Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Immunology > Lecture 3 > Flashcards

Lecture 3 Flashcards

1
Q

What carries out the adaptive immune system?

A

B and T lymphocytes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Describe the structure of antibody (BCR)?

A
  • 2 identical heavy chains (50 kDa)
  • 2 identical light chains (25 kDa)
  • bivalent
  • heavy and light chains held together by interchain disulfide bonds
  • secreted and membrane bound forms
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the hinge region?

A

-allows antibody to bind with both arms to many different arrangements of antigens on the surfaces of pathogens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Describe th eFab fragment?

A

fragment antigen binding; 2 identical fragments that bind antigen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the Fc fragment?

A

fragment crystallizable; 1 fragment responsible for destroying or clearing antigen from our bodies (effector function)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What bond forms intrachain immunoglobulin domains?

A

disulfide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Are all antibodies proteins with constant region?

A

no, they have variable and constant regions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what forms the antigen binding site?

A

variable heavy and constant light region

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is an epitope?

A

the region of the protein or bacteria that binds to the antibody

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Difference between monoclonal and polyclonal epitope?

A

monoclonal- antibody that only binds to one epitope

polyclonal- antibody that can bind to many sites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What does bivalent mean?

A

two binding sites on binding site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is an antigenic determinant?

A

region that antibody contacts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the difference between continuous and conformational epitopes?

A

continuous binds linearly and it is between amino acids

conformational- binds at different parts of the protein; usually occurs in tertiary structures that are denaturing

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are possible bonds between antigen and antibody?

A

noncovalent

  • hydrogen
  • van der waal
  • electrostatic interaction
  • hydrophobic forces
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is avidity?

A

The sum of affinity present

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Wht is affinity?

A

the strength of binding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is cross reactivity?

A

The ability for an antibody to bid to multiple epitopes

18
Q

What is somatic recombination?

A

allows for increase diversity of antibodies

19
Q

What are the kappa and lambda components of an antibody?

A

aprt of the light chain

  • have no functional difference
  • each antibody contains both of them
20
Q

What makes up each domain in antibody?

A

2 beta sheets connected by polypeptide loops

21
Q

Why is CDR3 so important in gene diversity?

A

It is where all the VDJ segments join forms a lot of gene diversity

22
Q

What segment is in the heavy chain but not in the light chain?

A

Segment

D

23
Q

What is different between Chain rearrangement in the Heavy and the light?

A

Light chain uses only V and J segments

rearragnes DNA/ DNA is loss….trasncription… RNA splicing

Heavy uses V D and J segments

  1. ) DJ segements join
  2. )V-DJ joining
  3. ) transcription
  4. ) alternative mRNA splicing that forms two products (mu and delta)
  5. ) translation
24
Q

What are recombination signal sequences? (RSSs)

A

recombination signal sequence that flank each V/d/J gene segment

12/23 rule

25
Q

What is the RAG complex?

A

recombinase composed 2 RAG1 and 2 RAG2 proteins, has endonuclease activity

26
Q

What is Junctional Diversity?

A

random incorporation of nucleotides at coding joints

27
Q

What are P nucelotides?

A

‘Palandromic”- consequence of RAG endonuclease action which create DNA hairpins. When repaired , the nick that opens the hairpin cna occur at several positions-> P nucelotides

28
Q

What are N nucleotides?

A

“non template’ consequence of termina ldeoxynucleotidyl transferase (TdT). This enzyme adds nucelotides to the opened hairpin ends

29
Q

What are diversifications of antibodies after B cells encounter antigen?

A
  • secreted antibodies
  • somatic hypermutation/ affinity maturation
  • class switching: mechanism and significance
30
Q

What class of antibodies are found on the membrane of B cell surface?

A

IgM and IgD

31
Q

What allows plasma cells to to produce secreted antibody?

A

alternative RNA processing

32
Q

What stabilizes the receptor of the membrane for the transmembrane antibody?

A

the hydrophobic region which is changed into a hydrophilic region to allow for secretion

33
Q

What are somatic hypermutations?

A

Targeted introduction of point mutations into V regions of H and L chains

  • leads to increased antibody affintiy
  • carried out by Activation Cytidine Deaminase (AID) and and deaminates C–> U
34
Q

What is affinity maturation?

A

selection of antibodies that have increased affinity for antigen

35
Q

What is isotype switching (1)?

A
  • prodcues immunoglobulin with a different constant region by identical antigen specificity
  • antibodies with different constant regions have different effector functions
  • homologous DNA recombination
36
Q

What is isotype switchign (2)?

A

DNA is lost

-further switching to downstream isotypes can take plae subsequently

37
Q

What is IgM?

A
  • monomer on B-cell
  • pentamer in serum
    - activates complement
    - neutralization (inactivation of (pathgen/toxin)
  • has 10 binding sites
38
Q

What is IgA?

A
  • 2 subclasses
  • IgA1- monomer in serum
  • IgA2-dimer in secretions

functions

  • neitralization
  • opsonization
  • major form of immunity at mucosal surface
  • More IgA made than any other antibidy
39
Q

What is IgG?

A

4 subclasses
longest 1/2 life —> passive immunization

Functions
neutralization 
opsonization 
complement activation 
**Cross placenta
40
Q

What are IgD and IgE?

A

IgD- monomer

  • B cell receptor
  • binds to basophils

IgE-monomer

  • least abundant in serum–> binds to mast cells and basophils via Fc region
  • immunity against parasitic infections
  • mediates allergic reactions

Immunology (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions