Chapter 6 - The Structure and Function of Antibodies At the end of this Chapter, students should be able to: . Explain the structure of the B cell receptor complex and immunoglobulins. . Describe the structure of the immunoglobulins, the process of class switching, and the distribution and function of the different classes of immunoglobulin in the body. Zoom polls are not for grades. I have solved the mystery of the missing videos - there was a button that was unselected in my Zoom account page (not sure how or why it happened). All future classes will have the video - unfortunately there is no video file to recover for Jan 18 and 20 lectures. 1
Chapter 6 - The Structure and Function of Antibodies What do antibodies bind to? The structure that antibodies bind to are called epitopes (or antigenic determinants): - have distinct three-dimensional shape (not necessarily a linear sequence), - are typically about the size of 4 - 5 amino acids, - but the epitopes don't have to be amino acids (proteins), - epitopes can also be lipid, carbohydrate, synthetic chemicals etc. Antigens typically have more than one kind of epitope. Recall, that TCRs recognize a linear sequence of amino acids (peptide) that are complexed with the MHC protein. Because antibodies can bind to different structures, they can be useful tools in research. Antibodies can be used to isolate specific molecules from solutions for example. 2
Chapter 6 - The Structure and Function of Antibodies Assume that the cartoon below is a bacterium called "Clostridium reallydangerous" that tries to infect MICB202 students (especially those doing online classes). The antibody is binding to a protein that the bacterium uses to adhere (bind) to the cells of MICB202 students during the infection process. The antibodies could be described as: Anti-C. reallydangerous antibodies. Anti-C. reallydangerous adherence protein antibodies. 0 0 Could also include antibody class in the name. Anti-C. reallydangerous IgG. Anti-C. reallydangerous adherence protein IgG. 3