Researchers at EMBL Hamburg and partner institutes have, for the first time, produced a large-scale structural map showing how influenza A directly rewires infected human cells by tracing virus–host protein interactions inside intact cells. The peer‑reviewed study reveals detailed protein contacts and spatial relationships that explain how the virus hijacks cellular machinery — findings the authors say could guide development of improved flu drugs and vaccines.
The international team, including scientists from the Leibniz Research Institute for Molecular Pharmacology (FMP) and Charité – Universitätsmedizin Berlin, used a customised experimental workflow to capture protein interactions within living infected cells. According to the researchers, this is the first map of direct virus–host protein contacts inside intact influenza‑infected cells with enough structural detail to model how the proteins fit together.
Jan Kosinski, group leader at EMBL Hamburg and the Centre for Structural Systems Biology, said the work “provides a new way to study flu‑host interactions in their native context.” He added that the current dataset is only “a snapshot of a moment during infection,” but that the approach opens the door to studying interactions across the full infection cycle.
To catch short‑lived and location‑specific contacts that previous methods missed, the team adapted cross‑linking mass spectrometry (XL‑MS) for virus‑infected cells. Boris Bogdanow of Charité explained the advantage of the method, saying it lets researchers “capture protein‑protein interactions directly in infected intact cells” while delivering structural clues about how those interactions occur. The authors say this structural information could help identify actionable targets for pharmaceutical intervention.
The XL‑MS experimental data were combined with a modified version of AlphaFold, the protein‑structure prediction algorithm, which the team fed with cross‑link constraints. That integration told the model which parts of viral and host proteins lie close together inside infected cells, improving reliability for virus–host complexes that are typically hard to predict.
The study highlights two major ways influenza A takes control of host cells. First, researchers traced how the viral surface protein haemagglutinin travels through the cell’s transport and processing systems, identifying host proteins that assist the virus in folding and modifying this essential surface protein during infection.
Second, the team discovered that influenza A infection causes paraspeckles — small, droplet‑like compartments in the cell nucleus — to dissolve. That dissolution releases RNA‑binding proteins the virus can exploit for its replication. “What surprised us most was the paraspeckles,” said lead author Iuliia Kotova, now at ETH Zurich, noting that the effect appeared across every cell line and flu strain tested and “might be a strategy” rather than a side effect.
Seasonal influenza is estimated to cause up to 650,000 deaths worldwide each year and serious illness in 3–5 million people. The authors stress that by revealing the structural interfaces between viral and human proteins, their map provides new targets and a framework for future drug and vaccine research.
Original Source: https://theshillongtimes.com/2026/07/21/study-reveals-how-flu-virus-hijacks-human-cells-to-multiply/
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Publish Date: 2026-07-21 06:12:00
