Immunology Notes

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Microbiology and Immunology
Microbiology and Immunology 3300B
Rodney Dekoter

Immunology NotesSept 29 How does an immune system that is evolutionarily conserved and slow to change respond to pathogens that can change rapidly B cell receptors T cell receptors and antibodies function as adaptor molecules that are capable of recognizing lots of pathogens The immune system is capable of generating millions of receptors PRRs B cell receptors and antibodies consist of four polypeptide chains linked by disulphide bonds The light chains can beorhave the same general size and shape Thelight chain is used more often The heavy chains can be orThe antibody type is defined by the heavy chains The light and heavy chains are composed of constant and variable regions The antigen binding sites are located at the adaptor end of the molecule in the variable region and this surface interacts with epitopes The variable region differs between individual antibodies The flexible hinge allows the molecule to conform to many shapes The constant region is constant from one molecule or cell to the next Antibodies can be cleaved into functionally distinct fragments This is used to determine the functions of the different parts of the molecule The protease papain cleaves at the flexile hinge producing two Fab fragments and one Fc fragment The Fabs are the variable regions and they contain the antigenbinding activity The Fc fragment is the constant region and contains no antigenbinding activity It will form crystals at high concentrations because the amino acids are similar Proteolytic cleavage by pepsin forms two fragments One contains both Fabs together and the other is the Fc fragment which is cut into several small fragments The domains of an immunoglobulin molecule are structurally similar They are called domains because they adopt similar structures They are called Ig domains and are repeating structures in many molecules The light chain C and V domains are made up of two antiparallel sheets The V domain is
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