Microbiology and Immunology 3300B Study Guide - Final Guide: Complement Receptor, Immunoglobulin M, Covalent Bond
DepartmentMicrobiology and Immunology
Course CodeMICROIMM 3300B
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Microimmune Study Notes Lecture 7
1. How does our immune system evolve to rapidly changing viruses?
Adaptive immune system – have a conserved region and a variable region. Variable
region can adapt – we have BCR and TCR.
2. Explain TCRs.
T Cell Receptors will recognize and MHC peptide complex. MHC complex must be
presented. They are very small peptides; 8-12 amino acids. TCR is specific to one
MHC allele and one peptide.
3. Explain BCRs.
B cell receptors are composed of poly peptide chains that are held together by
disulfide bonds. Each arm consists of 4 heavy chains and 2 light chains. There are
two types of light chains; kappa and lamba. Kappa is more commonly used. There
are more types of heavy chains which include: alpha, gamma, delta, elipson, and
miuex. Depending on the type of heavy chain = type of antibody used. All are
4. Discuss the structure of the BCR.
Heavy chains lower region is a constant region; does not change; all molecule types
will be the same. The heavy/light combination at the top is the variable region that
adapts to different pathogens. No antibody with the same lower constant region will
have the same variable region up top. There is a flexible hinge in between the two –
adapts to bind different molecules. There are also different types of carbohydrates
sitting on the heavy chain constant regions.
5. How can antibodies be cleaved?
If cleaved by Papain; it seperates the antibody into 3 distinct regions. 2FAB = 2
fragment antigen binding and 1 FC = 1 fragment crystallized.
If cleaved by pepsin; it seperates the antibody into 2 distinct regions. 1FAB = 1
fragment antigen binding and 1 FC that is partially degraded.
6. Domains of immunoglobins are structurally similar.
7. Discuss epitopes and paratopes.
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