Center for Vaccines and Immunology, Department of Infectious Diseases
Assistant Professor
Expertise
Immunology | Infectious Diseases | Vaccinology | Virology
Biography
Jarrod Mousa received his PhD from the University of Florida where he studied the structure and mechanism of multidrug transporters in pathogenic bacteria. He then completed a postdoctoral fellowship at the Vanderbilt Vaccine Center where he studied the human antibody response to respiratory syncytial virus. His research interests lie at the interface between immunology and structural biology, particularly looking at antibody-antigen interactions to inform the design of next-generation vaccines.
Research Interests
We are under constant threat from viruses, bacteria, parasites, and fungi, all of which express surface proteins critical for attachment, entry into host cells, virulence, and evasion of the host immune system. The Mousa Laboratory is interested in elucidating the molecular mechanisms by which the human immune system combats these pathogens. We use a wide-range of translational approaches to study the molecular interactions mediating antibody neutralization of infectious pathogens. We study the human antibody response to select pathogens utilizing approaches to isolate human monoclonal antibodies as potential therapeutics, and determine their mechanism of action using biochemical, immunological, and structural approaches such as X-ray crystallography. These efforts are informing the design of next-generation vaccines and therapeutics.
Two pathogens we have particular interest in are respiratory syncytial virus (RSV) and human metapneumovirus (hMPV). Both viruses are closely related and can cause severe respiratory tract infection in the immunocompromised, such as premature infants and the elderly. Unfortunately, no vaccine is currently available for either virus, leading to thousands of unnecessary hospitalizations and deaths each year worldwide. Developing a vaccine for RSV and hMPV has been particularly challenging due to the unpredictability of the human immune system to previously tested vaccines. Therefore, we are studying the molecular basis for antibody-mediated immunity to RSV and hMPV to better understand the mechanism by which these viruses can be neutralized effectively, and our isolated antibodies may serve as the next line of therapeutics in the continuing battle against RSV and hMPV infection.
We are also participating in collaborative efforts across the UGA Center for Vaccines and Immunology and Department of Infectious Diseases.
Educational Background
BS Chemistry, University of North Florida
BA English, University of North Florida
PhD Chemistry/Biochemistry, University of Florida
Postdoctoral Fellow in Virology/Immunology, Vanderbilt University Medical Center
Selected Publications
- Mousa, J.J, Yang Y., Tomkovich, S., Shima, A., Newsome, R., Tripathi, P., Oswald, E., Bruner, S. D., Jobin, C. MATE transport of the E. coli-derived genotoxin colibactin. Nature Microbiology 1, 2016, 15009.
- Wen, X., Mousa, J.J., Bates, J. Lamb, R.A., Crowe, J.E., Jardetzky, T.S. Structural basis for antibody cross-neutralization of respiratory syncytial virus and human metapneumovirus. Nature Microbiology 2, 2017, 16272.
- Mousa, J.J., Kose, N., Matta, P., Gilchuk, P., Crowe, J.E. A novel pre-fusion conformation-specific neutralizing epitope on the respiratory syncytial virus fusion protein. Nature Microbiology 2, 2017, 16271.
- Mousa, J.J., Sauer, M.F., Sevy, A.M., Finn, J.A., Bates, J.T., Alvarado, G., King, H.G., Loerinc, L.B., Fong, R.H., Doranz, B.J., Correia, B., Kalyuzhniy, O., Wen, X., Jardetzky, T.S., Schief, W.R., Ohi, M.D., Meiler, J., Crowe, J.E. Structural basis for non-neutralizing antibody competition at antigenic site II of the respiratory syncytial virus fusion protein. Proceedings of the National Academy of Sciences USA 2016, 113, E6849-E6858.
- Wen, X., Pickens, J., Mousa, J.J., Leser, G., Lamb, R.A., Crowe, J.E., Jardetzky, T.S. A chimeric pneumovirus fusion protein carrying neutralizing epitopes of both MPV and RSV. PLoS ONE 11, 2016, e0155917.
