F A C U L T Y   P R O F I L E 


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Professor of Pediatrics, Physiology & Cellular Biophysics and Microbiology & Immunology

Molecular biology of paramyxoviruses, viral entry, prevention of viral infection


Current Research

Our laboratory conducts basic research on paramyxoviruses that cause serious and prevalent childhood diseases, and on newly emerging paramyxoviruses that affect humans. We investigate common pediatric respiratory viruses (parainfluenza viruses, respiratory syncytial virus) as well as emerging lethal henipaviruses (Nipah and Hendra viruses). The focus is on the mechanisms of viral entry into host cells, in the intial stages of infection. The laboratory is best known for identifying critical roles of the viral receptor binding protein in activating the viral fusion process during infection. By identifying the mechanism of fusion activation, we have now have identified promising targets for interfering with the viral entry process.

The lab is organized around the interdisciplinary theme of virus-host interactions. Projects draw from strategies and methods of molecular biology, cell biology, biophysics, immunology, computational biology, structural biology, and virology. Projects are inter-related in ways that lead to constant communication and contributions to each other's development.


Selected Publications

Moscona, A. (2015) RSV vaccine: Beating the virus at its own game. Sci. Transl. Med. 7: 312fs344.

Mathieu, C., Huey, D., Jurgens, E., Welsch, J.C., DeVito, I., Talekar, A., Horvat, B., Niewiesk, S., Moscona, A. and Porotto, M. (2015) Prevention of measles virus infection by intranasal delivery of fusion inhibitor peptides. J. Virol. 89: 1143-1155.

Gui, L., Jurgens, E.M., Ebner, J.L., Porotto, M., Moscona, A. and Lee, K.K. (2015) Electron tomography imaging of surface glycoproteins on human parainfluenza virus 3: association of receptor binding and fusion proteins before receptor engagement. MBio. 6: e02393-02314.

Jurgens, E.M., Mathieu, C., Palermo, L.M., Hardie, D., Horvat, B., Moscona, A. and Porotto, M. (2015) Measles fusion machinery is dysregulated in neuropathogenic variants. MBio. 6: e02528-02514

Palgen, J.L., Jurgens, E.M., Moscona, A., Porotto, M. and Palermo, L.M. (2015) Unity in diversity: shared mechanism of entry among paramyxoviruses. Prog. Mol. Biol. Transl. Sci. 129: 1-32.

Palmer, S.G., DeVito, I., Jenkins, S.G., Niewiesk, S., Porotto, M. and Moscona, A. (2014) Circulating clinical strains of human parainfluenza virus reveal viral entry requirements for in vivo infection. J. Virol. 88: 13495-13502.

Xu, R., Palmer, S.G., Porotto, M., Palermo, L.M., Niewiesk, S., Wilson, I.A. and Moscona, A. (2013) Interaction between the hemagglutinin-neuraminidase and fusion glycoproteins of human parainfluenza virus type III regulates viral growth in vivo. MBio. 4: e00803-00813.

Welsch, J.C., Talekar, A., Mathieu, C., Pessi, A., Moscona, A., Horvat, B. and Porotto, M. (2013) Fatal measles virus infection prevented by brain-penetrant fusion inhibitors. J. Virol. 87: 13785-13794.

Talekar, A., Moscona, A. and Porotto, M. (2013) Measles virus fusion machinery activated by sialic acid binding globular domain. J. Virol. 87: 13619-13627.

Talekar, A., DeVito, I., Salah, Z., Palmer, S.G., Chattopadhyay, A., Rose, J.K., Xu, R., Wilson, I.A., Moscona, A. and Porotto, M. (2013) Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation. J. Virol. 87: 10980-10996.

Porotto, M., Salah, Z.W., Gui, L., DeVito, I., Jurgens, E.M., Lu, H., Yokoyama, C.C., Palermo, L.M., Lee, K.K. and Moscona, A. (2012) Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state. J. Virol. 86: 12838-12848.

Pessi, A., Langella, A., Capito, E., Ghezzi, S., Vicenzi, E., Poli, G., Ketas, T., Mathieu, C., Cortese, R., Horvat, B., Moscona, A. and Porotto, M. (2012) A general strategy to endow natural fusion-protein-derived peptides with potent antiviral activity. PLoS One. 7: e36833.