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Immunology > Lecture 3 Slides > Flashcards

Lecture 3 Slides Flashcards

0
Q

Antigen

A

Any substance that reacts with T or B lymphocytes

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1
Q

Immunogen

A

Substances that generate immune response

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2
Q

Simple to macromolecules

A

Carbohydrates, phospholipids, nucleic acids and proteins

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3
Q

Immunologic properties of antigens (Ag)

A

Immunogenicity
Antigenicity
Allerogenicity
Tolerogenicity

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4
Q

Is immunogenic same as antigenic

A

Yes, but antigenic does not equal immunogenic

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5
Q

Types of antigens

A

Alloantigen

Mitogen

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6
Q

Alloantigen

A

Antigen determinants found on a molecular structure of some members of the species, but not on the corresponding molecular structure of other members of the species. Inherited as simple Mendelian traits. Are usually detected when one member of a species is immunized with a molecule from member of same species

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7
Q

Mitogens

A

Polyclonal activator, e.g., PHA, ConA, LPs

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8
Q

Superantigen

A

Among the most potent t-cell mitogens known

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9
Q

What do super antigens bind to?

A

Residues in the variable domain of the T-cell receptor and to residues in class II MHC molecules outside of the antigen-binding cleft

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10
Q

What can super antigens cross link a t-cell to?

A

A class II MHC molecule even when the TCR does not recognize the bound antigenic peptide, leading to activation of the T-cell.

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11
Q

How does a super antigen activate all t-cells?

A

Expressing the V domain to which that super antigen binds

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12
Q

Common super antigens include

A

Staphylococcal enterotoxemia (Ses) and toxic shock syndrome toxin 1 (TSST1)

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13
Q

Hapten

A

Type of antigen
Small molecules which could never induce an immune response unless coupled to a carrier molecule (foreign protein) e.g. Dinitrophenyl, amino benzene sulphonate, arsonate

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14
Q

Haptein

A

Carrier molecule, unlike free haptein, can act as an immunogen

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15
Q

Hapten-carrier conjugate

A

Carrier and hapten combined

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16
Q

When hapten-carrier conjugate side to immunize rabbit, rabbit creates antibodies to

A

Hapten and carrier and conjugate of hapten and carrier

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17
Q

What antibodies form when one is injected with hapten

A

None

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18
Q

What antibodies form when one is injected with protein carrier (BSA)

A

Anti-BSA

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19
Q

What antibodies form when one is injected with hapten-carrier conjugate

A

Anti-DMP (major)
Anti-BSA (minor)
Anti-DNP/BSA (minor)

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20
Q

What do adjuvants do

A

Enhance immune response

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21
Q

Freund’s incomplete adjuvant

A

Prolongs antigen persistence
Enhances costimulatory signal
Induces granulosa formation

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22
Q

Freund’s complete adjuvant

A

Prolongs antigen persistence
+Enhances costimulatory signal
+Induces granulosa formation

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23
Q

Insoluble aluminum slats

A

Prolongs antigen persistence

Induces granulosa formation

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24
Q

Mycobacterium tuberculosis

A

Induces granuloma formation

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25
Q

Bordetella pertussis

A

Stimulates lymphocytes nonspecifically

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26
Q

Bacterial lypopolysaccaride (LPS)

A

Enhances costimulatory signal

Stimulates lymphocytes nonspecifically

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27
Q

Synthetic polynucleotides (poly IC/poly AU)

A

Stimulates lymphocytes nonspecifically

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28
Q

What factors of immunogenic influence immunogenicity

A

Immunogenic foreignness
Size
Chemical composition
Physical form (particulate>soluble; denatured>native;degradability Ag processing by Ag presenting cells)

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29
Q

What are biological contributions to immunogenicity

A

System genetics
Species
Individual responders vs non-responders
Age

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30
Q

How does method of admission contribute to immunogenicity

A

Dose
Route. Subcutaneous>intravenous>intra gastric
Adjuvant substances that enhance an immune response to an Ag

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31
Q

Epitope

A

Small,site on antigen which is recognized by antibody

Usually between one and six sugars or amino acids on the surface of the antigen

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32
Q

Antigenic determinant

A

Cluster of epitopes on the surface of an antigen

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33
Q

How many determinants does antigen have? Are they different?

A

Several and they are structurally different from each other

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34
Q

What does a monoclonal antibody react with

A

Only one determinant on the same antigen

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35
Q

What does antigenic determinant bind

A

Receptors on T cells or antibodies (B cells)

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36
Q

How does B cell interact with antigen? T cell?

A

B cell - involves binary complex of membrane Ig and Ag

T cell - involves ternary complex of T cell receptor, Ag, and MHC molecule

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37
Q

Do B cells and T cells bind with soluble antigen?

A

B cells - yes

T-cells - no

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38
Q

How are B cells and T cells involved with MHC molecules

A

B-cells - non requires

t-cells- required to display processed antigen

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39
Q

Chemical nature of antigens that react with B cells and T cells

A

B cells - protein, polysaccharide, lipid

T cells - mostly proteins, but some lipids and glycolipids presented on MHC-like molecules

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40
Q

Epitope properties recognized by B cells and T cells

A

B cells - accessible, hydrophobic, mobile peptides, containing sequential or no sequential amino acids
t-cells - internal linear peptides produced by processing of antigen and bound to MHC molecules

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41
Q

Antibodies

A

Immune-system related proteins that bind antigen

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42
Q

Where are antibodies present

A

On B cell membrane or secreted by plasma B cells

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43
Q

What do membrane bound antibodies confer

A

Antigen specificity

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44
Q

What do secreted antibodies serve as

A

The effector of the humoral immunity

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45
Q

Where are antibodies found

A

Electrophoresis separates plasma proteins into albumin and globulin. most antibodies are found in the gamma globulin fraction

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46
Q

Immunoglobulin

A

Ig
Proteins of molecular weight 150,000 - 900,00 Kd
Unique molecules, derived from immunoglobulin super gene

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47
Q

How does Ig bind

A

One end of Ig binds to antigens (the Fab portion) and other end is responsible for effector functions

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48
Q

fab portion of Ig

A

So called because it is the fragment of the molecule which is antigen binding

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49
Q

Fc portion of Ig

A

Crystallizable

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50
Q

Immunoglobulins are composed of

A

Two H chains and two L chains. They are heterodimers.

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51
Q

Where are disulfide bonds in IgG

A

Between heavy chains and bet, each heavy and light chain

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52
Q

What is variable region

A

Includes ends of light and heavy chains
Composed of 100-110 aa, give antibody it’s specificity for binding antigen
Fab or fragment antigen binding that include in the variable ends of an antibody

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53
Q

What is variable region further subdivided into

A

Hyper variable (HV) and framework (FR) regions

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54
Q

Hyper variable regions

A

Have a high ratio of different aa in a given position, relative to the most common amino acid in that position

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55
Q

Constant region

A 
Does not contain antigen binding domain
Sequence in constant region of the light chain are either lambda or kappa
There are five different sequences in heavy chain constant region and they determine the class or isotype of the antibody.
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56
Q

Hinge region

A

Constant region of light chain has one domain of homology
CH has homology domains (CH1, CH2 and CH3)
Extended peptides are found between CH1 and CH2 called hinge region
Make antibody more flexible
Found only in IgG, IGA, and IgD (3 CH)
IgM and IgE have no hinge but 4 CH

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57
Q

Where is hinge region found?

A

IgG, IgA, and IgD

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58
Q

What is subunit structure of immunoglobulin

A

4 polypeptide chains
2 heavy chains
2 light chains
Form a Y shaped unit

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59
Q

What bridges the two heavy chains

A

Interchain SS bond

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60
Q

How are light chains linked to heavy chains

A

Interchain SS bonds

61
Q

What two regions do heavy chains have

A

Amino acid homology constant region (CH)

Regions with variation in sequence (VH)

62
Q

CL chains of Ig are either

A

Kappa or lambda

63
Q

Regions of constant sequence homology are

A

CLkappa or CL lambda

64
Q

Regions of variable sequence homology are

A

VLkappa or VLlambda

65
Q

What does each CL or VL region have

A

Intrachain S-S bond

66
Q

What are H and L chains folded into

A

Globular domains

67
Q

What is different between IgG, IGA and IgD and IgE and IgM

A

First have hinge region. Second don’t.

First don’t have extra domain. Latter do.

68
Q

Primary structure

A

Accounts for variable and constant regions (domains) of the heavy and light chains
Amino acid sequence of polypeptide chain

69
Q

Secondary structure

A

Folding into antiparallel Beta sheets that are stabilized by hydrogen bonds

70
Q

Tertiary structure

A

Globular domains connected by polypeptide chains and stabilized by hydrophobic interactions and the disulfide bonds

71
Q

Quaternary structure

A

Globular domains of adjacent heavy and light chains interact forming the functional Ig molecule

No covalent bonding

72
Q

Is there covalent bonding in quaternary structure

A

No

73
Q

Two roles of immunoglobulin

A

Antigen receptor

Effector molecule

74
Q

Role of antigen receptor

A
  • recognition of and binding to antigens such as toxins, viruses, and exposed molecules on the surface of pathogenic organisms
  • V domain function
75
Q

Role of effector molecule

A

Elimination or inactivation of the foreign antigen or the cell that bears the antigen
C domain function

76
Q

Where are antibodies made

A

T cells release cytokines that make B lymphocytes evolve into plasma cells
Plasma cells secrete antibodies in greater amounts, but do not divide

77
Q

Where do plasma cells exist

A

In lymphoid tissues, not blood.

78
Q

Where do memory cells from B cells circulate

A

In blood?

79
Q

CDR

A

Complementarity determining region
-is the Ag binding site
Hyper variable region is not conserved

80
Q

What causes wide range of CDR specificities

A

Variation in length and sequence of the CDRs in each Fab fragment

81
Q

Antigenic determinants

A

Epitopes on antigen. Antibodies recognize and react with epitopes.

82
Q

Can immunoglobulins be immunogens

A

Yes

83
Q

Three antigenic determinants of immunoglobulin

A

Isotypic, allotypic, and idiotypic

84
Q

Isotopic determinants

A

Constant region determinants that distinguish Ig class and subclass within a species

85
Q

Allotypic determinants

A

Subtle amino acid differences encoded by different alleles of isotype genes. Can be detected by comparing the same antibody class among different inbred strains.

86
Q

Idiotypic determinants

A

Generated by conformation of amino acid sequences of heavy and light chain variable region specific for each antigen

87
Q

What is each idiotypic determinant called

A

Idiotope. Sum of individuals idiotopes is idiotype.

88
Q

Difference between primary and secondary responses

A

Primary is slow in onset, low in magnitude, shirt lived, and IgM
Secondary is rapid on onset, high in magnitude, long lived, IgG (or IgA or IgE)

89
Q

What does B cell do when it encounters its matching antigen

A

It is triggered. It engulfs the antigen and digests it. Then it displays antigen fragments bound to its unique MHC molecules.

90
Q

What do combination of MHC and antigen attract?

A

The help of a mature matching T cell

91
Q

What does T cell secrete

A

Cytokines that help the B cell to multiply and mature into antibody producing plasma cells

92
Q

What do antibodies do once they’ve been secreted?

A

They are released into the blood. They lock onto matching antigens. The antigen-antibody complexes are then cleared by the complement cascade or by the liver or the spleen

93
Q

Heavy chain, no. Of Ch Ig domains, subclasses, light chain, J chain, molecular formula:
IgG

A 
Gamma H
3CH
Human, gamma 1,2,3,4
L kappa or lambda
No J
Gamma2kappa2
94
Q

Heavy chain, GH Ig domains, subclasses, light chain, J chain, molecular formula:
IgM

A 
Mu H
4 CH
None
Kappa or lambda L
Yes J
Gamma2lambda2
95
Q

Heavy chain, GH Ig domains, subclasses, light chain, J chain, molecular formula:
IgA

A 
Alpha H
3
Alpha 1 and 2
K or lambda L
Yes J
(a2k2)n or (a2lamvda2)n n=1,2,3,4
96
Q

Heavy chain, GH Ig domains, subclasses, light chain, J chain, molecular formula:
IgE

A 
Epsilon
Four
None
Kappa or lambda
None
E2k2
97
Q

Heavy chain, GH Ig domains, subclasses, light chain, J chain, molecular formula:
IgD

A 
Delta
Three
None
Kappa or lambda
None
Delta2kappa2 or delta2lambda2
98
Q

Classes of immunoglobulins

A 
IgG
IgM
IgD
IgE
IgA
99
Q

What is the IgG structure

A

Monomer

100
Q

Percentage IgG serum antibodies

A

80%

101
Q

Location of IgG

A

Blood, lymph, intestine

102
Q

Half life IgG serum

A

23 days

103
Q

IgG complement fixation

A

Yes

104
Q

IgG placental transfer

A

Yes

105
Q

IgG known functions 3

A

Enhances phagocytosis
Neutralizes toxins and viruses
Protects fetus and newborn

106
Q

IgM structure

A

Pentamer

107
Q

IgM percentage serum antibodies

A

5-10%

108
Q

IgM location

A

Blood, lymph, B cell surface (monomer)

109
Q

IgM half life in serum

A

5 days

110
Q

IgM complement fixation

A

Yes

111
Q

IgM placental transfer

A

No

112
Q

Known functions of IgM 2

A

First antibodies produced during an infection

Effective against microbes and agglutination antigens

113
Q

IgD structure

A

Monomer

114
Q

IgD percentage serum antibodies

A

0.2%

115
Q

IgD location

A

B cell surface, blood, and lymoh

116
Q

IgD half life in serum

A

3 days

117
Q

IgD complement fixation

A

No

118
Q

IgD placenta transfer

A

No

119
Q

IgD known functions

A

Function unknown in serum

On B cell surface, initiate immune response

120
Q

IgE structure

A

Monomer

121
Q

IgE percentage serum antibodies

A

0.002%

122
Q

IgE location

A

Bound to mast cells and basophils throughout body. Blood

123
Q

IgE half life in serum

A

2 days

124
Q

IgE complement fixation

A

No

125
Q

IgE placenta transfer

A

No

126
Q

Known functions of IgE

A

Allergic reactions. Possibly lysis of worms

127
Q

IgA structure

A

Dimer

128
Q

IgA placental transfer

A

No

129
Q

IgA known functions

A

Localized protection of mucosal surfaces

Provides immunity to infant digestive tract

130
Q

IgA percentage serum antibodies

A

10-15%

131
Q

IgA location

A

Secretions (tears, saliva, intestine, milk) blood and lymph

132
Q

IgA half life in serum

A

6 days

133
Q

IgA complement fixation

A

No

134
Q

Where is J chain of secretory IgA

A

Right in middle of dimer.

135
Q

How is secretory IgA formed

A

Plasma cell in su mucosa
Secretes dimeric IgA
Dimeric IgA binds with poly-Ig receptor on epithelial cell
Travels in vesicle to other side of cell
Secreted by cell into lumen via enzymatic cleavage

136
Q

Functional properties of Ig

A 
Agglutination
Opsonized ion
Phagocytosis facilitation
Neutralization 
Immobilization of bacteria
Complement activation
Mucosal protection
137
Q

Agglutination

A

When antigen is mixed with its corresponding antibody. IgM particularly suitable for this.

138
Q

Opsonizatiom

A

Coating of bacteria for which the anti body’s Fab region has specificity (esp IgG)

139
Q

Phagocytosis facilitation

A

Cells possess Fc receptor, eg, neutrophil Polymorphonuclear Leukocytes (Polymorphs). Both the Fab and Fc portions of the immunoglobulin molecule are involved.

140
Q

Neutralization

A

Of toxins and blocking attachment. This applies particularly to IgG. Here, only Fab is involved

141
Q

Immobilization of bacteria

A

Antibodies against bacterial ciliate or flagellate eill hinder bacteria movement /ability to escape phagocytic cells. Only Fab is involved.

142
Q

Complement activation

A

(Classical pathway) especially by Fc region of IgM and IgG, leads to bacteria death by MAC; complement components also facilitate phagocytosis by cells possessing a receptor for C3b, eg, Polymorphs

143
Q

Mucosal protection

A

Provided mainly by IgA and to lesser degree IgM. IgA acts chiefly by inhibiting pathogens from gaining attachment to mucosal surfaces. This is a Fab function.

144
Q

Polyclonal antibody

A

A population of antibodies against one antigen, but against multiple epitopes of that antigen.

145
Q

Monoclonal antibody

A

An antibody which is directed against one epitope of one antigen

146
Q

Plasmacytomas

A

Cancer of a single colon of plasma cell, the end stage of B cell differentiation normally located in bone marrow

147
Q

Myeloma

A

Plasmacytomas once it metastasizes into multiple bone marrow sites

148
Q

Plasmacytomas tumor arises from

A

A single antibody producing cell, therefore the tumor produces a large amount of a single kind of Ig-myeloma protein

149
Q

Bence-Jones Protein

A

Patients with multiple myeloma excrete BJ proteins in the urine. It is a homogenous light chain of one or two classes of L chains (kappa or lambda)

150
Q

How are polyclonal antibodies different from monoclonal antibodies?

A
  • p antibodies recognize multiple epitopes, making rhem more tolerant of small changes in nature of antigen
  • p antibodies target multiple epitopes, so they provide more robust detection
  • monoclonal antibodies react with one epitope on antigen so are more specific
  • reproducible results???

Immunology (5 decks)

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