59-Antibody Structure and Function Flashcards

1
Q

antigen receptors

A

on surface of lymphocytes
B cell receptors
T cell receptors
many different receptors to recognize unlimited number of foreign Ags
clonically expressed-1 unique Ag receptor per lymphocyte clone

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2
Q

Surface BCR and soluble Ab molecules

A

identical except small transmembrane sequence on C terminal end

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3
Q

function of BCR

A

recognition of antigen

initiates signal transduction using CD79a/b to start intracellular signaling

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4
Q

CD79

A

needed for BCR to start intracellular signalling

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5
Q

structure of Ab

A

2 heavy chains
2 light chains
hinge region for torsion
disulfide bonds to hold molecules together
N linked carb chains linked to heavy chain for 3D structure and half life

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6
Q

variable region

A

heavy-VDJ
light-VJ
form antigen binding pocket, 2 identical pockets that bind identical antigens

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7
Q

constant region

A

no recombination, ensure structural integrity

H chain is for key effector functions

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8
Q

Fab region

A

Ag binding, 2 Fab regions=Fab2, bind 2 identical antigens

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9
Q

Fc region

A

below hinge region, heavy chain constant region

effector functions

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10
Q

Fab

A

cleave above hinge

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11
Q

Fc

A

cleave above hinge

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12
Q

Fab2

A

cleave below hinge

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13
Q

hypervariability regions

A

3 regions in both heavy and light, “complementarity determining regions”
1 and 2 and encoded in DNA
3 is recombination of VDJ or VJ

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14
Q

CDR

A

complementarity determining regions, variability in heavy and light chains
proximal in tertiary structure and form Ag binding pocket

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15
Q

epitope

A

small segment of Ag bound by Ag binding pocket, non covalent interactions

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16
Q

what can TCRs recognize vs BCR/Ag

A

TCR-peptides, require MHC

BCR/Ag-lipid, carb, protein, nucleic acid, interact with epitopes on surface of pathogens, do not require MHC

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17
Q

end product of B cell activation

A

cell that secretes Abs (soluble version of BCR) that recognize pathogen epitope and bind then recruite innate immunity to mediate destruction

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18
Q

Ab isotypes

A

defined by heavy chain constant region
5 isotopes encoded by loci
IgM, G, A, E, D

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19
Q

subclasses of Ab

A

IgG-4

IgA-2

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20
Q

IgM structure

A

4 constant regions, no hinge
large and inflexible=only in blood
secreted as pentamer-10 binding sites

21
Q

antibody that is a pentamer

A

IgM

22
Q

IgM functions

A

neutralization
agglutination
complement activation

23
Q

neutralization Abs

A

IgM, IgG, IgA

24
Q

agglutination Abs

A

IgM, IgG, IgA

25
Q

complement activation Abs

A

IgM, IgG

26
Q

IgG structure

A

3 constant regions with hinge
secreted as monomer-2 binding sites
most abundant
found in blood and tissues

27
Q

antibody that is a monomer

A

IgG, IgA in blood, IgE

28
Q

IgG functions

A
neutralization
agglutiniation
complement activation
opsonization/phagocytosis
Ab dependent cellular cytotoxicity
transplacental transfer
29
Q

opsonization/phagocytosis Abs

A

IgG, IgA

30
Q

Ab dependent cellular cytotoxicity Abs

A

IgG

31
Q

passive immunity to fetus through placenta Abs

A

IgG

32
Q

IgA structure

A

3 constant regions with hinge
monomer in blood
dimer in mucosal secretions

33
Q

antibody that is a dimer

A

IgA in mucosal secretions

34
Q

IgA functions

A

neutralization
agglutination
opsonization/phagocytosis
immunity in breast milk

35
Q

immunity in breast milk Abs

A

IgA

36
Q

IgE structure

A

4 constant regions, no hinge region

monomer

37
Q

IgE function

A

bound to mast cells with high affinity

mediate type 1 hypersensitivity reaction/ allergic reaction

38
Q

allergic reaction Abs

A

IgE

39
Q

IgD structure

A

3 constant regions with hinge, rarely secretes, used as BCR on naive B cells

40
Q

no hinge

A

IgM, IgE

41
Q

agglutination

A

traps microbes in a complex
impair movement, attachment, replication, colony formation
IgM, G, A- lots of binding sites or hinge with torsion

42
Q

neutralization

A

prevent pathogens and toxins from binding to their host

IgM, G, A

43
Q

Complement activation-Classical pathway

A

Ab binding to Ag makes immune complex formation
allosteric change in Fc to bind C1q to start complement cascade, Use IgM, G

recruit C4 and 2, activation of C3 convertase
cleave C3, C3a inflammation, C3b opsinization
recruit and cleave C5, C5a inflammation
C5b recruits C6, 7, 8, 9 to form MAC, create channel and lyse

44
Q

Opsonization

A

coating of pathogen with ligand recognized by phagocytic cells
IgG, IgA, C3b

45
Q

Phagocytic cell receptors

A

Fc receptor bind antibodies
C3b receptor bind C3b
4 IgG Fc receptors, 1 IgA Fc receptor, 4 C3b receptor

46
Q

natural killer cells

A

IgG Fc receptors bind IgG Abs with their Fc tail
provide specifficity to NK cells to recognize and bind Ags on target cells
kill using proteolytic enzymes and inducing apoptosis

47
Q

maternal IgG

A

to fetus through circulation
can cause disease
hemolytic disease of newborns
IgG aBs against Rh blood group, give RhoGAM to Rh- moms

48
Q

maternal IgA

A

in mothers milk

protect baby’s gut