Use of a vesicular stomatitis virus complementation system to analyze respiratory syncytial virus binding

Respiratory syncytial virus (RSV) can be difficult to manipulate in the laboratory because it produces a fragile, filamentous virion that does not bud efficiently from the cell surface and which is sensitive to purification. These properties have complicated the studies of RSV envelope protein–host cell interactions. In this paper, we have tested the ability of the RSV attachment protein, G, to complement virus attachment of a recombinant vesicular stomatitis virus (VSVΔG*), which lacks any viral attachment protein. Using an enzyme-linked immunosorbent assay (ELISA) to detect bound virus, VSVΔG* virions were shown to incorporate the RSV G protein and to bind to Hep-2 cells. Binding of RSV G protein-complemented VSVΔG* virus was inhibited by incubation with RSV-specific antibodies and by the addition of exogenous sulfated glycosaminoglycans, indicating that binding by the complemented virus exhibited the characteristics of RSV binding rather than those of VSV. These results demonstrate that complementation studies with VSVΔG* may be useful in virus–host interaction studies of the RSV G protein.