Skip to main content
. 2009 Jan 16;284(3):1628–1635. doi: 10.1074/jbc.M807469200

FIGURE 1.

FIGURE 1.

Enhanced binding of Mab45 to NiV-G (G) induced by ephrinB2 (B2) receptor binding. A, polyclonal (806) and monoclonal (Mab26 and Mab45) anti-NiV-G antibodies binding to full-length NiV-G expressed in CHOpgsA745 (CHO) cells in the presence or absence of soluble B2 protein at room temperature (∼20 °C) as detected by flow cytometry. % normalized binding indicates MFI values normalized to the MFI values obtained in the absence of soluble B2 (set at 100% for each antibody examined). Average ± S.E. are shown, n = 3. B, similar experiment to A, except performed at 4 °C. C, binding of Mab45 to CHO cells expressing G or mutant E533Q at 37 °C when increasing concentrations of soluble ephrinB1 (B1), ephrinB2 (B2), or ephrinB3 (B3) were used. Logarithm of the molar concentration of the soluble ephrinBs used was plotted against % normalized binding, calculated as in A. Average ± S.E. are shown, n = 4. D, the inhibitory properties of 806, Mab26, or Mab45 antibodies were measured by mixing the indicated concentrations with NiV/vesicular stomatitis virus renilla luciferase pseudotyped particles immediately before infection of Vero cells. Data are shown as % inhibition normalized to luciferase activity in the absence of any antibodies. Average ± S.E. are shown; n = 3.