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Immunohematology and Serology > Chapter 2 - Antibody > Flashcards

Chapter 2 - Antibody Flashcards

1
Q
  • Which three classes have a hinge region in their Fc?

- Where exactly is the hinge region?

A
  • The Fc region of IgG, IgA, and IgD

- Has a hinge region between the CH1 and CH2 that gives flexibility

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2
Q
  • Describe the structure of the immunoglobulin hinge region

- What purpose does it serve?

A
  • Region is not globular: stretch of prolines

- So paratopes have flexibility to reach the epitopes

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3
Q
  • What are the other two classes that don’t have a hinge region?
  • What do they have instead?
A
  • IgM and IgE do not have a hinge region

- - Have an extra constant region CH4 instead

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4
Q

Glycosylation

  • Define
  • Where does it occur on each of the Ig?
A
  • Little bit of sugar molecules added to the amino acids of the immunoglobulin
  • Occurs at the CH2 of IgG, IgA, and IgD, and at the CH3 of IgM and IgE
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5
Q
  • In comparison to other Ig, how much IgA is in the serum?
  • Where is it the primary Ig?
  • Describe the structure in both locations.
A
  • Second highest in serum concentration
  • IgA primary immunoglobulin in secretions
  • In serum: it is a monomer
  • In secretion: it is a dimer
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6
Q

IgA Dimer:

  • Where are the monomers joined?
  • What are they joined by?
  • What segment does this have unique to IgA and its purpose?
A
  • The Fc regions together and the Fab regions facing out
  • Held together by a 15,000 dalton J (joining) chain
  • Contains a secretory piece that is synthesized by an epithelial cell
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7
Q

IgA dimers joined with the J chain:

  • what type of cell receptor do they bind to?
  • what does that cell do with the Ig after binding?
A
  • Bind to an epithelial cell receptor
    • A precursor of the secretory piece
  • The Ig is brought into the epithelial cell
    • Transverses the epithelial cell
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8
Q
  • What happens to the IgA at the secretory lumen?

- What is the final step for IgA?

A
  • Part of the secretory piece is cleaved

- The IgA dimer attached to the remaining secretory piece (70,000 daltons) is secreted

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9
Q

IgA: Secretory functions

- What are they (4)?

A
  • Prevents the entrance of pathogens
  • Cross-links multiple epitopes to form aggregates
  • Easily removed by the ciliated cells of the mucous membranes and by gut peristalsis
  • Also functions by blocking adhesion of the bacteria, virus, or toxin
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10
Q

IgA Subclasses:

  • what are they?
  • where do you find each of them?
A
  • IgA1
    • Main component of serum IgA
  • IgA2
    • Main component of secreted IgA
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11
Q

Classes, Subclasses, and Light Chains: IgA

  • Binds complement?
  • Opsonic?
  • Transferred through placenta?
A
  • Does not bind complement
  • It is opsonic
  • Not transferred via placenta to the fetus
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12
Q

Classes, Subclasses, and Light Chains: IgA

  • How does it transfer to a newborn?
    • what else is transferred this way?
A
  • Transferred to newborn by breast milk

- - Contains lots of IgA and other proteins, oligosaccharides, and fatty acids

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13
Q

Classes, Subclasses, and Light Chains: IgM

  • % in the serum?
  • Structure
    • shape
    • Fc and Fab locations
A
  • 5–10% of the immunoglobulin in serum
  • Pentamer composed of 5 of the 2 heavy chain and 2 light chain units
    • Starfish-like shape
    • Fc regions in the center
    • Fab arms extended out
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14
Q

Classes, Subclasses, and Light Chains: IgM

  • Size?
  • what is another name for this type of Ig?
  • What is a tumor called that produces IgM?
A
  • Largest immunoglobulin
    • 900,000 daltons
  • Called a macroglobulin because of large molecular weight
  • Tumor in which the tumor plasma cells make IgM is called a macroglobulinemia
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15
Q

Classes, Subclasses, and Light Chains: IgM

  • what type of cells does this Ig bring together?
  • good/bad at agglutination?
  • good/bad at precipitation?
A
  • Brings together cells that are slightly charged
    • Repulsion due to charge is diminished over great binding distance
  • Best immunoglobulin at agglutination and precipitation
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16
Q

Classes, Subclasses, and Light Chains: IgM

  • Fixes complement?
  • Opsonic?
  • What type of antigens does it neutralize?
A
  • Best at fixing complement by the classical pathway
  • Opsonic
  • Neutralizes toxins and viruses
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17
Q

Classes, Subclasses, and Light Chains: IgM

  • How quickly does it respond to antigens?
  • Why does it have a lower affinity?
  • Does it have a high or low avidity? Why?
A
  • First immunoglobulin produced in response to an antigen
  • Produced without the somatic mutation events that improve affinity, so affinity is lower
  • But Avidity can be high
    • 10 paratopes on a pentameter, as opposed to 2 on a monomer
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18
Q

Classes, Subclasses, and Light Chains: IgM in newborns

  • made or acquired?
  • what does it mean if it’s seen in a newborn?
A
  • First immunoglobulin produced in a newborn
  • Elevations in IgM after birth indicate an infection
    • the baby was exposed after birth
19
Q

Classes, Subclasses, and Light Chains: IgM in newborns

  • does it cross the placenta?
  • does it cross into extravascular spaces?
  • what is the half-life?
A
  • Does not cross the placenta
  • Does not enter extravascular spaces
  • Half-life is 10 days
20
Q

Classes, Subclasses, and Light Chains: IgM on B cells

  • describe the structure
  • what region is different compared to serum IgM?
A
  • Monomeric not pentameric
  • Slightly different Fc region
    • Transmembrane and cytoplasmic regions
21
Q

Classes, Subclasses, and Light Chains: IgM on B cells

  • where is most surface IgM found?
  • what are some other cells it is found on?
A
  • Immature B cells
  • Mature B cells
    • Most surface IgM is found on immature and mature B cells
  • Plasma cells
  • Memory B cells
22
Q

Classes, Subclasses, and Light Chains: IgM on B cells

  • what does the antigen bind to on the B cell?
  • what does it do to the cell once it binds?
  • what does the B cell then become?
A
  • Antigen binding to surface IgM
    • Sends signals into B cell
  • Activates, proliferates
  • Becomes memory or plasma cell
23
Q

Classes, Subclasses, and Light Chains: IgD

  • % in serum?
  • what cells found on?
  • what role does it serve on that cell?
  • what is its main function?
A
  • Only ~ 0.2% of serum immunoglobulin
  • On the surface of mature B cells
  • Involved in antigen-specific B cell activation and is a maturation marker for the B cell
  • Functions as a specific antigen receptor
24
Q

Classes, Subclasses, and Light Chains

  • what two Ig appear on a B cell and in what order?
  • what does the addition of the second Ig help the B cell to do (2)?
A

IgM appears on the surface of B cells first, then IgD

  • IgD:
    • Helps the B cell respond to signals from T cells
    • Helps the B cell switch to synthesis of IgG, IgA, or IgE
25
Q

Classes, Subclasses, and Light Chains: IgD

  • Binds complement?
  • Opsonic?
  • Transferred through placenta?
A
  • Does not bind complement
  • Not opsonic
  • Not transferred to the fetus through placenta
26
Q

Classes, Subclasses, and Light Chains: IgE

  • concentration in serum
  • what notable reaction in the body is it responsible for?
  • molecular size?
    • why is it that size?
  • what cells are responsible for producing it?
A
  • Lowest in concentration
  • Responsible for immediate type hypersensitivity
  • ~ 190,000 daltons
    • due to extra CH region which binds mast cells
  • Made by plasma cells along respiratory tract, the skin, and alimentary tract
27
Q

Classes, Subclasses, and Light Chains: IgE

  • what cells does it bind to?
  • what happens to those cells once binding occurs?
A
  • Binds to mast cells

- Binding of the antigen will cause mast cell degranulation

28
Q

Classes, Subclasses, and Light Chains: IgE

  • What granules are released upon mast cell binding
  • What symptoms does that illicit in the body?
A
  • Releases histamine, heparin, and chemotactic factors
  • Substances cause the classic symptoms of allergy, hay fever, asthma, vomiting, diarrhea, hives, shock, and anaphylactic death
29
Q

Classes, Subclasses, and Light Chains: IgE

  • in what instance does this Ig serve in a protecting role?
    • How does it do this?
A
  • Protective role for things that have penetrated the mucosa, such as parasites
    • Triggers inflammatory response
    • Brings eosinophils, neutrophils to the area
30
Q

Classes, Subclasses, and Light Chains: IgE

  • Binds complement?
  • Opsonic?
  • Transferred through placenta?
A
  • does not bind complement
  • does not enhance phagocytosis
  • does not pass through the placenta
31
Q

Classes, Subclasses, and Light Chains: Light chains

  • what are the two types?
  • what ratio are they found in?
  • what does it mean when they are found in urine?
  • what are they called then?
A
  • Two types: kappa (k) and lambda (λ)
    • No functional differences between types
  • Present in roughly a 2:1 ratio
  • Found in the urine of patients with myeloma
    • One of the first diagnostic markers of a tumor
  • Called Bence-Jones proteins
32
Q
  • What happens when an animal is inoculated with human Ig?
A
  • will result in the production of antibodies to different regions of the immunoglobulin.
33
Q

Vaccination of an animal with human immunoglobulin:

  • What are isotypic determinants?
  • What are allotypic determinants?
  • What is the significance of the idiotype?
A
  • Isotypic determinants, heavy chain type - difference is related to which constant region is involved
  • Allotypic determinants, different on different members of the same species - difference is inherited from mom/dad
  • May regulate immune response
34
Q
  • What is the clonal selection theory?

- What is the key idea behind it?

A
  • Proposes how the huge and diverse immunoglobulin repertoire could exist
  • Key idea: lymphocytes that can only react with one antigen, before any encounter with antigen has occurred. When these lymphocytes interact with antigen they proliferate and make a clone of cells that respond only to that antigen
35
Q
  • What is the conservation of DNA theory?

- - what are the three pieces that make up the theory?

A
  • diversity theory
    1. Antigen-independent random recombinational events of DNA gene segments during B-cell maturation
    1. Antigen-dependent clonal deletion of self-reactive B cells
    1. Antigen-dependent somatic mutation and affinity maturation
36
Q

Antigen-Independent Diversity
- define
- what three genes are the heavy chain variable regions
encoded by?
– what happens after the genes go through recombination?

A
  • Random recombinational events of DNA gene segments during B-cell maturation
  • Encoded by three gene segments: V, D, and J genes
  • Gene segments after recombination are joined to the heavy chain constant region
37
Q

Antigen-Independent Diversity
- what two genes are the light chain variable regions
encoded by?
– what happens after the genes go through recombination?

A
  • Encoded by two gene segments: V and J genes

- Gene segments are joined to the light chain constant region after a recombinational event

38
Q

Antigen-Independent Diversity: Tonegawa discovery

  • what chromosome are the genes that make the following components located on?
    • heavy chains
    • kappa light chains
    • lambda light chains
A
  • heavy chains made by genes from chromosome 14
  • kappa light chains are made by genes from chromosome 2
  • lambda light chains are made by genes from chromosome 22
39
Q

Antigen-Dependent Clonal Deletion

- what purpose does it serve?

A
  • Decreases diversity in a mechanism

- - Helps maintain the self–non-self recognition system of the acquired immune response

40
Q

Antigen-Dependent Clonal Deletion

  • when does maturational arrest occur?
  • what happens to the “arrested” cell?
A
  • Occurs if a maturing B cell meets and binds with its antigen prior to maturation
  • Does not become a mature B cell
41
Q

Antigen-Dependent Clonal Deletion

- in this particular process, how does apoptosis occur?

A
  • the B cell, after receiving certain signals, produces enzymes that degrade its own DNA to commit cellular suicide
42
Q

Antigen-Dependent Somatic Mutation and Affinity Maturation

- what happens when a B or T-cell binds antigen (4)?

A
  • Rapid proliferation of the cell occurs
  • Initially each offspring cell is identical in binding to the original parental cell
  • Mutation occurs during this rapid proliferation
  • Cells that have increased affinity of binding are selected and proliferate more
43
Q

Antibody Purification

- what characteristics must be taken into account when trying to purify proteins (4)?

A
  • Solubility characteristics
  • Molecular weight
  • Binding affinities
  • Charge
44
Q

Antibody Purification

- what are the two methods of purifying antibody?

A
  • Ammonium sulfate precipitation

- Affinity purification of antibody

Immunohematology and Serology (8 decks)

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