lecture 6- antibodies and antigens Flashcards

1
Q

what group of globulins are most Abs found

A

gamma globulins

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2
Q

how are the chains of Abs held together

A

covalent disulfide bridges as well as by non covalent interactions

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3
Q

what is the difference between the V and C regions

A

V regions contain the Ag-binding site and C region determines the fate of the Ag

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4
Q

how does the heavy chain C region of secreted IgG end

A

in tail pieces

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5
Q

what anchors the molecule in the plasma membrane for membrane bound IgM on B cells

A

a C-terminal transmembrane and cytoplasmic portions

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6
Q

what does papain digestion of IgG allow

A

separation of 2 Fab fragments and complement- and Fc receptors-biding the Fc fragment

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7
Q

what does proteolysis of IgG by pepsin generate

A

a single bivalent antigen-binding fragment

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8
Q

define affinity

A

tightness of Ag-Ab binding

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9
Q

define valence of an Ab

A

the maximum number of antigenic determinants with which it can react

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10
Q

how many Fab regions does IgG have

A

2 Fab regions

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11
Q

what does avidity depend on

A

affinity of the Ab for the epitope and the valence of both the Ab and Ag

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12
Q

what happens to the functional antigen recognition and effector functions when there is an affinity maturation (somatic mutations in variable region) of the antibody structure

A

functional: increased affinity; effector: no change

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13
Q

what happens to the functional antigen recognition and effector functions when there is a change from membrane to secreted form of an antibody

A

no change in functional antigen recognition and effector function change: change from B cell receptor function to effector function

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14
Q

what happens to the functional antigen recognition and effector functions when there is isotype switching in Abs

A

no change in functional antigen recognition but the effector function changes because each isotype serves a different set of effector functions

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15
Q

what are the proliferation cytokines

A

IL-2, IL-4, IL-5

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16
Q

what are the differentiation cytokines

A

IL-2, IL-4, IL-5, TNF-gamma, TGF-beta

17
Q

where is IgA most common

A

mucosal secretions

18
Q

where is IgM mainly found

A

plasma

19
Q

where is IgE absorbed

A

surface of fast cells

20
Q

what is the molecular weight of IgM, IgD, IgG, IgA, and IgE, respecitively

A

970, 184, 150, 160, 188

21
Q

what is the most abundant Ig in the blood

A

IgG

22
Q

what provides the bulk of immunity to most bloodborne pathogens

A

IgG

23
Q

what Igs can Naive B cells express

A

both IgM and IgD and both are specific for the same Ag

24
Q

what is the primary function of IgD

A

Ag receptor on B lymphocytes, but is probably also involved in regulating B cell function when it encounters Ag

25
Q

what is blood IgM composed of

A

five 4-chain units held together by disulfide bridges

26
Q

what initiates the polymerization of the subunits during secretion from a plasma cell (IgM)

A

J-chain of IgM

27
Q

describe Sc

A

part of the poly-Ig receptor involved in the transepithelial transport of exocrine IgA and stabilizes IgA against proteolytic degradation in the GI tract