Tufts University School of Medicine

How the flu virus builds a better mousetrap

First real-time visualization reveals that protein molecules on virus surface reach out to hijack target cells and reset the trap if they fail
Findings published in Cell show how the flu virus resets its trap
How the flu virus resets its trap: Advanced smFRET imaging of individual molecules of the influenza surface protein hemagglutinin (HA) reveals a new model of HA function. (Image used with permission of Cell)

BOSTON (June 28, 2018)—For the first time, scientists have directly visualized in real-time structural changes in the surface protein of the influenza virus that may help the virus to fuse with and enter target cells before hijacking their functions. Researchers at Tufts University School of Medicine found that single molecules of  the protein hemagglutinin (HA) that reside on the surface of the virus unfold to stretch toward target cells, then refold and try again 5 to 10 times per second. The discovery shows the flu virus to be more dynamic than previously thought and may help efforts to develop more effective vaccines and better understand other viruses such as Ebola, HIV, and SARS. The research appears in the journal Cell online June 28 and in print August 9.

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Department:

Molecular Biology and Microbiology

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Research