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

Go to the profile of Michael Chao
Apr 13, 2017
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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.

Nature Microbiology 2: 16271 (2017)

Nature Microbiology 2: 16272 (2017)

Go to the profile of Michael Chao

Michael Chao

Associate Editor, Nature Microbiology

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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