Penn Veterinary Medicine | University of Pennsylvania

Description of Research Expertise

Research Interests
Molecular Mechanisms of Negative-Sense RNA Virus Assembly/Budding.

Key words: Ebola virus; VSV; Matrix Proteins; Budding; Reverse-Genetics; Virus-Host Interactions.

Description of Research
My laboratory is interested in the molecular events that lead to virus assembly and budding. Our model virus systems include vesicular stomatitis virus (a virus that causes disease in bovine and equine species), and Ebola virus (a deadly human pathogen and potential agent of bioterrorism). Our studies are focused on the viral matrix proteins which are the major building blocks of the virus and function in assembly and budding. We are particulary interested in understanding how these viral matrix proteins interact with host proteins to faciltiate the budding process. By understanding the structure and function of these viral matrix proteins, we hope in the long term to be able to develop anti-viral drugs designed to inhibit the assembly and budding stages of these viral pathogens.

Rotation Projects for 2006-2007
1. Structure and Function studies on Ebola virus VP35, VP40, VP24, NP, and GP proteins.
2. Mechanism of viral RNA packaging into Ebola VLPs.
3. VSV Reverse-Genetics; Budding and Assembly of VSV Recombinants.
4. Rabies virus L-domain function. Reverse-genetics and pathogenesis.

Lab personnel:
Dr. Atsushi Okumura - Senior Postdoctoral Fellow
Dr. Yuliang Liu - Postdoctoral Fellow
Dr. Santanu Mukherjee - Postdoctoral Fellow

Selected Publications

Okumura, Atsushi. Pitha, Paula M. Harty, Ronald N.: ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity. Proceedings of the National Academy of Sciences of the United States of America 105(10): 3974-9, Mar 11 2008.

Han, Ziying. Harty, Ronald N.: Influence of calcium/calmodulin on budding of Ebola VLPs: implications for the involvement of the Ras/Raf/MEK/ERK pathway. Virus Genes 35(3): 511-20, Dec 2007.

McCarthy, Sarah E. Johnson, Reed F. Zhang, Yong-An. Sunyer, J Oriol. Harty, Ronald N.: Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and budding. Journal of Virology 81(20): 11452-60, Oct 2007.

Irie, Takashi. Carnero, Elena. Okumura, Atsushi. Garcia-Sastre, Adolfo. Harty, Ronald N.: Modifications of the PSAP region of the matrix protein lead to attenuation of vesicular stomatitis virus in vitro and in vivo. Journal of General Virology 88(Pt 9): 2559-67, Sep 2007.

Han, Ziying. Licata, Jillian M. Paragas, Jason. Harty, Ronald N.: Permeabilization of the plasma membrane by Ebola virus GP2. Virus Genes 34(3): 273-81, Jun 2007.

Johnson, Reed F. McCarthy, Sarah E. Godlewski, Peter J. Harty, Ronald N.: Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E minigenome RNA into virus-like particles. Journal of Virology 80(11): 5135-44, Jun 2006.

Johnson R.F., McCarthy S.E., Godlewski P.J., and Harty R.N.: Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E minigenome RNA into virus-like particles J. Virol. 80(11): 5135-44, Jun 2006.

Johnson R.F., Bell P., and Harty R.N.: Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology Virol J. 3(1): 31, May 2006.

Johnson, Reed F. Bell, Peter. Harty, Ronald N.: Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology. Virology Journal 3: 31, 2006.

Irie, Takashi. Harty, Ronald N.: L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus recombinants. Journal of Virology 79(20): 12617-22, Oct 2005.