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Image Search Results
Journal: Viruses
Article Title: Receptor Binding-Induced Conformational Changes in Herpes Simplex Virus Glycoprotein D Permit Interaction with the gH/gL Complex to Activate Fusion
doi: 10.3390/v15040895
Figure Lengend Snippet: Characterization of wt and cys2 proteins. ( a ) Diagram of the Biacore 3000 protocol for analyzing gH/gL binding to gD, wt or cys2. ( b ) Soluble wt 306t and cys2 306t proteins were attached to the biosensor chip via 1D3 Mab. Soluble gH/gL was injected across the chip surface. Only the gH/gL binding curves are shown. Black curve, binding of gH/gL to wt gD; brown curve, binding of gH/gL to cys2. ( c ) Diagram of the Biacore 3000 protocol for analyzing the binding of gH/gL to a gD-nectin-1 receptor complex. gD molecules were attached to the biosensor chip via 1D3 Mab. Sequential injection of nectin-1 followed by injection of soluble gH/gL. ( d ) Nectin-1 binds to both wt (dark purple) and cys2 (light purple) gD proteins. ( e ) gH/gL bound to wt gD (blue) but not to cys2 mutant gD (cyan). ( f ) Diagram of the Biacore 3000 protocol for analyzing gD–gH/gL binding in the presence of TCEP. gD molecules were attached to the biosensor chip via 1D3 Mab. Nectin-1 was pre-mixed with 1 mM TCEP and flowed over the captured gD molecules, followed by the injection of soluble gH/gL. ( g ) Nectin-1 binds to both wt (purple) and cys2 (light purple) gD proteins. ( h ) As expected, gH/gL bound to wt gD (blue). Due to the reduction of the disulfide bond, gH/gL is now able to bind cys2 mutant gD as well (cyan).
Article Snippet: To address this hypothetical model, we adapted the
Techniques: Binding Assay, Injection, Mutagenesis
Journal: Viruses
Article Title: Receptor Binding-Induced Conformational Changes in Herpes Simplex Virus Glycoprotein D Permit Interaction with the gH/gL Complex to Activate Fusion
doi: 10.3390/v15040895
Figure Lengend Snippet: Ability of gD L268N to bind gH/gL. ( a ) Diagram of the Biacore 3000 protocol for analyzing the binding of gH/gL to a gD-receptor complex. gD molecules, wt, or L268N, both as 306t truncations were attached to the biosensor chip via 1D3 Mab. Sequential injection of nectin-1 followed by injection of soluble gH/gL. ( b ) Nectin-1 binds to both wt (purple) and L268N (pink) gD proteins. ( c ) gH/gL was flowed over the gD-nectin-1 complexes. gH/gL bound to wt gD (blue) but not to L268N mutant gD (cyan). ( d ) Diagram of the SPR protocol for analyzing gH/gL binding to gD 285t , wt, or the L268N mutant. Only the gH/gL binding curves are shown. gH/L binds to wt gD (black curve). No gH/gL binding was observed for the L268N mutant (orange curve).
Article Snippet: To address this hypothetical model, we adapted the
Techniques: Binding Assay, Injection, Mutagenesis