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Richard Plemper


Ph.D. in Cell Biology and Biochemistry, University of Stuttgart, Germany, 1999
Postdoctoral training in the Molecular Medicine Program at Mayo Clinic and the Department of Microbiology & Immunology at Emory University.


Richard Plemper, Professor at Georgia State University, specializes in myxovirus pathogenesis and the development of therapeutics against myxovirus infection. His research is primarily focused on understanding how RNA viruses of the myxovirus families (influenza virus and human pathogens of the paramyxovirus family) enter cells and replicate their genetic information, and applying this insight to the development of novel antiviral therapeutic strategies.
Dr. Plemper earned his Ph.D. degree in Cell Biology and Biochemistry at the University of Stuttgart in Germany. Before joining Georgia State University, he was an Associate Professor in the Department of Pediatrics at Emory University.

Research Interests

Myxovirus Biology and the Development of Myxovirus Inhibitors

The primary focus of research in my laboratory is to elucidate how RNA viruses of the myxovirus families (influenza virus and human pathogens of the paramyxovirus family such as measles virus and respiratory syncytial virus) enter cells and replicate their genetic information, and apply this insight to the development of novel antiviral strategies. We pursue this goal in three major research programs:

  1. To define the structural and mechanistic framework for paramyxovirus infection.
  2. To mechanistically characterize the viral RNA-dependent RNA-polymerases and develop allosteric and substrate-analog inhibitors of myxovirus polymerases.
  3. To identify druggable viral and host targets that are required for myxovirus replication and develop novel small-molecule antivirals with anti-myxovirus indication spectrum.

My group reaches these aims in an interdisciplinary approach that combines molecular virology, cell biology and biochemistry, structural biology, light and electron microscopy, high-throughput assay design and execution with medicinal chemistry, pharmacology, and viral pathogenesis models.



  1. Krumm SA, Takeda M, Plemper RK. The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity. J Biol Chem. 288, 29943-29953 (2013).
  2.  Brindley MA, Suter R, Schestak I, Kiss G, Wright ER, Plemper RK. A stabilized headless measles virus attachment protein stalk efficiently triggers membrane  fusion. J Virol. 87, 11693-11703 (2013).
  3. Yan D, Krumm SA, Sun A, Steinhauer DA, Luo M, Moore ML, Plemper RK. Dual myxovirus screen identified a small-molecule agonist of the host antiviral response. J Virol. 87, 11076-11087 (2013).
  4. Brindley MA, Takeda M, Plattet P, Plemper RK. Triggering the measles virus fusion machinery. Proc Natl Acad Sci U S A. 2012 109:E3018-3027 (2012).
  5. Steinhauer DA, Plemper RK. Structure of the primed paramyxovirus fusion protein. Proc Natl Acad Sci U S A. 109:E3018-3027 (2012).
  6. Dochow M, Krumm SA, Crowe JE Jr, Moore ML, Plemper RK. Independent structural domains in paramyxovirus polymerase protein. J Biol Chem. 287, 6878-6891 (2012).
  7. Plemper RK, Brindley MA, Iorio RM. Structural and mechanistic studies of measles virus illuminate paramyxovirus entry. PLoS Pathog. 7:e1002058 (2011).
  8. Krumm SA, Ndungu JM, Yoon JJ, Dochow M, Sun A, Natchus M, Snyder JP, Plemper RK. Potent host-directed small-molecule inhibitors of myxovirus RNA-dependent RNA-polymerases. PLoS One. 6, e20069 (2011).
  9. Brindley MA, Plemper RK. Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H. J Virol. 84, 12174-12184 (2010). Featured Article
  10. Yoon JJ, Krumm SA, Ndungu JM, Hoffman V, Bankamp B, Rota PA, Sun A, Snyder  JP, Plemper RK. Target Analysis of the experimental measles therapeutic AS-  136A. Antimicrob. Agents Chemother. 53, 3860-3870 (2009)
  11. Paal T, Brindley MA, St Clair C, Prussia A, Krumm SA, Gauss D, Snyder JP, Plemper RK. Probing the spatial organization of measles virus fusion   complexes. J Virol. 83, 1159-1171 (2009).
  12. Lee JK, Prussia A, Paal T, White, LK, Snyder JP, Plemper RK. Functional interaction between paramyxovirus fusion and attachment proteins. J. Biol. Chem. 283, 16561-16572 (2008).
  13. Lee JK, Prussia A, Snyder JP, Plemper RK. Reversible inhibition of fusion activity of the measles virus F protein by an engineered intersubunit disulfide bridge. J. Virol. 81, 8821-8826 (2007).
  14. White LK, Yoon JJ, Lee JK, Sun A, Du Y, Fu H, Snyder JP, Plemper RK. Non-nucleoside inhibitor of measles virus RNA-dependent RNA polymerase complex activity. Antimicrob. Agents Chemother. 51, 2293-2303 (2007).
  15. Doyle J, Prussia A, White LK, Sun A, Liotta DC, Snyder JP, Compans RW and  Plemper RK. Two domains that control pre-fusion stability and transport competence of the measles virus fusion protein. J Virol, 80, 1524-1536 (2006).
  16. Plemper RK, Erlandson KJ, Lakdawala AS, Sun A, Prussia A, Boonsombat J, Aki-Sener E, Yalcin I, YildizI, Temiz-Arpaci O, Tekiner B, Liotta DC, Snyder JP and   Compans RW. A target site for template-based design of measles virus entry    inhibitors. Proc. Natl. Acad. Sci. USA, 101, 5628-5633 (2004).

Full Publications