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Audray K. Harris, Ph.D.

Photo of Audray K. Harris, Ph.D. 

Chief, Structural Informatics Unit

Laboratory of Infectious Diseases

Major Areas of Research

  • Structure-function of viral glycoproteins
  • Epitope mapping and structure-supported design of immunogens
  • Molecular architecute and assembly of viruses
  • Predictive structural correlations to virus pathogenesis and immune escape
  • Coherent integration of structural, computational and biological information

Program Description

The Structural Informatics Unit (SIU) seeks to elucidate the molecular architecture of viral proteins and the roles that factors, such as pH environment and protein modification and variation, play in modulating structure-function, epitope display, and viral pathogenesis. The research program exploits 3D electron microscopy of viruses and protein complexes with antibodies to obtain structural information. Structural analyses are supported by other structural, biochemical, and immunological analyses in order to understand antigen-antibody interactions and aid in structure-assisted immunogen design for infectious diseases. Our research program integrates structural and biochemical studies with bioinformatics to facilitate a collaborative synergy between these disciplines in the context of the focus of structure-function studies of viruses and viral proteins. A major focus is on the antigenicity, structure, and function of respiratory viruses, such as influenza.

HIV gp140 trimers
HIV gp 140 trimers
Influenza virus particles
Influenza virus particles

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Dr. Harris received his Ph.D. in 2002 from The University of Alabama at Birmingham. Following postdoctoral training at the National Institute of Arthritis and Musculoskeletal and Skin Diseases, he joined the National Cancer Institute as a research fellow. In 2012, Dr. Harris was selected as an Earl Stadman Investigator and in 2013 joined the Laboratory of Infectious Diseases.

Research Group

Currently recruiting postdoctoral fellows

Selected Publications

Harris A, Subramaniam S. HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 MPER-directed broadly neutralizing antibody. Z13e1. 2013. Submitted.

Harris A, et al. Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies. Proc Natl Acad Sci U S A. 2013. In press.

Harris A, Borgnia MJ, Shi D, Bartesaghi A, He H, Pejchal R, Kang YK, Depetris R, Marozsan AJ, Sanders RW, Klasse PJ, Milne JL, Wilson IA, Olson WC, Moore JP, Subramaniam S. Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. Proc Natl Acad Sci U S A. 2011 Jul 12;108(28):11440-5.

Watts NR, Vethanayagam JG, Ferns RB, Tedder RS, Harris A, Stahl SJ, Steven AC, Wingfield PT. Molecular basis for the high degree of antigenic cross-reactivity between hepatitis B virus capsids (HBcAg) and dimeric capsid-related protein (HBeAg): insights into the enigmatic nature of the e-antigen. J Mol Biol. 2010 May 14;398(4):530-41.

Last Updated January 28, 2013

Last Reviewed January 28, 2013