%0 Journal Article %A Avadhanula, Vasanthi %A Wang, Yan %A Portner, Allen %A Adderson, Elisabeth %T Nontypeable Haemophilus influenzae and Streptococcus pneumoniae bind respiratory syncytial virus glycoprotein %D 2007 %J Journal of Medical Microbiology, %V 56 %N 9 %P 1133-1137 %@ 1473-5644 %R https://doi.org/10.1099/jmm.0.47086-0 %K NTHi, nontypeable Haemophilus influenzae %K GFP, green fluorescent protein %K CHO, Chinese hamster ovary %I Microbiology Society, %X Respiratory syncytial virus (RSV) infection is associated with secondary bacterial infections caused by nontypeable Haemophilus influenzae (NTHi) and Streptococcus pneumoniae. The pathogenesis of these complications is not completely understood; however, viral infection of respiratory epithelial cells promotes colonization by these bacteria. In the present study, RSV virions associated with NTHi and pneumococci in an inoculum-dependent manner in a fluid-phase binding assay. Adherence of NTHi and S. pneumoniae to epithelial cells transiently expressing RSV G glycoprotein was 2- and 2.2-fold higher, respectively, than adhesion to cells transfected with the vector alone (P <0.01). Furthermore, 4.6- and 6.2-fold larger numbers of NTHi and pneumococci bound to cells expressing a membrane-bound full-length RSV G protein than to cells expressing a truncated non-membrane-bound protein (P ≤0.005). Pre-incubating cells expressing membrane-bound G protein with blocking anti-RSV G antibodies reduced bacterial adherence by 78–84 % (P ≤0.005). These studies demonstrate that RSV G protein is a receptor for both NTHi and S. pneumoniae. Strategies to prevent this interaction may reduce the incidence of secondary bacterial complications of RSV infection. %U https://www.microbiologyresearch.org/content/journal/jmm/10.1099/jmm.0.47086-0