Selected article for: "cell infect and host cell"
Author: Eric W. Stawiski; Devan Diwanji; Kushal Suryamohan; Ravi Gupta; Frederic A. Fellouse; J. Fah Sathirapongsasuti; Jiang Liu; Ying-Ping Jiang; Aakrosh Ratan; Monika Mis; Devi Santhosh; Sneha Somasekar; Sangeetha Mohan; Sameer Phalke; Boney Kuriakose; Aju Antony; Jagath R. Junutula; Stephan C. Schuster; Natalia Jura; Somasekar Seshagiri
Title: Human ACE2 receptor polymorphisms predict SARS-CoV-2 susceptibility
  • Document date: 2020_4_10
    • ID: jfdshwfh_14
    Snippet: Mutagenesis of four residues in the S-protein-binding interface of rat ACE2 was sufficient to convert rat ACE2 into a human SARS-CoV receptor, further indicating the importance of this region in determining the host range and specificity of CoVs (Li et al., 2005b) . Considering these findings, we focused on variants within the human ACE2claw S-protein RBD-binding interface and identified protein alterations in 44 codons that 6 resulted in 49 uniq.....
    Document: Mutagenesis of four residues in the S-protein-binding interface of rat ACE2 was sufficient to convert rat ACE2 into a human SARS-CoV receptor, further indicating the importance of this region in determining the host range and specificity of CoVs (Li et al., 2005b) . Considering these findings, we focused on variants within the human ACE2claw S-protein RBD-binding interface and identified protein alterations in 44 codons that 6 resulted in 49 unique variants for a total of 968 allelic variants. This included K26R, the second most frequent human ACE2 protein-altering variant (0.4% allele frequency; allele count=797, gnomAD), S19P, T27A, K31R, N33I, H34R, E35K, E37K, D38V, N51S, N64K, K68E, F72V, T921, Q102P, G326E, G352V, D355N, H378R, Q388L, and Table 2 ). These variants are likely to either increase or decrease the binding affinity of ACE2 to the S-protein and thereby alter the ability of the virus to infect the host cell.

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