Figure 1 : Purified Tulane virus (TV) virions interact with some synthetic sialoglycoconjugates (SGCs) in ELISA-based binding assays.

From: Tulane virus recognizes sialic acids as cellular receptors

Figure 1

Cesium chloride gradient-purified TV virions (1 × 104 PFU/mL) were coated on microtiter plates and incubated with various synthetic SGCs or oligosaccharides (1 μg/mL, X-axis), including N-acetylneuraminic acid (Neu5Ac), N-glycolylneuraminic acid (Neu5Gc), 3’-sialylactose, 6’-sialyllacNAc, type A disaccharide (GalNAc-α1-3-Gal), and type B trisaccharide. All of these SGCs and oligosaccharides are linked to polyacrylamide (PAA) and biotinylated. The bound SGCs and oligosaccharides were detected by streptavidin-horseradish peroxidase (HRP) conjugates. Binding signals were shown as optical density (OD450, Y-axis). Neu5Gc, 3’-sialylactose, and type A disaccharide were negative controls, while type B trisaccharide and the interaction between Neu5Ac and the recombinant HA protein (10 μg/mL, coated on plate) of an H3N1 influenza virus (Neu5Ac-HA) were positive controls. The binding of the cell lysate without TV with Neu5Ac (Neu5Ac-cell lysate) or 6’-sialyllacNAc (6’-sialyllacNAc-cell lysate) are also negative controls. A dashed line indicates the signal cutoff of 0.1. Each binding experiment was repeated at least four times. The statistical differences between the binding results and the negative control (Neu5Gc) are indicated.