Endothelial Galectin-1 Binds to Specific Glycans on Nipah Virus Fusion Protein and Inhibits Maturation, Mobility, and Function to Block Syncytia Formation
Figure 7
The F3 glycan is critical for galectin-1 inhibition of NiV-F maturation and function.
A, The F3 mutant (NiV-F missing the F3 glycan) is resistant to galectin-1 inhibition of syncytia formation in endothelial and glial cells, using the heterologous cell fusion assay described in Fig. 1. PK13 cells expressing NiV-G and either wildtype NiV-F (white) or NiV-F lacking the F3 glycan (black) were added to indicated cells in the presence of galectin-1 (HUVEC, 10µM; U87, 20µM). The y-axis shows percent inhibition of fusion. Data are mean ± SD of triplicate samples from one of three replicate experiments. * p = 0.0001, calculated using unpaired Student's t test. B, The F3 glycan on NiV-F is critical for galectin-1 inhibition of NiV-F0 internalization. Cells transfected with NiV-F3 (lacking the F3 glycan) were cell surface biotinylated and incubated in the presence of galectin-1 (20µM) (bold line), or buffer control (dashed line), for the indicated times to allow internalization. Internalized NiV-F3 was quantified as in Fig. 4. Data are mean ± SEM for seven replicate experiments.