SARS-CoV-2 Spike Protein Receptor Binding-ACE2 Interaction Increases Carbohydrate Sulfotransferases and Reduces N-Acetylgalactosamine-4-Sulfatase through Phospho-p38-MAPK and RB-E2F1

Immunohistochemistry of post-mortem lung tissue from patients with SARS-CoV2 infection showed marked decline in intensity and distribution of N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB), increase of total chondroitin sulfate by immunohistochemistry, and increase of vascular-associated carbohydrate sulfotransferase (CHST)15 [1]. The mechanisms leading to these observations were not explained by signaling pathways known to be activated by exposure to coronaviruses. This report addresses the underlying reactions leading to these observations in a cell-based model, using normal, human, primary small airway epithelial cells, treated with the SARS-CoV-2 spike protein receptor binding domain protein.