ISSN: 1948-5964
+44 1300 500008
Boivin G, Hamelin ME, Bouhy X, Trauger R and Moss R
Respiratory syncytia virus (RSV) infection is a common respiratory infection in infants and children for which there is a need for new therapies. Viral attachment appears to be mediated by interaction of the G protein with negatively charged carbohydrates such as glycosaminoglycans (GAGs) on the cell surface. DAS181 is a bifunctional fusion protein comprised of a sialidase linked to a polycationic sequence derived from human amphiregulin (hAR) that allows the molecule to target the sialidase enzymatic activity to GAGs. Based on the ability of DAS181 to bind to cell-surface GAGs we investigated whether DAS181 might interrupt RSV infection of Hep-2 cells by virtue of its unique hAR sequence. We report here that pre-exposure of Hep-2 cells to DAS181 appears to block infectivity of RSV of Hep-2 cells with an estimated IC50 value of 13.40 μM (p=0.009). In comparison, ribavirin exhibited an IC50 of 44.55 μM (p=0.004) under the same conditions. These data suggest that the expression of the hAR sequence may be sufficient to block RSV infection of Hep-2 cells and thus may provide a novel approach to target RSV infection.