Benoît Arragain

This study shows that ANP32 is a conserved host factor for viral replication in the Articulavirales order, using structural and biochemical analyses of TiLV and its interaction with ANP32.

This study identifies transient RNA structures that drive nucleotide insertions leading to the formation of MBCSs in HPAIVs.

The paper describes the cryo-EM structure of TiLV nucleoprotein bound to RNA, revealing its RNA-binding mechanism and structural conservation across Articulavirales.

The paper reveals ANP32's role as an electrostatic chaperone stabilizing influenza polymerase complexes, explaining host adaptation and providing structural insights into replication complexes.