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Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of <t>bNAbs</t> <t>CR6261</t> ( D ), <t>CR9114</t> ( E ), and <t>FI6v3</t> ( F ). Structure 3UBE was used for modeling .
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Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .

Journal: Viruses

Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

doi: 10.3390/v18010032

Figure Lengend Snippet: Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .

Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

Techniques: Binding Assay

Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.

Journal: Viruses

Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

doi: 10.3390/v18010032

Figure Lengend Snippet: Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.

Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

Techniques: Binding Assay, Virus, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison

Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.

Journal: Viruses

Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

doi: 10.3390/v18010032

Figure Lengend Snippet: Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.

Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison