Rupert C. L. Beale

SARS-CoV-2 envelope protein induces LC3 lipidation via the V-ATPase-ATG16L1 axis

This study shows SARS-CoV-2 E protein induces LC3 lipidation through the V-ATPase-ATG16L1 axis, which supports viral replication rather than inhibiting it.

Caspase cleavage of Influenza A virus M2 disrupts M2-LC3 interaction and regulates virion production

This study shows that caspase cleavage of the Influenza A virus M2 protein disrupts its interaction with LC3, reducing virion production.

The V-ATPase/ATG16L1 axis is controlled by the V1H subunit

This paper identifies the V1H subunit of V-ATPase as a regulator of ATG16L1 recruitment in response to pH gradient disruption, linking V-ATPase function to autophagy activation.

The stem loop 2 motif is a site of vulnerability for SARS-CoV-2

The paper identifies the stem loop 2 motif as a vulnerable site in SARS-CoV-2 that can be targeted by antisense oligonucleotides to inhibit replication and infection.