ArticleMicrobiology spectrum2025
Critical amino acid residues in human ACE2 for SARS-CoV-2 spike protein binding and virus entry.
Article in Microbiology spectrum, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Review
- Computational and experimental identification of potential neutralizing peptides derived from human ACE2 against SARS-CoV-2 infection.Journal of virology · 2026Article
- Computational Discovery of Potent Nucleoprotein Inhibitors for Influenza A Virus: Validation Through QM/MM Analysis and Experimental Binding Assays.Molecules (Basel, Switzerland) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
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 simulations and pseudovirus assays, revealed that D30V and H34R substitutions reduce hACE2 binding affinity and fusogenic activity, impairing SARS-CoV-2 entry. However, the double mutant D30V-H34R did not reduce viral entry efficiency further, suggesting compensatory molecular interactions at the ACE2-S binding interface. These insights contribute to a deeper understanding of SARS-CoV-2-host interactions and may guide future therapeutic development targeting viral entry mechanisms. IMPORTANCE: Given the pivotal role of angiotensin-converting enzyme 2 (ACE2) in mediating viral entry and the genetic divergence observed in ACE2 orthologs across different species, we aimed to elucidate further the molecular intricacies underlying the interactions between severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike (S) protein and ACE2. In this study, we examined the amino acid residues in ACE2 orthologs interacting with SARS-CoV-2 spike receptor-binding domain to identify those with discernible effects on viral binding and entry. Through
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Registered trials
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