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          About NIAMS
          Norman R. Watts, Ph.D.





Norman R. Watts, Ph.D.


Staff Scientist
    Protein Expression Laboratory Portrait of Norman Watts. 
            Contact Information

                                                  301-402-3418
                
                                                9000 Rockville Pike
                  
            50 South Drive
      
                  
            Building 50, Room 1509
      
                                   Bethesda MD 20892
                
                                                norman_watts@nih.gov 
                                          Media Resources
                                  
            High Resolution Image 
                Summary
          Structural virology has fascinated Dr. Norman R. Watts ever since he first discovered the field over 30 years ago. He has studied bacteriophages, crop pathogens and human viruses. In his spare time he enjoys stone carving and high altitude mountaineering.
        
                  Research Statement
          
            Dr. Watts’ research is focused on two viruses that have great impacts on people’s health, human immunodeficiency virus (HIV-1) and hepatitis B virus (HBV). Globally, 78 million people have been afflicted with HIV since the beginning of the epidemic, 37 million are living with HIV, and over 1 million die annually of related illnesses. HIV-1 expresses a regulatory protein called Rev that is indispensable for viral replication, yet its complete molecular structure remains unknown and there are no therapeutics that target Rev. The Protein Expression Laboratory, in collaboration with the Laboratory of Structural Biology Research, was the first to solve the atomic structure of the amino-terminal domain of Rev. We are currently pursuing the structure of the carboxyl-terminal domain, and also the structures of Rev in complex with viral RNA and with host proteins. In addition, we have generated synthetic antibody fragments targeted against Rev that strongly inhibit HIV replication in peripheral blood mononuclear cells.

Hepatitis B virus (HBV) is a major cause of liver disease in humans, afflicting almost 400 million worldwide, and is the leading cause of hepatic cancer. HBV expresses a protein indispensable to its replication called “core-antigen” (this forms the virus capsid) and a very closely related protein called “e-antigen” whereby the virus blinds the human immune system to its presence. The Protein Expression Laboratory, again in close collaboration with the Laboratory of Structural Biology Research, has closely examined, primarily by electron microscopy, the interaction of core-antigen with not only numerous monoclonal antibodies widely employed in clinical diagnosis but also the entire antibody repertoire in a patient. In addition, our laboratory was the first to determine the molecular structure of the e-antigen, and the remarkable way in which it differs from core-antigen. With this information we have developed not only the first and only completely molecularly defined clinical assay for HBV, but are also developing specific inhibitors of core-antigen and e-antigen function. 

            Scientific Publications
              A single endoplasmic reticulum aminopeptidase-1 protein allotype is a strong risk factor for Behçet's disease in HLA-B*51 carriers.

    Takeuchi M, Ombrello MJ, Kirino Y, Erer B, Tugal-Tutkun I, Seyahi E, Özyazgan Y, Watts NR, Gül A, Kastner DL, Remmers EF
        

                    Ann Rheum Dis.
        
                    2016 Dec;
        
                    75(12).
        
                    doi: 10.1136/annrheumdis-2015-209059
                            PMID: 27217550
  The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.

    DiMattia MA, Watts NR, Cheng N, Huang R, Heymann JB, Grimes JM, Wingfield PT, Stuart DI, Steven AC
        

                    Structure.
        
                    2016 Jul 6;
        
                    24(7).
        
                    doi: 10.1016/j.str.2016.04.015
                            PMID: 27265851
  A cell-penetrating antibody fragment against HIV-1 Rev has high antiviral activity: characterization of the paratope.

    Zhuang X, Stahl SJ, Watts NR, DiMattia MA, Steven AC, Wingfield PT
        

                    J Biol Chem.
        
                    2014 Jul 18;
        
                    289(29).
        
                    doi: 10.1074/jbc.M114.581090
                            PMID: 24878961
  Assessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry.

    Bereszczak JZ, Watts NR, Wingfield PT, Steven AC, Heck AJ
        

                    Protein Sci.
        
                    2014 Jul;
        
                    23(7).
        
                    doi: 10.1002/pro.2470
                            PMID: 24715628
  An unusual topological structure of the HIV-1 Rev response element.

    Fang X, Wang J, O'Carroll IP, Mitchell M, Zuo X, Wang Y, Yu P, Liu Y, Rausch JW, Dyba MA, Kjems J, Schwieters CD, Seifert S, Winans RE, Watts NR, Stahl SJ, Wingfield PT, Byrd RA, Le Grice SF, Rein A, Wang YX
        

                    Cell.
        
                    2013 Oct 24;
        
                    155(3).
        
                    doi: 10.1016/j.cell.2013.10.008
                            PMID: 24243017
  Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.

    Bereszczak JZ, Rose RJ, van Duijn E, Watts NR, Wingfield PT, Steven AC, Heck AJ
        

                    J Am Chem Soc.
        
                    2013 May 1;
        
                    135(17).
        
                    doi: 10.1021/ja402023x
                            PMID: 23597076
  Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein.

    DiMattia MA, Watts NR, Stahl SJ, Grimes JM, Steven AC, Stuart DI, Wingfield PT
        

                    Structure.
        
                    2013 Jan 8;
        
                    21(1).
        
                    doi: 10.1016/j.str.2012.10.017
                            PMID: 23219881
  Specificity of an anti-capsid antibody associated with Hepatitis B Virus-related acute liver failure.

    Wu W, Chen Z, Cheng N, Watts NR, Stahl SJ, Farci P, Purcell RH, Wingfield PT, Steven AC
        

                    J Struct Biol.
        
                    2013 Jan;
        
                    181(1).
        
                    doi: 10.1016/j.jsb.2012.10.004
                            PMID: 23079477 
          Education
              
            **Agriculture Canada**
NSERC Postdoctoral Fellow, 1992–1994

**University of Minnesota**
NSERC Postdoctoral Fellow, 1990–1992

**University of New Brunswick, Canada**
Ph.D., 1990             
                        Experience
              
            **Staff Scientist**
Protein Expression Laboratory, NIAMS/NIH, 1999–present

**Fogarty Fellow**
Laboratory of Structural Biology Research, NIAMS/NIH, 1994–1999


Last Updated: September 2021


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