Structure of influenza D virus NS1 reveals a novel Zn-binding site and ssRNA-binding activity

IDV NS1 C-terminal effector domain contains a novel Zn2+-binding site and preferential ssRNA-binding activity, and disrupting it blocks recovery of infectious recombinant virus.

• Why it matters: IDV NS1 is a key virulence factor in related influenza viruses, but its structure and RNA-binding mechanism were unclear, limiting understanding of IDV replication and zoonotic risk.
• What they did: Crystal structures were solved for the NS1 N-terminal RNA-binding domain and C-terminal effector domain; CTD ssRNA binding was mapped by mutagenesis to lysine/arginine residues and a Zn2+-binding site.
• The result: Single-residue substitutions that disrupted either Zn2+-binding or the RNA-binding interface prevented recovery of infectious recombinant IDV, showing CTD integrity is required for viral replication.

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