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          About NIAMS
          Elif Eren, Ph.D.





Elif Eren, Ph.D.


Staff Scientist
    Protein Expression Laboratory Photo of Dr. Eren. 
            Contact Information

                                                  301-451-2281
                
                                                9000 Rockville Pike
                  
            50 South Drive
      
                  
            Building 50, Room 1511
      
                                   Bethesda MD 20892
                
                                                elif.eren@nih.gov 
                Summary
          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.
        
                  Research Statement
          
            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. 

            Scientific Publications
              Structural characterization of the Myxococcus xanthus encapsulin and ferritin-like cargo system gives insight into its iron storage mechanism.

    Eren E, Wang B, Winkler DC, Watts NR, Steven AC, Wingfield PT
        

                    Structure.
        
                    2022 Apr 7;
        
                    30(4).
        
                    doi: 10.1016/j.str.2022.01.008
                            PMID: 35150605
  Conformational changes in tubulin upon binding cryptophycin-52 reveal its mechanism of action.

    Eren E, Watts NR, Sackett DL, Wingfield PT
        

                    J Biol Chem.
        
                    2021 Oct;
        
                    297(4).
        
                    doi: 10.1016/j.jbc.2021.101138
                            PMID: 34461087
  Capsids of hepatitis B virus e antigen with authentic C termini are stabilized by electrostatic interactions.

    Watts NR, Palmer IW, Eren E, Steven AC, Wingfield PT
        

                    FEBS Lett.
        
                    2020 Mar;
        
                    594(6).
        
                    doi: 10.1002/1873-3468.13706
                            PMID: 31792961
  Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.

    Eren E, Watts NR, Dearborn AD, Palmer IW, Kaufman JD, Steven AC, Wingfield PT
        

                    Structure.
        
                    2018 Oct 2;
        
                    26(10).
        
                    doi: 10.1016/j.str.2018.06.012
                            PMID: 30100358
  Structure of an RNA Aptamer that Can Inhibit HIV-1 by Blocking Rev-Cognate RNA (RRE) Binding and Rev-Rev Association.

    Dearborn AD, Eren E, Watts NR, Palmer IW, Kaufman JD, Steven AC, Wingfield PT
        

                    Structure.
        
                    2018 Sep 4;
        
                    26(9).
        
                    doi: 10.1016/j.str.2018.06.001
                            PMID: 30017564
  A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export.

    Watts NR, Eren E, Zhuang X, Wang YX, Steven AC, Wingfield PT
        

                    J Struct Biol.
        
                    2018 Aug;
        
                    203(2).
        
                    doi: 10.1016/j.jsb.2018.03.011
                            PMID: 29605570
  Chimeric rabbit/human Fab antibodies against the hepatitis Be-antigen and their potential applications in assays, characterization, and therapy.

    Zhuang X, Watts NR, Palmer IW, Kaufman JD, Dearborn AD, Trenbeath JL, Eren E, Steven AC, Rader C, Wingfield PT
        

                    J Biol Chem.
        
                    2017 Oct 6;
        
                    292(40).
        
                    doi: 10.1074/jbc.M117.802272
                            PMID: 28842495
  Modeling of the rotavirus group C capsid predicts a surface topology distinct from other rotavirus species.

    Eren E, Zamuda K, Patton JT
        

                    Virology.
        
                    2016 Jan;
        
                    487().
        
                    doi: 10.1016/j.virol.2015.10.017
                            PMID: 26524514 
          Education
              
            **Worcester Polytechnic Institute (MA, USA)**
Ph.D., Biochemistry (2007)

**Middle East Technical University (Ankara, Turkey)**
M.Sc., Biochemistry (2001)

**Middle East Technical University (Ankara, Turkey)**
B.Sc., Chemistry (1999)             
                        Experience
              
            **Staff Scientist (2020 - Present)**
National Institute of Arthritis and Musculoskeletal and Skin Diseases, MD

**Research Fellow (2015 - 2020)**
National Institute of Arthritis and Musculoskeletal and Skin Diseases, MD

**Research Fellow (2014 - 2015)**
National Institute of Allergy and Infectious Diseases, MD

**Postdoctoral Fellow (2007 - 2012)**
University of Massachusetts Medical School, MA


Last Updated: February 2022


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