Welcome to the Dikeakos Lab

In addition to the virally encoded enzymes required for replication and assembly, HIV-1 expresses a collection of accessory proteins that lack intrinsic enzymatic activity but which are essential for disease pathogenesis by dysregulating host cell enzymatic activities to counterattack the host antiviral response and promote virus replication. In particular, the HIV-1 accessory protein Nef is required for the efficient onset of AIDS following HIV-1 infection. Nef modifies the host cellular environment in many ways, including alteration of T cell activation, modulation of apoptotic and autophagic pathways, as well as disrupts the intracellular trafficking of MHC-I and other cell surface molecules of helper T cells and macrophages. Our laboratory is interested in the various interactions between Nef and host cellular partners and how these interactions modulate membrane trafficking pathways to evade the immune system.

Recent Publications:

An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I. Dikeakos JD, Thomas L, Kwon G, Elferich J, Shinde U, Thomas G. Mol Biol Cell. 2012 Jun;23(11):2184-97. Epub 2012 Apr 11. PMID: 22496420 [PubMed - in process]

Tumor necrosis factor-related apoptosis inducing ligand (TRAIL) induced lysosomal translocation of proapoptotic effectors is mediated by phosphofurin acidic cluster sorting protein-2 (PACS-2). Werneburg NW, Bronk SF, Guicciardi ME, Thomas L, Dikeakos JD, Thomas G, Gores GJ. J Biol Chem. 2012 May 29. [Epub ahead of print] PMID: 22645134 [PubMed - as supplied by publisher]