Although measles is a disease not often seen in the developed world, it is the leading cause of child mortality due to an infectious agent in the developing world. Signaling Lymphocytic Activation Molecule (SLAM), also known as CD150, was recently discovered to be a MV receptor along with the previously known CD46. To determine important amino acids in the binding of SLAM to MV, out lab first identified the V region of SLAM to be the essential one for infection through infectivity studies. We then compared the permeability of human, mouse dog and tamarin SLAM to MV infection, and found that only human and tamarin SLAM allow MV infection. For this thesis, The hydrophobic and hydrophilic residues of SLAM which were different between human and mouse were mutated to evaluate the importance of each for SLAM and MV H protein binding. These results were then compared with a computer-generated model of SLAM. Our results reveal a hydrophilic region of the molecule that is very important for binding.
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