

A

H chain

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49
Q

Hence, IgG has an

A

γ H chain, IgM a μ chain, IgA an α chain, IgD a δ chain, and IgE an ε chain.

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50
Q
  • unique amino acid sequence that is common to all immunoglobulin molecules of a given class in a given species
A

Isotype

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51
Q
  • Minor variations of these sequences that are present in some individuals but not others
A

Allotype

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52
Q
  • variable portions of each chain are unique to a specific antibody molecule.
A

Idiotype

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53
Q

75-80% of total serum immunoglobulins

A

IgG

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54
Q

has the longest half-life of any immunoglobulin class

A

IgG

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55
Q
  • Second most efficient at binding complement
A

IgG1 (67%)

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56
Q
  • largest hinge region and the largest number of interchain disulfide bond
A

IgG3 (7%)

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57
Q

most efficient at binding complement

A

IgG3 (7%)

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58
Q

have shorter hinge segments, which tend to make them poor mediators of complement activation

A

IgG2 (22%)

IgG4 (4%)

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59
Q

Major functions of IgG:
1. providing (?) because IgG can cross the placenta
2. fixing (?)
3. coating antigen for enhanced (?)
4. neutralizing (?)
5. participating in (?)

A

immunity for the newborn

complement

phagocytosis (opsonization)

toxins and viruses

agglutination and precipitation reactions

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60
Q

Macroglobulin

A

IgM

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61
Q

5-10% of total serum immunoglobulins

A

IgM

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62
Q

Half-life: 10 days

A

IgM

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63
Q
  • glycoprotein with several cysteine residues which serves as linkage points and holds together the five monomeric units
A

J or joining chain

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64
Q

Starlike shape

A

IgM

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65
Q

Primary response antibody

A

IgM

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66
Q

it is the first to appear after antigenic stimulation, and it is the first to appear in the maturing infant.

A

IgM

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67
Q

most efficient of all immunoglobulins at triggering the classical complement pathway

A

IgM

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68
Q

also serves as a surface receptor for antigen

A

IgM

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69
Q

Functions of IgM:

A
  1. Complement fixation
  2. Agglutination
  3. Opsonization
  4. Toxin neutralization
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70
Q

10-15% of all circulating immunoglobulin

A

IgA

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71
Q

is synthesized in plasma cells found mainly in mucosal-associated lymphoid tissue, and it is released in dimeric form

A

Secretory IgA

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72
Q

It is not capable of fixing complement by the classical pathway, although aggregation of immune complexes may trigger the alternate complement pathway

A

IgA

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73
Q

IgA Secretory component (molecular weight of about (?))

A

70,000

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74
Q

is later attached to the FC region around the hinge portion of the a-chains

A

IgA

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75
Q
  • plays an important role in neutralizing toxins produced by microorganisms and helps to prevent bacterial adherence to mucosal surfaces.
A

Secretory IgA

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76
Q

Monomer; mainly found in serum

A

IgA1

77
Q

Dimer held together by a J chain

A

IgA2

78
Q

predominant form in secretions at mucosal surfaces

A

IgA2

79
Q

found as a dimer along the respiratory, urogenital, and intestinal mucosa

A

IgA2

80
Q
A

IgA2

81
Q

it also appears in milk, saliva, tears, and sweat

A

IgA2

82
Q

Half-life: 2 to 3 days

A

IgD

83
Q

Most of the IgD present is found on the surface of immunocompetent but unstimulated B lymphocytes

A

IgD

84
Q

second type of immunoglobulin to appear

A

IgD

85
Q

play a role in B-cell activation (regulating B-cell maturation and differentiation)

A

IgD

86
Q

more susceptible to proteolysis than other immunoglobulins

A

IgD

87
Q

does not bind complement

A

IgD

88
Q

does not bind to neutrophils or macrophages

A

IgD

89
Q

does not cross the placenta

A

IgD

90
Q

0.0005% of total serum immunoglobulins; least abundant

A

IgE

91
Q

most heat-labile of all immunoglobulins

A

IgE

92
Q

does not participate in typical immunoglobulin reactions such as complement fixation, agglutination, or opsonization

A

IgE

93
Q

it is incapable of crossing the placenta

A

IgE

94
Q

may serve a protective role by triggering an acute inflammatory reaction that recruits neutrophils and eosinophils to the area to help destroy invading antigens that have penetrated IgA defenses

A

IgE

95
Q

Eosinophils, especially, play a major part in the destruction of large antigens such as parasitic worms that cannot be easily phagocytized

A

IgE

96
Q

150,000
900,000
160,000
180,000
190,000

A

IgG
IgM
IgA
IgD
IgE

97
Q

7S

A

IgG
IgA
IgD

98
Q

19s

A

IgM

99
Q

8S

A

IgE

100
Q

γ
μ
α
δ
ε

A

IgG
IgM
IgA
IgD
IgE

101
Q

H chain subclasses: γ1, γ 2, γ 3, γ 4

A

IgG

102
Q

H chain subclasses: None

A

IgM
IgD
IgE

103
Q

H chain subclasses: α1, α2

A

IgA

104
Q

H chain molecular weight: 50,000-60,000

A
105
Q

H chain molecular weight: 70,000

A
106
Q

H chain molecular weight: 55,000 - 60,000

A
107
Q

H chain molecular weight: 62,000

A
108
Q

H chain molecular weight: 70,000 - 75,000

A

IgG
IgM
IgA
IgD
IgE

109
Q

Constant domains (H chain): 3

A

IgG
IgA
IgD

110
Q

Constant domains (H chain): 4

A

IgM
IgE

111
Q

Percent of total immunoglobulin: 70-75

A
112
Q

Percent of total immunoglobulin: 10

A
113
Q

Percent of total immunoglobulin: 10-15

A
114
Q

Percent of total immunoglobulin: <1

A
115
Q

Percent of total immunoglobulin: 0.002

A
116
Q

Serum concentration (mg/dL): 800-1600

A
117
Q

Serum concentration (mg/dL): 120-150

A
118
Q

Serum concentration (mg/dL): 70-350

A
119
Q

Serum concentration (mg/dL): 1-3

A
120
Q

Serum concentration (mg/dL): 0.005

A
121
Q

Serum half-life (days): 23

A
122
Q

Serum half-life (days): 6

A
123
Q

Serum half-life (days): 5

A
124
Q

Serum half-life (days): 1-3

A
125
Q

Serum half-life (days): 2-3

A
126
Q

Carbohydrate content (weight percent): 2-3

A
127
Q

Carbohydrate content (weight percent): 12

A
128
Q

Carbohydrate content (weight percent): 7-11

A
129
Q

Carbohydrate content (weight percent): 9-14

A
130
Q

Carbohydrate content (weight percent): 12

A
131
Q

Electrophoretic migration: γ2–α1

A
132
Q

Electrophoretic migration: γ 1–β12

A
133
Q

Electrophoretic migration: γ2–β2

A
134
Q

Electrophoretic migration: γ1

A
135
Q

With Complement Fixation

A
136
Q

Without Complement Fixation

A
137
Q

Crosses placenta

A
138
Q

The bonding of antigen to antibody is exclusively.

A

noncovalent

139
Q

The strength of a single antigen-antibody bond (antibody affinity) is produced by the summation of the

A

attractive and repulsive forces.

140
Q

The four types of noncovalent bonds involved in antigen-antibody reactions are:

A

o hydrophobic bonds
o hydrogen bonds,
o van der Waals forces
o electrostatic forces.

141
Q

Attempts to explain the (?) of antibody for a particular antigen began long before the actual structure of immunoglobulins was discovered

A

specificity

142
Q

Ehrlich postulated that certain cells had specific surface receptors for antigen that were present before contact with antigen occurred.

A

Ehrlich’s Side-Chain Theory

143
Q

Once antigen was introduced, it would select the cell with the proper receptors, combination would take place, and then receptors would break off and enter the circulation as antibody molecules.

A

Ehrlich’s Side-Chain Theory

144
Q

New receptors would form in place of those broken off, and this process could be repeated.

A

Ehrlich’s Side-Chain Theory

145
Q

Ehrlich’s Side-Chain Theory Two key premises:

A
  1. the lock and-key concept of the fit of antibody for antigen
  2. the idea that an antigen selected cells with the built-in capacity to respond to it
146
Q

1950s- (?) independently supported the idea of a clonal selection process for antibody formation

A

Niels Jerne and Macfarlane Burnet

147
Q

Key premise- individual lymphocytes are genetically pre-programmed to produce one type of immunoglobulin and that a specific antigen finds or selects those particular cells capable of responding to it, causing them to proliferate.

A

Clonal Selection Theory

148
Q

The receptors Ehrlich originally postulated are the surface immunoglobulins IgM and IgD, found on unstimulated B lymphocytes.

A

Clonal Selection Theory

149
Q

Repeated contact with antigen would continually increase a specific lymphocyte pool.

A

Clonal Selection Theory

150
Q

Such a model provides an explanation for the kinetics of the immune response

A

Clonal Selection Theory

151
Q

Monoclonal Antibody
1975- (?) discovered a technique to produce antibody arising from a single B cell, which has revolutionized serological testing. For their pioneering research, they were awarded the Nobel Prize in 1984.

A

Georges Kohler and Cesar Milstein

152
Q

Their technique fuses an activated B cell with a myeloma cell that can be grown indefinitely in the laboratory.

A

Kohler and Milstein’s

153
Q

Myeloma cells are cancerous plasma cells.

A

Kohler and Milstein’s

154
Q

Normally, plasma cells produce antibody, so a particular cell line that is not capable of producing antibody is chosen.

A

Kohler and Milstein’s

155
Q

In addition, this cell line has a deficiency of the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT) that renders it incapable of synthesizing nucleotides from hypoxanthine and thymidine, which are needed for DNA synthesis.

A

Kohler and Milstein’s

156
Q

The greatest impact of MAbs in immunology has been on the analysis of (?).

A

cell membrane antigens

157
Q

MAbs have multiple clinical applications, including the following:

A
  1. Identifying and quantifying hormones
  2. Typing tissue and blood and delivering immunotherapy
  3. Identifying infectious agents
  4. Identifying clusters of differentiation for the classification of leukemias and lymphomas and follow-up therapy
  5. Identifying tumor antigens and autoantibodies
158
Q
  • fusion of two different types of cells
A

Hybridoma

159
Q

cancerous plasma cells

A

Myeloma cells

160
Q

Myeloma cells are deficiency of the enzyme:

A

hypoxanthine- guanine phosphoribosyl transferase (HGPRT)

161
Q

Cannot make their own DNA

A

Myeloma cells

162
Q

They will die out unless they are fused to a plasma cell

A

Myeloma cells

163
Q

HYBRIDOMA PRODUCTION
1. (?) in immunized with a certain antigen
2. (?) are harvested
3. Spleen cells are combined with myeloma cells in the presence of (?) (surfactant)
4. (?) brings about fusion of plasma cells with myeloma cells producing a hybridoma
5. After fusion, cells are placed in culture using a selective medium containing (?).
6. Myeloma cells are normally able to grow indefinitely in tissue culture, but in this case they cannot, because both pathways for the synthesis of (?) are blocked.
7. This leaves only the (?), which have the ability (acquired from the myeloma cell) to reproduce indefinitely in culture and the ability (acquired from the normal B cell) to synthesize nucleotides by the HGPRT and thymidine kinase pathway.

A

Mouse

Spleen cells

PEG

PEG

hypoxanthine, aminopterin, and thymidine (HAT)

nucleotides

fused hybridoma cells

164
Q

Culture in this medium is used to separate the hybridoma cells by allowing them to grow selectively.

A

hypoxanthine, aminopterin, and thymidine (HAT)

165
Q

One pathway, which builds DNA from degradation of old nucleic acids, is blocked, because the myeloma cell line employed is deficient in the required enzymes (?)

A

HGPRT and thymidine kinase

166
Q

The other pathway, which makes DNA from new nucleotides, is blocked by the presence of (?)

A

aminopterin

167
Q

Consequently, the (?) die out.

A

myeloma cells

168
Q

(?) cannot be maintained continuously in cell culture, so these die out as well

A

Normal B cells

169
Q

is the ability of a substance to induce an immune reaction.

A

Immunogenicity

170
Q

(?) is the ability of a substance to react with a preformed antibody or receptor.

A

antigenicity

171
Q

(?) must be somewhat complex, with an appreciable molecular weight, and must be considered foreign by the immune system.

A

Immunogens

172
Q

The relatively small area of the antigen that reacts with an antibody or receptor is called a (?).

A

hapten

173
Q

(?) are too small to be immunogens on their own right but may become immunogenic when associated with a larger molecule.

A

Haptens

174
Q

The (?) may act as haptens.

A

penicillin

175
Q

Two terms, affinity and avidity, are used to describe the strength of the (?) between antigen and antibody.

A

noncovalent, reversible interactions

176
Q

describes the strength of association between one epitope and one idiotype.

A

Affinity

177
Q

describes the strength of association between multiple binding sites such as those formed by the polyvalent IgM and its antigens.

A

Avidity

178
Q

can thus have a high avidity if multiple binding sites are engaged simultaneously.

A

A low- affinity antibody

179
Q

are compounds that nonspecifically increase the immune response to immunogens.

A

Adjuvants

180
Q

Immunoglobulins are V-shaped proteins having two identical light(L) and two identical heavy(H) chains, which are held together by (?).

A

disulfide bridges

181
Q

Both the low-molecular weight L and the high molecular-weight H chains have (?).

A

constant and variable regions

182
Q

These regions are subdivided into segments called (?).

A

domains

183
Q

L chains have (?).

A

one variable and one constant domain

184
Q

H chains have (?) and there or (?).

A

one variable

four constant domains

185
Q

The (?) are responsible for antigen binding, and the (?) are responsible for various other functions.

A

variable domains

constant chains

186
Q

Amino-acid differences in the constant region divide the L chains into either a

A

Kappa or a lambda type

187
Q

There are five immunoglobulin classes (lgG, IgM, IgA, IgE, and IgD), which are identified by differences in their

A

heavy chains

188
Q

The gamma H chain is expressed on IgG, the alpha on IgA, the mu on IgM, the epsilon in IgE, and the delta on on IgD.

A

IMMUNOLOGY AND SEROLOGY LECTURE (12 decks)

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