As discussed above, infection by SARS-CoV is the result of several steps, including receptor binding, S glycoprotein conformational alterations, and proteolysis within endosomes that is mediated by capthepsin L (30). SARS-CoV infection has been shown to be blocked by targeted inhibitors of cathepsin L (30). On a related note, it has been shown that complete inhibition of viral entry and replication can result from treatment of cells with a cathepsin inhibitor as well as treatment with the serine protease inhibitor, camostat, which blocks activity of the type II transmembrane serine protease (TTSP) TMPRSS2, a surface-expressed serine protease that cleaves the coronavirus S protein and is involved in viral entry into a host cell (31). It has been proposed that imatinib may inhibit the function, localization or activity of TMPRSS2 (29). This suggests that this may be a promising drug:target match that could be further explored as a potential treatment for SARS-CoV-2 infection, since SARS-CoV-2 uses the SARS-CoV receptor ACE2 and the protease TMPRSS2 to enter host cells. In addition, ABL and ARG kinases have been found, in cancer cells, to promote secretion of the endosomal protease cathepsin L (30) (32). Thus, the testing of the ability of ABL inhibitors to inhibit cathepsin L in the context of viral infection may be warranted. It may generally be worthwhile to evaluate each of these targets with respect to what is known about SARS-CoV-2 infection and conduct further studies to elucidate potential therapeutic approaches involving ABL inhibition.