Jarrod J. Mousa, PhD

Research Interest

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. Currently, we are focusing our efforts on the respiratory pathogens respiratory syncytial virus, human metapneumovirus, the parainfluenza viruses, and Streptococcus pneumoniae.

Lab Focus

Molecular mechanisms of Pneumovirus and Paramyxovirus neutralization

• Identification of neutralizing antigenic sites on viral glycoproteins
• Human antibody isolation to viral fusion and attachment proteins
• Structural analysis of antibody-antigen interactions
• Full characterization of antibody candidates

Broadly-reactive antibodies to Streptococcus pneumoniae

• Isolation of human monoclonal antibodies to pneumococcal conjugate vaccination
• Structural analysis of antibody-glycan interactions
• Identification of new human mAbs with broadly-reactive protein targets

Recent Publications

Mousa, J.J., Binshtein, E., Human, S., Fong, R.H., Alvarado, G., Doranz, B.J., Moore, M.L., Ohi, M.D., Crowe, J.E. (2017). Broad and potent neutralizing human antibody recognition of antigenic site IV on Pneumovirus fusion proteins. PLoS Pathogens, 14, 2018, e1006837.

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. *Featured on the April 2017 Cover

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. *Featured on the April 2017 Cover

Luo, Z., Ren, H., Mousa, J.J., Rangel, D., Dias, L.P., Bruner, S.D., Pei, Y., Keyhani, N.O. The PacC transcription factor regulates secondary metabolite production, stress response, but has only minor effects on virulence in the insect pathogenic fungus Beauveria bassiana. Environmental Microbiology 19, 2017, 788-802.

Mousa, J.J., Newsome, R. C., Yang, Y., Jobin, C. Bruner, S.D. ClbM is a versatile, cation-promiscuous MATE transporter found in the colibactin biosynthetic gene cluster. Biochemical and Biophysical Research Communications 482, 2017, 1233-1239.

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 USA2016, 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.

Mousa, J.J., Bruner, S.D. Structural and mechanistic diversity of multidrug transporters. Natural Product Reports 33, 2016, 1255-1267.

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.

Zhibing L., Yujie L., Mousa, J.J, Bruner, S., Zhang, Y., Pei, Y., and Keyhani, N. BbMsn2 acts as a pH-dependent negative regulator of secondary metabolite production in the entomopathogenic fungus Beauveria Bassiana. Environmental Microbiology 17, 2015, 1189-1202.

PubMed

Complete List of Published Work in PUBMED