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Immunology > Lecture 6- Immunoglobulins > Flashcards

Lecture 6- Immunoglobulins Flashcards

(52 cards)

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1
Q

Describe the structure of an antibody

A

Y shaped, joined by disulfide bonds, 2 light chains, 2 heavy chains, variable and constant region, FAB and FC region

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2
Q

What two basic amino acid sequences encode the light chain constant region

A

Kappa and lambda

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3
Q

Do B cell antibodies produce both kappa and lamdba

A

Never, just 1

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4
Q

How are B cell lymphomas marked

A

Increase in frequency in 1 type of light chain

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5
Q

FAB

A

Fragment antigen binding site, smaller, readily penetrate deep into tissues, can’t generate immune response but can neutralize

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6
Q

CroFab

A

Only approved antivenin in US

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7
Q

FC

A

Fragment crystallization

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8
Q

Where does proteolytic cleavage by papain occur

A

Above disulfide bond so end up with 2 FAB regions and 1 FC

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9
Q

Where does proteolytic cleavage by pepsin occur

A

Below the disulfide bone so you get 1 FAB region (F’ab)2 and one FC region (pfc’)

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10
Q

How does variation occur in binding sites

A

Heavy and light chain recombinations and how they interact with each other leads to additional specificity

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11
Q

What region of antibody determines class and function

A

Constant region

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12
Q

What are the 5 classes of antibodies

A

IgM, IgD, IgG, IgA, and IgE

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13
Q

What Ig’s are important for neutralization

A

IgG and IgA

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14
Q

What Ig’s are important for opsonization

A

IgG

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15
Q

What Ig’s are important for sensitization for killing by NK cells

A

IgG

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16
Q

What Ig’s have sensitization of mast cells

A

IgE

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17
Q

What Ig’s have sensitization of basophils

A

IgD and IgE

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18
Q

What Ig’s activate complement

A

IgG and IgM (better)

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19
Q

What Ig transport across epithelium

A

IgA

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20
Q

What Ig transports across placenta

A

IgG

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21
Q

What are the two subtle differences in antibody structure

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A

Location of disulfide bonds and different carbohydrates linked to the antibody

22
Q

What is IgM

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A

1st class of antibodies produced by B cells after activation, secreted as a pentamer so can’t penetrate tissues, J-chain promotes polymerization, binds with C1 to activate complement

23
Q

What is IgG

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A

Most abundant class of antibody, found in blood and tissues, interacts with C1 to activate complement, crosses placenta, 20 day half life

24
Q

How does IgG achieve 20 day half life and why is it important

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A

IgG is pinocytoses from plasma and binds to FcRN (neonatal receptors) within endosomes. Once bound IgG-FcRN complex directs endosome away from lysosomes, fuses with cell membrane and releasing IgG back into circulation

25
Monomeric IgA
Found in blood stream, engage in neutralization, BCR on memory B cells
26
IgA1
Activates alternative pathway, mostly found in serum
27
IgA2
Does not activate complement, most found in secretions
28
What do both isotypes of IgA do
Bind Fc receptors on phagocytic cells- initiate phagocytosis and respiratory burst
29
Secretory IgA
Found at mucosal surfaces- secreted across epithelium into breastmilk, tears, saliva, gut and respiratory mucosa Neutralize antibodies
30
Selective IgA deficiency
Loss of IgA production, leads to increased risk of infections at mucosal surfaces
31
IgE
Binds with high affinity to mast cells and basophils, important in fighting parasites and allergic reactions- triggers release of histamine and interleukins
32
IgD
Signals for B cell activation, enhances mucosal immunity
33
IgY
Found in birds, reptiles and lungfish
34
Where is IgM found
Blood
35
Where is IgG found
Blood, extracellular fluid, tissues
36
where is IgA found
Secretions across epithelia like breastmilk
37
Where is IgE found
Associated with mast cells so right beneath the skin
38
What are the 6 antibody functions
1. B cell activation 2. Neutralization 3. Optimization 4. Complement activation 5. Antibody dependent cellular toxicity 6. Mast cell and basophil activation
39
What is B cell activation
BCR bound to CD79A and CD79B, enough binding of BCR’s will activate B cells T cell independent, doesn’t generate memory cells
40
Neutralization
Virus binds to receptor on cell surface and receptor endocarditis virus and it starts releasing viral DNA To prevent things antibody blocks binding to virus receptor and can also block fusion by binding to virus
41
Opsonization
Bacterium is coated with complement and IgG antibody, C3b binds to CR1 and antibody binds to Fc receptor and bacteria are phagocytosed. Macrophage membranes fuse created enclosed vesicle, the phagocyte. Lysosome fuses and degrades bacteria.
42
Fc receptor free antibody vs aggregation of antibodies
Free antibody does not cross link Fc receptors, binding to an aggregation of antibodies like those on bacterial surfaces activates the macrophage leading to phagocytosis
43
Complement activation with IgG and IgM
Both activate C1 in the classical pathway
44
Why is IgM more efficient in complement than IgG
IgM is more efficient because C1 can bind 1 IgM but in IgG it must bind at least 2.
45
Antibody dependent cell mediated cytotoxicity (ADCC)
Antibody binds antigen on surface of target cells, FC receptors on NK cells recognize bound antibody, cross linking FC receptors signals NK cell to kill target cell via toxic granules, results in apoptosis
46
Mast cells and basophils
Involved in mobilizing cells to site of infection, releasing histamine Bind IgE and IgG IgE binds and causes release of cellular contents, increases blood flow and vascular permeability, recruits neutrophils, macrophages, eosinophils, and antigen specific lymphocytes, increases lymph flow
47
What is the main Ig involved in primary immune response
IgM
48
What Ig’s are involved in complement activation
IgG and IgMw
49
What Ig’s are involved in neutralization
IgG, IgA, IgM
50
What Ig’s are involved in opsonization
IgG, IgA
51
What Ig’s are involved in ADCC-NK cells
IgG
52
What Ig’s are involved in degranulation of mast cells and basophils
IgE

Immunology (22 decks)

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