Dr. Eren received her Ph.D. from Worcester Polytechnic Institute (WPI), where she studied metal transport mechanisms across membranes by P-type ATPases. Mutations in Cu-ATPases, a subfamily of ATPases, are associated with Menkes and Wilson’s diseases in humans. During her postdoctoral studies at the University of Massachusetts Medical School (UMASS), she focused on the structure and function of outer membrane proteins, mainly Occ-family of porins from P. aeruginosa, and their role in bacterial pathogenesis and antibiotic resistance. After her postdoctoral studies, Dr. Eren joined the National Institute of Allergy and Infectious Diseases (NIAID) at NIH as a research fellow where she studied host immune system manipulation by Rotavirus proteins. In 2015, she joined the Laboratory of Structural Biology Research and the Protein Expression Laboratory at the National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS). She currently studies the underlying mechanisms of viral pathogenesis, viral protein-host protein interactions, and the potential use of humanized scFvs and nanobodies for treatment.
Due to the development of resistance to current HIV antiretroviral therapy (ART) and the known toxicity of some of the ART drugs, there is a clear need to identify and develop novel compounds for use in the treatment of HIV-1 patients. The HIV-1 Rev protein is a key regulatory factor that is essential for both early and late phases of viral replication cycles, and therefore represents an important viral target for drug development. Rev completes nucleocytoplasmic transport of unspliced or partially spliced HIV-1 mRNA by cooperatively assembling on the highly structured ~350 nucleotide long Rev response element (RRE) and hijacking the host Crm1/Ran-GTP export system. Rev interacts with Crm1 through a leucine-rich nuclear export signal located in its C-terminus, and with RRE through an Arginine rich motif (ARM) located in the N-terminal region. The ARM is a highly specific sequence which contains a nuclear localization signal. Rev has been reported to interact with many host proteins including importin-ß, histone chaperons (Nap1 and B23), and tubulin through its ARM domain. Very little is known about most of these interactions. Dr. Eren's research focuses on understanding the structural and mechanistic aspects of Rev-host protein interactions and finding target regions to inhibit Rev activity using antibodies, synthetic peptides, and aptamers.