Chapter 4 and Chapter 5 and Chapter 6

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2-15-23 Read the Behring & Kitasato article and complete the associated HW assignment Immunoglobulin structure; Chpt 4.1-4.8 Be prepared to draw (from memory) an immunoglobulin molecule (IgG) and identify the location of the Antigen binding sites, Variable regions, Constant regions, Hinge region, Fc region, Heavy chain, Light chain, and Hypervariable regions. What does the hinge region do? What is an Immunoglobulin domain and how are hypervariable regions related to it? What are continuous and conformational epitopes? What are some of the interactions that determine antigen binding by antibodies? We will not be describing antibody-antigen interactions in detail, but you should be aware of the variety of interactions that can take place. 2-20-23 Generation of antibody diversity; Chpt 5.1-5.8 Be prepared to draw a picture showing the active immunoglobulin locus in a mature B cell (not secreting antibody). Indicate the positions of Ig gene segments and where the coding sequences are located for the following regions of the antibody molecule: Variable, hypervariable, constant region, antigen binding site. What specific changes take place at the immunoglobulin locus during B cell development in the bone marrow? What is the difference between V(D)J recombination and class switching? What is the function of recombination signal sequences? What is the "12/23 rule" What is combinatorial and junctional diversity? Do not memorize the exact sequence of events in Rag- mediated recombination, but be prepared to explain what RAG and Tdt proteins do in the process. We will not be covering immunodeficiencies associated with defects in gene segment recombination in detail, but do understand what SCID is and the impact of a loss of activity in recombinase functions. 2-22-23 (Exam 1) 2-27-23 Antibody classes; Chpt 4.6-4.8, 5.8, 5.9 Monoclonal antibodies; Appendix A.8, ELISA; A.4) (9th Chpt 5.12-5.16, Monoclonal antibodies; Appendix A.7, ELISA; A.4)
Assays of T cell function; Appendix A. 26, A.28, A.30) (9th A.26, A.28, A.30) What structural features (in general) distinguish the different classes of immunoglobulins? Which classes are multivalent? Which are divalent? What functional differences are found between different Ig classes? (We are not covering Figure 4.7 (9th 5.20) in detail, but you should appreciate the major differences found between the Ig classes indicated in the figure and the text). When does Ig class switching occur? How is a preparation of anti-tetanus toxin antibody purified from antisera different from a preparation of anti-tetanus toxin antibody purified from a monoclonal producing hybridoma? What cells are used to make a monoclonal antibody-producing hybridoma? What characteristic does each cell type provide? Why does the intensity of color in the well at the end of an ELISA assay reflect the amount of antigen in the original sample? (We are not covering radioimmunoassay). Why is 3H-Thymidine incorporation a measure of cell proliferation? (We are not covering carboxyfluorescein assays of cell proliferation or cytotoxicity) How does a 51Cr-release assay identify T cells with cytotoxic activity? What distinguishes adoptive immunization from passive immunization? How could adoptive transfer be used for cancer treatment? We are starting our investigation of T cell function, beginning with MHC restriction, then describing T cell antigen receptors, MHC structure and function and mechanisms of antigen presentation. There is a substantial amount of material in MHC structure and antigen presentation sections 3-1-23 TCR structure and genetics 4.14, 4.15, 4.21, 5.10-5.11, 7.7 (9th ed 4.11, 4.12, 4.20, 5.9-5.10, 7.7) 1. What is the domain structure of the TCR? How many antigen binding sites does it have? How does the structure compare (in general) to immunoglobulin? (We are not doing the detailed analysis of TCR structure described in fig 4.19) 2. In general, how does gene segment rearrangement at that TCR locus compare with Ig 3. What is the ligand for the TCR? How does this compare to Ig? 4. Which subunits of the TCR and Ig carry out intracellular signaling and what domain structure is used for this? 5. How does gamma/delta TCR recognition of ligands differ from alpha/beta TCR recognition of ligands?
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