The Lassa Virus’s Molecular Key to Infection
A new study in Biophysical Journal reveals critical details about how Lassa virus (LASV), a deadly hemorrhagic fever pathogen, enters human cells. The research focuses on the virus’s glycoprotein complex, specifically its fusion domain, which is responsible for merging the viral membrane with the host cell’s lysosomal membrane. The work demonstrates that this domain exhibits significant structural plasticity and identifies bis(monoacylglycero)phosphate, a lipid found in lysosomes, as a key host factor exploited by the virus to facilitate membrane fusion and initiate infection.
Why it might matter to you: This research provides a precise molecular blueprint for a critical step in the pathogenesis of a high-consequence RNA virus. For microbiologists and virologists focused on host–microbe interactions and viral replication, these findings highlight a specific lipid–protein interaction as a potential target for novel antiviral strategies. Understanding the structural basis of LASV entry could directly inform rational vaccine development and the design of fusion inhibitors, advancing efforts to combat emerging and endemic viral threats.
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