FIGURE 2
FROM:
The Influence of Blood on In Vivo Adenovirus Bio-distribution and Transduction
Andrew H Baker, John H Mcvey, Simon N Waddington, Nelson C Di Paolo and Dmitry M Shayakhmetov
BACK TO ARTICLEFigure 2.

Structural homology between coagulation factors and Ad5 binding. (a) Molecular model of the serine protease (blue), epidermal growth factor (EGF)-like (red), and Gla (cyan) domains of human FVIIa. The location of the calcium ions is indicated by green spheres. The active site inhibitor is represented by ball and stick. (b) Alignments of human Gla-EGF1-EGF2-serine protease amino acid sequences were generated using ClustalW and edited in BioEdit (http://www.mbio.ncsu.edu/BioEdit/bioedit.html/). The Gla (cyan), EGF-like (red), and serine protease (blue) domains are indicated by the colored bars. (c) Surface plasmon resonance analysis of FX–adenovirus interactions. AdKO1 1011 virus particles/ml was perfused over FX, and FXI was immobilized onto a CM5-sensor chip in 50 mmol/l Tris pH 7.4; 150 mmol/l NaCl; 5 mmol/l CaCl2; 0.005% Tween 20 at a flow rate of 20
l/minute at 25°C. Depicted are sensorgrams demonstrating FX specific binding (purple trace) following injection of AdKO1. No binding to the FXI channel is observed (green trace). Injection of 3 mmol/l ethylenediaminetetraacetic acid (EDTA) dissociates the virus from the FX, indicating that this is a calcium-dependent interaction. RU, response units.
