Respiratory syncytial virus (RSV) is the most common cause of acute lower respiratory infection among children worldwide and the leading cause of infant hospitalization for respiratory disease in developed countries. RSV invades host cells via a type I fusion (F) glycoprotein that undergoes dramatic structural rearrangements during the fusion process. Neutralizing monoclonal antibodies, such as 101F, palivizumab, and motavizumab, target two major antigenic sites on the RSV F glycoprotein. The structures of these sites as peptide complexes with motavizumab and 101F have been previously determined, but a structure for the trimeric RSV F glycoprotein ectodomain has remained elusive. Crystal structures of related parainfluenza F glycoproteins have revealed a large conformational change between the prefusion and postfusion states.
RSV Fusion Glycoprotein Realtime-3D Biologic Explorer
Use the interactive realtime 3D Biologic Explorer to visualize the internal anatomy and dynamic shape changes of the RSV Fusion Glycoprotein. (Best viewed in a full-screen desktop browser).
3D Print RSV Fusion F Glycoprotein
3D printed protein models of RSV Fusion F Glycoprotein visualize the conformational changes of this viral protein during membrane fusion. Each chain is colored uniquely, with one chain colored blue to red from N to C-Terminal. Using the interface below, configure the scale and materials using the horizontal slider and drop-down menu. Created from PDB ID: 5TDL, 3RRR