id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-288824-sygnmiun	Lam, SD	SARS-CoV-2 spike protein predicted to form complexes with host receptor protein orthologues from a broad range of mammals	2020-08-19		.txt	text/plain	7353	412	54	To predict infection risks, we modelled S-protein:ACE2 complexes from 215 vertebrate species, calculated changes in the energy of the complex caused by mutations in each species, relative to human ACE2, and correlated these changes with COVID-19 infection data. We correlated changes in the energy of the complex with changes in the structure of ACE2, chemical properties of residues in the binding interface, and experimental COVID-19 infection phenotypes from in vivo and in vitro animal studies. We used multiple methods to assess the relative change in binding energy (ΔΔG) of the SARS-CoV-2 S-protein:ACE2 complex following mutations in DC residues and DCEX residues that are likely to influence binding. Irrespective of host, the SARS-CoV-2 spike receptor binding domain is conserved (Fig. 4b) across tested human and animal associated SARS-CoV-2, suggesting mutations in the RBD are not required for infections observed in non-human species to date.	./cache/cord-288824-sygnmiun.txt	./txt/cord-288824-sygnmiun.txt