Critical amino acid residues in human ACE2 for SARS-CoV-2 spike protein binding and virus entry.

ABSTRACT: The coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), remains a significant global public health concern due to the continuous emergence and rapid spread of new variants. SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as its primary receptor to initiate viral entry into host cells. While ACE2 is highly conserved across different species, genetic variability in the interacting surfaces between ACE2 orthologs and SARS-CoV-2 spike (S) protein can modulate viral binding affinity and entry efficiency. This study investigates the impact of amino acid substitutions in human ACE2 (hACE2) interacting with the receptor-binding domain of SARS-CoV-2 S protein. Site-directed mutagenesis, combined with molecular dynamics sim

SUBMITTER: Chen W 

PROVIDER: S-EPMC12323325 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature