Benoît Arragain

Structures of the Tilapia Lake Virus replication complex show that ANP32 is a host factor for replication across the Articulavirales order

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.

Structure of the Tilapia lake virus nucleoprotein bound to RNA

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

Structures of influenza A and B replication complexes explain avian to human host adaption and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.

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