PMC:7712180 / 68440-69873 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7712180","sourcedb":"PMC","sourceid":"7712180","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7712180","text":"The aa sequences of hACE2 were aligned with aa sequences of ACE2 orthologues of possible natural reservoirs and possible intermediate hosts. Only the aa sequences corresponding to the hACE2 interface are shown in Figure 4b. Adaptation of each zoonotic virus to interact with aa residues at the hACE2 binding interface is critical for efficient transmission among humans. The hACE2 residues K31, D38, Y41 and K353 are important host determinants of adaptation of civet SARSr-CoV to human SARS-CoV (Figure 4b), and viral S1 RBD residues at the positions of 479 and 487 are important determinants of SARS-CoV binding preference (Figure 8a–c). The K479N mutation from civet to human viral S1 RBD can accommodate K31 on hACE2 [238]. The S487T mutation from civet to human viral S1 RBD can accommodate a hydrophobic pocket between Y41 and K353, neutralized by D38, on the hACE2 receptor for efficient interactions [234]. These findings agree with results obtained by Kan et al. [100] suggesting that viruses with SNVs leading to aa changes at these two positions are able to be transmitted from animals to infect humans and from humans to humans by close contact. However, the roles of the additional 4 aa substitutions at position 344 in the RBD but outside the RBS (Figure 8b) and positions 227, 244 and 778 outside the RBD in viruses isolated from patients during the global epidemic [100] in human-to-human transmission remain 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