April 2017 cover
Crystal structures define the molecular basis of antibody neutralization of RSV. Image by James Crowe and Jarrod Mousa; Cover Design: Samantha Whitham
Published in
Microbiology
Stopping RSV in its tracks
Crystal structures of two potent RSV antibodies in complex with the RSV fusion protein determine the molecular basis for neutralization of the virus, including a new antigenic site and the basis for cross-reactivity with human metapneumovirus.
Refers to "A novel pre-fusion conformation-specific neutralizing epitope on the respiratory syncytial virus fusion protein" by Mousa et al.
and
"Structural basis for antibody cross-neutralization of respiratory syncytial virus and human metapneumovirus" by Wen et al.
Project Manager, Harvard TH Chan School of Public Health
I first developed an interest in bacterial pathogenesis while at Cornell University. I then earned my PhD in Biomedical and Biological Sciences from Harvard University in Eric Rubin’s laboratory, studying cell wall remodelling in Mycobacterium tuberculosis. From 2012-2015, I continued my training as a postdoctoral fellow in Matthew Waldor’s lab at Harvard Medical School, investigating the role of DNA methylation on regulating fundamental cellular processes in Vibrio cholerae.
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