Lecture 7 Flashcards

1
Q

how do you make a monoclonal antibody?

A

a mouse is injected with Ag that has multiple epitopes, spleen cells are isolated, then fused with myeloma cells, the resulting hybridomas are selected for the specific Ab’s they secrete, those are then cloned

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2
Q

how do you make polyclonal antibodies?

A

inject a mouse with Ag containing multiple epitopes, isolate the serum, and the result is a polyclonal antiserum

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3
Q

what are 3 defining characteristics of BCRs?

A
  1. are secreted or membrane bound
  2. bind to intact molecules
  3. can recognize proteins, lipids, adn carbs
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4
Q

what are 2 defining characteristics of TCRs?

A
  1. membrane bound ONLY
  2. bind only to peptide Ag bound to MHC
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5
Q

describe the structure of a T Cell Receptor?

A

αβ heterodimer with only one Ag binding site

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6
Q

why does the RAG enzyme go through two cycles to produce a T-cell receptor protein?

A

because both the α-chain locus and the β-chain locus must undergo recombination from germline DNA

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7
Q

how many proteins is CD3 made of?

A

3

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8
Q

what is CD3 important for?

A

signal transduction

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9
Q

what are the 2 classes of T cell receptors?

A

α:β or γ:δ

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10
Q

what are characteristics of α:β TCR’s?

A

high specificity, “signature” molecule of adaptive immune response, binds Ag presented by MHC I or II

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11
Q

what are the characteristics of γ:δ TCR’s?

A

recognize classes of Ag present on groups of pathogens, functions more in innate immune response, NOT associated with MHC

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12
Q

organization of TCR genes are very similar to what other genes?

A

imunoglobulin genes

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13
Q

how does the mechanism of TCR rearrangement occur?

A

RAG recognizes RSS, 1/2 the recombinase recognizes RSS and VJ and VDJ joining, circular excision products are made by looping out and deletion during rearrangement

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14
Q

what does SCID stand for?

A

severe combined immunodeficiency

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15
Q

what causes SCID?

A

a mutation in RAG genes

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16
Q

what is the result of the RAG gene mutation?

A

no functional B or T lymphocytes, no TCR excision circles

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17
Q

MHC class I binds peptides recognized by what?

A

CD8 T cells

18
Q

MHC class I is expressed on what type of cell?

A

almost all somatic

19
Q

what does MHC class I function in?

A

pathogen surveillance and killing somatic cells

20
Q

MHC class II binds peptides recognized by what?

A

CD4 T cells

21
Q

what types of cells is MHC class II expressed on?

A

dendritic cells, macrophages, B cells

22
Q

what do MHC class II function in?

A

activating helper T cells

23
Q

give a brief explanation of Ag processing and presentation.

A

a pathogen protein enters the cell, the protein is broken down and Ag is processed, Ag binds to an MHC molecule on the membrane of the cell and is presented to a TCR

24
Q

what is the difference in MHC class I and MHC class II structure?

A

MHCI has an α and β chain whereas MHCII has two α chains

25
what is the result of a T cell binding to a virally infected cell?
cells dies
26
what is the result of a T cell binding to a macrophage?
macrophage is activated and cytokines are released
27
what is the result of a T cell binding to a B cell?
B cell activates granulizing and secreting antibody
28
where can Ag be derived from?
the cytosol and the vesicular system
29
what are the two Ag processing pathways?
1. cytosolic 2. endocytic
30
explain the cytosolic pathway
presents peptide with Class I MHC and uses endogenous self-peptides
31
explain the endocytic pathway
presents peptide with class II MHC and uses exogenous peptides
32
how are proteins carefully regulated?
there is continuous turnover, short half lives, and rapid degradation of abnormal proteins
33
what are proteosomes? name two examples
enzymes that degrade proteins 1. ubiquitin 2. immunoproteosome
34
define ubiquitin
constitutively tags cytosolic proteins for degradation
35
define immunoproteosome
produces peptides preferred by TAP and MHCI in cells stimulated by IFNs
36
where are MHCI synthesized?
rough ER
37
how do peptide fragment move from the cytosol to the rough ER?
TAP
38
what ensures that proteins are folded correctly?
chaperons
39
name the two chaperones involved in MHCI assembly
calreticulin and tapasin
40
what allows the MHCI +microglobulin+peptide to be released from the rough ER?
ERp57
41
what enzyme has the ability to shorten a peptide so that a MHCI can travel to the cell surface?
ERAP