Nonstructural protein 6

Nsp6, along with nsp3 and nsp4, plays a critical role in membrane rearrangement. In SARS-CoV-1 nsp6 is known to activate autophagy by inducing perinuclear vesicles localized around the microtubule organization center. SARS-CoV-2 nsp6 is 87% identical to SARS-CoV-1 nsp6. Non-conservative mutations are located on the protein surface.

Narrative

Upon infection, corona viruses create signature membrane rearrangements (e.g. DMVs) so that the viral RNA replication complex may anchor to host machinery (den Boon and Ahlquist 2010). Nsp6, along with nsp3 and nsp4, plays a critical role in this membrane rearrangement (Angelini et al. 2013). In SARS-CoV-1 nsp6 is known to activate autophagy (Cottam et al. 2011) by inducing perinuclear vesicles localized around the microtubule organization center (Angelini et al. 2013).

Structural analysis and comparison with SARS-CoV-1 nsp6 – SARS-CoV-2 nsp6 is 87% identical to SARS-CoV-1 nsp6. Non-conservative mutations are located on the protein surface.