Summary

Dr. Eren received her Ph.D. from Worcester Polytechnic Institute (WPI), where she studied metal transport mechanisms across eukaryotic, bacterial and archeal membranes by P-type ATPAses. During her postdoctoral studies at University of Massachusetts Medical School (UMASS), she focused on structure and function of outer membrane proteins, mainly Occ-family of porins, and their role in bacterial pathogenesis and antibiotic resistance. Currently, Dr. Eren works as a research fellow at National Institutes of Health (NIH) where she studies the underlying mechanisms of viral pathogenesis, viral protein-host protein interactions and the potential use of humanized scFvs and nanobodies for treatment.

Research Statement

Dr. Eren’s research is mainly focused on human immunodeficiency virus (HIV-1) and other viruses that can coinfect HIV-1 patients and increase morbidity and mortality rates, such as hepatitis B virus (HBV). HIV-1 rev protein is a key regulatory factor that is essential for both early and late phases of viral replication cycles. Rev binds to a 240-base region of complex RNA structure, the rev response element (RRE), and facilitates the export of unspliced or partially spliced viral RNAs from the nucleus to the cytoplasm. In addition to RRE, rev binds to several host proteins including Crm1/Ran-GTP complex, histone chaperons and tubulin. Dr. Eren and her colleagues use a combination of x-ray crystallography, cryo-em and biochemical methods to solve the structures of rev-RRE and rev-host protein complexes to find target regions to inhibit rev activity using antibodies, peptides and/or synthetic aptamers.

The HBV core gene encodes two proteins that share high sequence similarity but differ in their N- and C-termini and form two distinct dimers: core-antigen, which forms the nucleocapsid, and e-antigen which serves as an immune modulator. Recently, Dr. Eren and her colleagues identified antibodies and scFvs that bind to different epitopes on the core- and e-antigen dimers with sub-nanomolar affinity and prevent capsid formation in vivo. Current studies are focused on the use of these antibodies as potential therapeutic agents.

Last Updated: April 2019