Create a table to convey the structural differences between the five immunoglobulin classes. Include the following: Molecular Weight Protein in the heavy chain (example: IgM has two mu heavy chains) Any subclasses (if applicable) Uniqueness of the structure (if any) (monomer, dimer, etc) If it can cross the placenta (Yes or No) If it can agglutinate and/or precipitate (Yes or No) Where the antibody found (serum, saliva, etc.) Percentage of circulating immunoglobulin (in serum)

Create a table to convey the structural differences between the five immunoglobulin classes. Include the following: Molecular Weight Protein in the heavy chain (example: IgM has two mu heavy chains) Any subclasses (if applicable) Uniqueness of the structure (if any) (monomer, dimer, etc) If it can cross the placenta (Yes or No) If it can agglutinate and/or precipitate (Yes or No) Where the antibody found (serum, saliva, etc.) Percentage of circulating immunoglobulin (in serum)

Principles Of Pharmacology Med Assist

6th Edition

ISBN:9781337512442

Author:RICE

Publisher:RICE

Chapter16: Antifungal, Antiviral, And Immunizing Agents

Section: Chapter Questions

Problem 20RQ

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Antibody diversity is generated by multiple mechanisms, each of which contributes to the generation of antibodies with up to 1011 different amino acid sequences in their antigen-binding sites. Several of these mechanisms involve changes in the DNA sequences encoding the antibody heavy and light chain proteins. One mechanism that does not rely on changes to the DNA within the immunoglobulin heavy and light chain gene loci is, instead, dependent on: The contributions of amino acids from both the heavy chain and the light chain to form the antigen-binding site The random usage of V, D, and J gene segments to form the heavy chain V region sequence The random usage of k light chains versus l light chains to pair with the heavy chain The activity of TdT to add random nucleotides at the junctions between the V, J, and D region sequences The fact that heavy chain V regions contain an extra gene segment encoded by the D region compared to light chain V regions
alpha:beta TCRs are membrane-bound proteins comprised of two polypeptides linked by a disulfide bond. Both polypeptide components of the alpha:beta TCR are members of the immunoglobulin superfamily, and each of their domains share structural similarity with regions of antibody proteins. However, due to the different functions of TCRs versus antibodies, the overall domain organization of the TCR is not the same as for an antibody. In the figure below, describe three features that are incorrect illustrations of the alpha:beta TCR.
The immunoglobulin molecules of a particular mammalian species have kappa and lambda light chains and heavy chains. The kappa gene consists of 250 V and 8 J segments. The lambda gene contains 200 V and 4 J segments. The gene for the heavy chain consists of 300 V, 8 J, and 4 D segments. If just somatic recombination and random combinations of light and heavy chains are taken into consideration, how many different types of antibodies can be produced by this species?
One strategy for vaccine development currently under investigation is the use of pathogen-derived T cell epitopes as a component of the vaccine. For viral pathogens, implementing this strategy involves scanning the predicted amino acid sequences of the viral proteins for likely peptide epitopes that would bind to MHC class I and MHC class II molecules. In addition to the complication of MHC sequence polymorphism in the human population, another complication of this strategy for peptide epitopes that would bind to MHC class II proteins is: The importance of viral proteins containing peptides that are cleaved into 8–10 amino acid long fragments. The ability of viruses to mutate their proteins to avoid MHC anchor residue sequences. The fact that long peptides (>13 amino acids) are rapidly degraded in cells. The fact that MHC class II proteins are intrinsically stable, even in the absence of binding to a peptide. The absence of defined sequence motifs that predict peptide binding to…
For the following questions, specify which immunoglobulin is being described, according to the following key: a) IgA b) IgE c) IgG d) IgM e) more than one 33) Produced early in infection with high avidity 34) Labeled "secretory* 35) Most associated with parasitic infection 36) Generally produced most prominently following clearance of initial infection 37) Pentameric 38) Capable of forming a hybridoma 39) Associated with mast cell activation 40) Found predominantly in mucus secretions
Before the mechanism for generating antibody diversity had been established, a mechanism based on protein folding around an antigen was proposed, primarily by Linus Pauling. In this model, antibodies that had different specificities had the same amino acid sequence but were folded in different ways. Propose a test of this model.
Explain the difference between affinity and avidity. For which immunoglobulin class might avidity be particularly important in antigen recognition?
Briefly explain the characteristics of the Immunoglobulin (Ig) Classes.
There are two classes of MHC molecules with distinct subunit compositions but similar three-dimensional structures. Both MHC class I and MHC class II molecules are highly polymorphic genes in the human population, with tens to hundreds of different alleles co-existing in the population. This means that a comparison of the MHC protein sequences between two individuals would reveal amino acid differences between one individual and the next. However, these amino acid differences are not randomly distributed along the entire protein, but are clustered in certain locations. In the figure below, the diagram that most correctly indicates the regions of greatest variability between different MHC proteins (shown by the red highlights) is:
Several vaccines against viral infections are made by isolating purified surface proteins of the viral particle, mixing them with an adjuvant to stimulate an innate immune response, and injecting the mixture into people. Two examples of this are the vaccine against Hepatitis B virus, and the vaccine against Human Papilloma Virus (the ‘cervical cancer’ vaccine). One interesting property of vaccines of this type (known as ‘subunit vaccines’) is that there is a requirement for a CD4 T cell response to the vaccine antigen in order to generate antibodies to the innocuous protein in the vaccine. In the case of the Hepatitis B vaccine, the viral protein included in the vaccine is the Hepatitis B surface antigen (HepB-SAg), a protein that is approximately 200 amino acids in length. The graph in Figure Q4.27 shows the data from immunizing individuals with this vaccine, and monitoring their production of protective antibody responses to the viral protein. a) What results would be predicted if…
Which of the IgG subclasses would you think was in principle most desirable for use as a therapeutic monoclonal antibody, and why? Are there any disadvantages to using this subclass and how might they be overcome?
How are antibodies unique? Please discuss the structure of an antibody. What are the V and C regions? Discuss how the few hundred genes involved are capable of making endless amounts of antibodies. Besides medical treatment what is another way antibodies can be used?