id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-277137-k3jj5vom	Anand, Praveen	SARS-CoV-2 strategically mimics proteolytic activation of human ENaC	2020-05-26		.txt	text/plain	2707	144	53	We report that SARS-CoV-2 has evolved a unique S1/S2 cleavage site, absent in any previous coronavirus sequenced, resulting in the striking mimicry of an identical FURIN-cleavable peptide on the human epithelial sodium channel α-subunit (ENaC-α). Although the furin-like cleavage motifs can be found in other viruses (Coutard et al., 2020) , the exact mimicry of human ENaC-a cleavage site raises the specter that SARS-CoV-2 may be hijacking the protease network of ENaC-a for viral activation. The overlap of the cell-types expressing ACE2 and ENaC-a, and similar spatial distributions at the apical surfaces, suggest that SARS-CoV-2 may be leveraging the protease network responsible for ENaC cleavage. SARS-CoV-2 then exploits enzymes called proteases to cut, or cleave, its spikes at a specific site which allows the virus to infiltrate the host cell. show that the spike proteins on SARS-CoV-2 may have the same sequence of amino acids at its cut site as a human epithelial channel protein called ENaC-a.	./cache/cord-277137-k3jj5vom.txt	./txt/cord-277137-k3jj5vom.txt