In several well characterized paramyxoviruses, membrane fusion is initiated by a protein complex that involves the respective virus fusion and attachment proteins. In these viruses, the binding of the attachment protein to the cell surface receptor induces a conformational change in the F protein, which in turn mediates membrane fusion (reviewed in [8] and [9]). In the case of RSV, no convincing evidence for an association between its fusion and attachment
SCH900776 has been demonstrated, and the trigger that initiates membrane fusion is still not understood. As a consequence, biochemical mechanisms have been proposed to explain how the F protein is able to mediate membrane fusion without the aid of other virus
proteins (e.g. [10]). In this report, we provide the first direct evidence that the RSV F and G proteins are able to interact to form a protein complex on the surface of virus particles. This implies that the RSV fusion process may be similar to that reported for other paramyxoviruses, and suggests the G protein may play an ancillary role in the virus-mediated membrane fusion process.
