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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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This figure depicts the effect of angiotensin II (1-8) on spike protein binding. In , the addition of angiotensin II (1-8) significantly enhanced spike-AXL binding. In contrast, and show that angiotensin II (1-8) did not significantly alter <t>spike-ACE2</t> binding and spike-NRP1 binding, respectively. combines the data in , , and to show the effect of angiotensin II (1-8) on spike protein binding across different receptors. Angiotensin II (1-8) selectively enhanced spike-AXL binding and did not influence spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.
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This figure depicts the effect of angiotensin II (1-8) on spike protein binding. In , the addition of angiotensin II (1-8) significantly enhanced spike-AXL binding. In contrast, and show that angiotensin II (1-8) did not significantly alter <t>spike-ACE2</t> binding and spike-NRP1 binding, respectively. combines the data in , , and to show the effect of angiotensin II (1-8) on spike protein binding across different receptors. Angiotensin II (1-8) selectively enhanced spike-AXL binding and did not influence spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.
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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:

This figure depicts the effect of angiotensin II (1-8) on spike protein binding. In , the addition of angiotensin II (1-8) significantly enhanced spike-AXL binding. In contrast, and show that angiotensin II (1-8) did not significantly alter spike-ACE2 binding and spike-NRP1 binding, respectively. combines the data in , , and to show the effect of angiotensin II (1-8) on spike protein binding across different receptors. Angiotensin II (1-8) selectively enhanced spike-AXL binding and did not influence spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.

Journal: bioRxiv

Article Title: Angiotensin peptides enhance SARS-CoV-2 spike protein binding to its host cell receptors

doi: 10.1101/2024.12.12.628247

Figure Lengend Snippet: This figure depicts the effect of angiotensin II (1-8) on spike protein binding. In , the addition of angiotensin II (1-8) significantly enhanced spike-AXL binding. In contrast, and show that angiotensin II (1-8) did not significantly alter spike-ACE2 binding and spike-NRP1 binding, respectively. combines the data in , , and to show the effect of angiotensin II (1-8) on spike protein binding across different receptors. Angiotensin II (1-8) selectively enhanced spike-AXL binding and did not influence spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.

Article Snippet: Recombinant human ACE2 was purchased from Sino Biological, Inc. (Wayne, PA, USA).

Techniques: Protein Binding, Binding Assay

This figure presents the effect of angiotensin IV (3-8) on spike protein binding. , , and all show that adding angiotensin IV (3-8) significantly enhanced spike-AXL binding, spike-ACE2 binding, and spike-NRP1 binding, respectively. combines the data in , , and to illustrate the effect of angiotensin IV (3-8) on spike protein binding across different receptors. Although angiotensin IV (3-8) enhanced spike-AXL binding, spike-ACE2 binding, and spike-NRP1 binding, the difference angiotensin IV (3-8)’s enhancement of spike-AXL binding and angiotensin IV (3-8)’s enhancement of spike-ACE2 binding and the difference angiotensin IV (3-8)’s enhancement of spike-AXL binding and angiotensin IV (3-8)’s enhancement of spike-NRP1 binding are significant, implying that angiotensin IV (3-8) enhanced spike-AXL binding more than it increased spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.

Journal: bioRxiv

Article Title: Angiotensin peptides enhance SARS-CoV-2 spike protein binding to its host cell receptors

doi: 10.1101/2024.12.12.628247

Figure Lengend Snippet: This figure presents the effect of angiotensin IV (3-8) on spike protein binding. , , and all show that adding angiotensin IV (3-8) significantly enhanced spike-AXL binding, spike-ACE2 binding, and spike-NRP1 binding, respectively. combines the data in , , and to illustrate the effect of angiotensin IV (3-8) on spike protein binding across different receptors. Although angiotensin IV (3-8) enhanced spike-AXL binding, spike-ACE2 binding, and spike-NRP1 binding, the difference angiotensin IV (3-8)’s enhancement of spike-AXL binding and angiotensin IV (3-8)’s enhancement of spike-ACE2 binding and the difference angiotensin IV (3-8)’s enhancement of spike-AXL binding and angiotensin IV (3-8)’s enhancement of spike-NRP1 binding are significant, implying that angiotensin IV (3-8) enhanced spike-AXL binding more than it increased spike-ACE2 binding and spike-NRP1 binding. One asterisk (*) denotes a p-value equal to or less than 0.05 and “NS” represents “not significant”.

Article Snippet: Recombinant human ACE2 was purchased from Sino Biological, Inc. (Wayne, PA, USA).

Techniques: Protein Binding, Binding Assay