Characterization of homo and heterodimeric chemokine CXCR4 and CCR5 receptors association with molecular chaperones and scaffold

Human Immunodeficiency Virus (HIV) infection occurs via the attachment of the virus on cell surface receptors, particularly CD4, CXCR4 or CCR5. Yet, while we understand how we can remove the receptors from the cell surface, we do not know very well how the receptors get to the surface. Also, it was shown that CXCR4 and CCR5 can function as pairs in a cell, just like two CXCR4 or two CCR5 receptors can. As for most cell surface receptor dimers, very little is known regarding the specific proteins that interact with each receptor pair and how this affects the signal sent in the cell. We believe each receptor dimer can interact specifically with a group of proteins, of which some will be different. We want to understand the influence of interacting partners on the trafficking route used by receptors and how it affects the signals sent inside the cell. We have shown that there are some specific partners that interact specifically with some complexes while they do not interact with other receptor pairs. We used one of those partners and showed that altering its expression can modify the extent of HIV infection. We believe that interfering with normal interactors of HIV receptors could lead to the development of new therapies that could complement the ones currently available.