ABSTRACT
The novel betacoronavirus (SARS-CoV-2) is highly contagious and can cause serious acute respiratory illness syndromes, often fatal, called covid-19. It is an urgent priority to better understand SARS-CoV-2 infection mechanisms that will help in the development of prophylactic vaccines and therapeutics that are very important to people health and socioeconomic stability around the world. The surface coronavirus spike (S) glycoprotein is considered as a key factor in host specificity because it mediates infection by receptor-recognition and membrane fusion. Here the analysis of CoV-2 S protein revealed in S1subunit a B56-binding LxxIxE-like motif that could recruit the host protein phosphatase 2A (PP2A). This motif is absent in SARS-CoV and MERS-CoV. PP2A is a major family of serine/threonine phosphatases in eukaryotic cells. Phosphatases and kinases are big players in the regulation of pro-inflammatory responses during pathogenic infections. Moreover, studies have shown that viruses use multiple strategies to target PP2A in order to manipulate host’s antiviral responses. The latest studies have indicated that SARS-CoV-2 is involved in sustained inflammation in the host. Therefore, by controlling acute inflammation; it is possible to eliminate its dangerous effects on the host. Among efforts to fight covid-19, the interaction between LxxIxE-like motif and PP2A-B56-binding pocket could be a target for the development of a bioactive peptide and ligand inhibitors for therapeutic purposes.
