Elucidating conserved interactions between viral glycoproteins and cellular factors

Viral glycoproteins are found on the surface of all enveloped viruses, mediating binding to host receptors and the initiation of entry events. In addition, numerous vaccines employ the same viral glycoproteins as immunogens, either vectored or recombinant in nature. During infection viral glycoproteins are thought to interact with various host-factors, facilitating their trafficking to the cell surface. However, these interactions are not currently well understood or characterised. Using a human gene expression microarray, the cellular response to expression of various viral glycoproteins (Ebola, Nipah, VSV and Measles) was assessed in vitro . Specifically, we found a number of genes with a fold change greater than 2 displaying significantly altered expression across all four glycoprotein transfections. A subset of these genes were selected for validation by qPCR and extended to RSV (respiratory syncytial virus) fusion protein (F) transfection. The expression of these genes was then further investigated in Measles and RSV infected cells. Our data has identified host genes with altered expression in response to a diverse panel of viral glycoproteins, potentially elucidating a conserved set of pathways important for viral glycoprotein activity. Greater understanding of the proteins and pathways involved in glycoprotein expression has the potential to identify mechanisms underpinning host susceptibility to disease as well as improving the yield of vaccine producing cells.