Chp3 Adaptive Immunity Flashcards

1
Q

What are the hallmarks or Adaptive Immunity. What is recognized?

A

Antibodies and t cell repectors
very specific
antibodies and TCR recognize epitopes

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2
Q

What is the definition and main function of an antibody. What are they collectively called? Where are they located? How many subtypes? Name them

A

Epitope binding proteins, found on the surface of B cells and in the blood serum (humoral). Known as Immunoglobulins? 5 IgM, IgG, IgA, IgD, IgE

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3
Q

What is the function and location of TCR’s?

A

Found on t-cell surfaces and recognize epitopes via the MHC complex

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4
Q

Define immunogenicity and Antigenicity.

A

Immu: ability to induce humoral or cell mediated response
anti: ability to combine with antibodies or MHC/TCR

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5
Q

What is a hapten?
What is a hapten-carrier conjugate?
- list 3 types of determinants

A

An antigen that is too small to induce an immune response. They LACK immunogenicity.

HCC: a protein that combines with hapten to produce an immune response

1) causes antibody to bind to hapten
2) ABS will bind to the carrier protein
3) abs will bind to the entire conjugate

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6
Q

List 4 things that determine if something is a good immunogen. What is the general size for an active immunogen?

A

1) being foreign
2) molecular size
3) chemical composition- lipids are poor, too repetitive
4) ability to be processed and presented via MHC

100,000 daltons

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7
Q

Describe how genotype, material presentation and adjuvents may increase immunogenecity.

A

genotype: many genes code for antibodies and MHC, highly variable, people react differently
material: it’s dosage and route of entry is important, if dosage is too high it may induce tolerance or not work at too low of a dosage
adjuvents: enhance, not sure how, but are recognized by TLR’s (water-in-oil)

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8
Q

What are the 5 routes of drug entry?

A

intravenously, intradermal, subcutaneously, intramuscular, intraperitoneal(into cavities)

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9
Q

What epitopes? How do they differ with B and T cells?

A

antigenic determinants that are recognized by the adaptive immune system.

B cells: epitopes that are present on the outer part of pathogen, because they dont use MHC, the epitope is intact for the antibodies to bind to
T: These epitopes are usually from within the pathogen, because these are broken down by APC/phagocytes and presented through MHC

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10
Q

What is a sequential and non sequential epitope?

A

draw it

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11
Q

Discuss the overall structure of an antibody. Use the terms light, heavy chain, effector, hinge, antigen binding, biological activity, hypervariable region, isotype, allotype, idiotype. Draw and label. WHERE IS IT FOUND?

A

found in serum, MALT, mother’s milk, saliva, tears (if you have bitch feelings)
Composed of a light and heavy chain, each chain has a hypervariable region that binds to antigen and a constant region that has other biological activities. The effectors bind and interact with complement. The hinge region is only found in some types.

Isotype: different constant region in species

allotype: differences that occur in some individuals
idiotype: differences that occur in variable region, even in the same isotype.

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12
Q

What is the reason some have a hinge region?

What is the Fab and Fc region?

A

when the gamma, delta and alpha heavy chains are rich in proline and cysteine, gives many S-S bonds and flexibility.

Fab= where the antigen binds, Fc is the effector functions

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13
Q

List 4 functions of antibodies with regards to their effectors.

A
  • complimentary binding via hypervariable region
  • promote phagocytosis via opsonization
  • activate complement
  • ADCC= antibody dependant cell mediated cytotoxity, activation of Nk cells towards the antibody Fc region.
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14
Q

Which antibodies are one unit, dimer and pentamer? Which have a hinge?

A

IgG, D, E are one unit, IgA is a dimer and IgM is a pentamer.

IgG and A, D have the hinge

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15
Q

IgM:

Structure and function. What is the J-chain?

A

first one produced, pentamer, best for agglutination and activated complement.

J chain is a joining chain and binds.

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16
Q

IgD:

Structure/function.

A

Has a hinge, 4 domains, membrane bound on B cells, can undergo class changes, activates basophils/mast cells

17
Q

IgG:

Structure/function

A

Most abundant, hinge, 4 sub classes, pass the placenta, activates complement.

18
Q

IgE:

Structure/function

A

allergic responses, no hinge, involved in Antibody Dependant Cell Cytotoxicity.

19
Q

What is the main function of a Mast Cell and does IgE aid it’s response?

A

An allergin will bind to IgE and then cross link to another IgE, this will bind to Mast cell via Fc region of the IgE and cause it to release its granules/histamine which causes the allergic response. This release is required to activate cells involved with ADCC.

20
Q

IgA:

structure/function

A

Dimer/hinge/J chain all present.
Found in breast milk, mucus.

Can cross link with large antigen, J chain give binding and transport across membranes and protects it from acids/enzymes in GI tract.

21
Q

What is the PolyIg Receptor and how does it aid IgA?

A

Allows it entry through epithelial cells , then it becomes a part of the IgA, which gives it protective abilities and allows it to easily pass through epithelial membranes.

22
Q

Name the 4 members of the immunoglobulin super family.

A

antibodies, TCRs, MHCI/II, CAMs

23
Q

What is a monoclonal antibody and how do you make one?

A

specific to only one type of epitope.

Inject a mouse in antigen, isolate spleen cells, take plasma cells out of spleen cells, mix with myelomas and this makes a hybridoma, then isolate the antibody.

24
Q

Compare and contrast BCR’s and TCR’s in relation to function towards antigens.

A

BCR’s are found in soluble form, strongly bind to antigen and bind directly to antigen, TCR are not and weakly bind to antigen through MHC complex.