B cells: antibodies Flashcards

1
Q

Structure of ab = shape

A

Y shaped glycoprotein
- contains carb covalently linked to protein

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2
Q

Ab aka

A

Immunoglobulin (ig)

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3
Q

Describe immunoglobulin

A

Protein fam to which abs and B cell receptors belong - these are ig like domains

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4
Q

What are abs made up of

A

2 identical disulfide linked heavy chains and 2 identical light chains
4 chains in total

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5
Q

Describe variable region

A

Both heavy and light chain have a variable region

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6
Q

Describe constant region

A

Both heavy and light chain have a constant region

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7
Q

Name all regions of ab

A

Vl = variable region in lc
Vh = variable region in hc
Cl = constant region in lc
Ch = constant region in hc

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8
Q

Variable region functions

A

Ag binding
Vl and vh = forms antigen binding site= 2 identical sites per ab
Binding can result in neutralization and other fucntions

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9
Q

Constant region functions

A

Involved in complement activation - c1q—> classical pathway
= binding ag —> cascade classical pathway
Constant region fc binding fc receptors

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10
Q

What else can constant region do - explain more

A

Constant region fc binding fc receptors On phagocytes and other cell types like mast cells, eosinophils
= fc receptors Bind fc region = can lead to phagocytosis, or secretion of histamine/granulocytes

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11
Q

Describe fab fragments

A

2 fab fragments per ab
Each has ag binding domain and part of Constant heavy and light chains

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12
Q

Describe fc fragment

A

One fragment
Constant region heavy chain
Receptors that bind abs recognize fc portion

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13
Q

Fab =

A

Fragment antigen binding

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14
Q

Fc =

A

Fragment crystallizable

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15
Q

Describe 3d structure ab - bonds/what’s it look like

A

Held together by inter/intra chain disulfide covalent bonds - keeps everything together
Both constant and variable regions folded in complex 3d structure including beta strands

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16
Q

Describe variable region - complementarity determining region

A

Cdr = ag binding site, has direct contact with ag
Hyper variable loops -3per variable do domain (2hc/lc = 6x2 cdrs = 12 cdrs per ab)
Not part of beta stands

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17
Q

What do cdrs have

A

Greatest variability in ab sequence = highly variable

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18
Q

Where are cdrs

A

At extremities of ab
At ends of abs = direct binds ag

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19
Q

Describe ag binding to ig

A

Ag binding to ab = involves non covalent bonding between ig and ag epitope
Uses other types of interactions

20
Q

What types of interactions involved when. Ag binds ig - name some

A

Hydrogen bonds
Van der waals
Hydrophobic ionic

21
Q

Describe antibody:antigen binding - specificity

A

Lock and key specificity

22
Q

Describe antibody:antigen binding - Where is it

A

Extremities of abs

23
Q

Describe antibody:antigen binding - Is there a size restriction for ag

A

Size variability of what’s being recognized by ab

24
Q

Describe antibody:antigen binding - Are cdrs the same length

A

Variantion in ab = cdrs vary in length

25
Describe antibody:antigen binding - Location of epitopes
Can be anywhere on ag
26
Antibody classes
5 major classes Diff number of ig like domain, diff lengths of constant region of heavy chain Diff carb groups
27
What differentiates the 5 major classes of abs
By aa sequence of heavy chain constant region = heavy chain differentiates diff abs Fc fragment of each ig = diff
28
Do all antibody classes do same things
Noooo Each class does diff fucntions during immune response
29
Describe igm structure
Pentameric - 5 igms linked 5 abs linked together via disulphide bonds Heavy chain = one variable region and 4 constant regions
30
Describe igm - expressed on
Mature naive B cells express transmembrane igm prior to activation
31
Describe igm functions
Part of first wave of secreted abs - plasma blasts Most effect initiator of complement cascade
32
Why is igm good at initiating complement
Binds c1q = makes good landing pad bc of igm size
33
Describe igd structure
Heavy chain = one variable region and 3 constant regions - so shorter
34
Describe igd functions
Part of first wave of secreted abs = some secreted only
35
Describe igg structure
Heavy chain = one variable region and 3 constant regions
36
Describe igg fucntion
Most abundant in plasma 2 subclasses in humans = igg1,2,3,4 Produced following differentiation in germinal centre = bc class switching only happens here
37
Describe ige structure
Heavy chain = one variable region and 4 constant regions
38
Describe ige fucntion
Produced in response to helminth infection - th2 response
39
Describe iga structure
Heavy chain = one variable region and 3 constant regions Monomer in plasma Dimmer in mucous secretions through j chain (majority, j chain = polypeptide linking disulfide bonds)
40
Describe iga functions
Important for mucosal immunity 2 subclasses = iga1, iga2
41
Describe experimental and clinical uses of abs - what can abs be made to bind
Can be made to bind virtually any epitope Can be made to bind another ab
42
Describe experimental and clinical uses of abs - ex of ab binding any epitope
antibody against TNF- for the treatment of rheumatoid arthritis
43
Describe experimental and clinical uses of abs - ex of ab binding to another ab
an antibody against the Fc region of IgG
44
Describe Elisa
Enzyme linked immunosorbent assay = if want to know how much of a protein in sample Primary ab specific to target and secondary ab specific to fc region primary ab and conjugated with colour More intense the colour = means more fo protein fo interest
45
Describe western blot
Intensity of band = how much Size = see if bound to something 2nd and conjugated so can see band
46
Describe immunogenicity - note
Possible for immune system to mount an immune system response against therapeutic drug - including mabs Slowly mimic human ab and decrease immunogenicity of it - to make as similar to human ag but prevent immune response