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The L455F mutation increases the binding affinity of the spike protein to <t>ACE2.</t> A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated <t>hACE2</t> to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model
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The L455F mutation increases the binding affinity of the spike protein to <t>ACE2.</t> A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated <t>hACE2</t> to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model
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The L455F mutation increases the binding affinity of the spike protein to <t>ACE2.</t> A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated <t>hACE2</t> to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model
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The L455F mutation increases the binding affinity of the spike protein to <t>ACE2.</t> A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated <t>hACE2</t> to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model
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The L455F mutation increases the binding affinity of the spike protein to ACE2. A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated hACE2 to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model

Journal: BMC Infectious Diseases

Article Title: Characterization of private mutations in the spike protein of SARS-CoV-2 correlates with viral prevalence

doi: 10.1186/s12879-025-11414-3

Figure Lengend Snippet: The L455F mutation increases the binding affinity of the spike protein to ACE2. A Fluorescence imaging of WT/EG.5.1/EG.5.1-L455F spike pseudovirus-infected 293/ACE2 cells at 72 h. B Relative Fluorescence Units (RFU) measured in 293/ACE2 cells infected with WT/EG.5.1/EG.5.1-L455F spike pseudoviruses at 72 h. *, P < 0.05, ****, P < 0.0001. C and D Biolayer interferometry was used to analyze the binding of biotinylated hACE2 to EG.5.1 spike protein or EG.5.1-L455F spike protein. The curves represent the results of a global fit of the data using a 1:1 binding model

Article Snippet: Recombinant Human ACE2 Protein (His & AVI Tag), Biotinylated (Sino Biological, Beijing, China), and SARS-CoV-2 EG.5.1 spike-L455F (synthesized by Sino Biological, Beijing, China) were tested for molecular interactions at concentrations of 500nM, 250nM, 125nM, 62.5nM and 31.25nM, respectively.

Techniques: Mutagenesis, Binding Assay, Fluorescence, Imaging, Infection

Complex models of the spike protein RBD with hACE2. A Structural representation of the complex between EG.5.1 RBD (yellow) and hACE2 (purple), highlighting the positions of L455 (red) and L456 (grey) in the EG.5.1 RBD. B Structural representation of the complex between EG.5.1-L455F RBD (green) and hACE2 (blue), highlighting the positions of F455 (red) and L456 (grey) in the EG.5.1-L455F RBD

Journal: BMC Infectious Diseases

Article Title: Characterization of private mutations in the spike protein of SARS-CoV-2 correlates with viral prevalence

doi: 10.1186/s12879-025-11414-3

Figure Lengend Snippet: Complex models of the spike protein RBD with hACE2. A Structural representation of the complex between EG.5.1 RBD (yellow) and hACE2 (purple), highlighting the positions of L455 (red) and L456 (grey) in the EG.5.1 RBD. B Structural representation of the complex between EG.5.1-L455F RBD (green) and hACE2 (blue), highlighting the positions of F455 (red) and L456 (grey) in the EG.5.1-L455F RBD

Article Snippet: Recombinant Human ACE2 Protein (His & AVI Tag), Biotinylated (Sino Biological, Beijing, China), and SARS-CoV-2 EG.5.1 spike-L455F (synthesized by Sino Biological, Beijing, China) were tested for molecular interactions at concentrations of 500nM, 250nM, 125nM, 62.5nM and 31.25nM, respectively.

Techniques: