Researchers at EMBL Hamburg and collaborators at the Leibniz Research Institute for Molecular Pharmacology (FMP) have mapped how the influenza A virus rewires infected human cells in unprecedented detail. To do this, the researchers used a customized experimental workflow to directly observe how proteins interact inside intact infected cells.
Every year, seasonal influenza kills up to 650,000 people globally and causes serious illness for 3–5 million individuals. The influenza A virus, in particular, has been responsible for several pandemics, including the 1918 Spanish flu pandemic. When this virus infects cells, it releases its genetic material, called RNA, which contains blueprints for a handful of proteins. These proteins then spread throughout the host cell and repurpose its molecular machinery to make more viruses.
Scientists want to understand this process in detail because it would help in designing better drug therapies and vaccines against the flu virus. That's why it's crucial to figure out how proteins of the flu virus interact with proteins of host cells and subvert them to meet the virus's needs. This is the first time scientists have mapped direct virus-host protein contacts at scale inside intact influenza-infected cells, with enough structural detail to model how the proteins fit together.
"Our work provides a new way to study flu-host interactions in their native context and with structural insight," said Jan Kosinski, group leader at EMBL Hamburg and Centre for Structural Systems Biology (CSSB). "The current results are a snapshot of a moment during infection, and they open the door to studying flu-host interactions across the entire infection cycle."
Source: Phys.org
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