Host cell transmembrane protein MARCH8 targets lysine residues to inhibit SARS-CoV-2 and other viruses
The search for effective inhibitors with therapeutic potential against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), responsible for the shattering pandemic of coronavirus disease 2019 (COVID-19), has thrown up some surprising results.
A new study, released as a preprint on the
bioRxiv server, deals with the inhibitory activity of a membrane protein that has broad-spectrum activity against multiple viruses, showing that this is due to its effect on cytoplasmic lysine residue incorporation into replicating virions.
MARCH8 inhibits envelope protein expression
The membrane-associated RING-CH (MARCH) 8 protein is one of eleven similar proteins that form one category of RING-finger E3 ubiquitin ligases. It has two transmembrane domains linked by a short ectodomain. It reduces the expression of many host transmembrane proteins, such as the strategically importan
A new study discusses the origin of the furin cleavage site on the SARS-CoV-2 spike protein, which is responsible for the virus’s relatively high infectivity compared to relatives in the betacoronavirus subgenus.