In this chapter we review the structure and function of the RSV surface glycoproteins, including recent X-ray crystallographic data of the F glycoprotein in its pre- and postfusion conformations, and discuss how this information informs antigen selection and vaccine development.

May 8, 2019 · RSV F is a class I fusion protein that mediates fusion of the viral membrane with a host-cell membrane, a process that poses an otherwise insurmountable energetic barrier to viral entry.

Fusion glycoprotein F0 of the human respiratory syncytial virus (RSV) is a critical fusion glycoprotein that facilitates entry of the virus into host cells by mediating the fusion of the viral and cellular membranes.

The RSV genome encodes for 11 proteins of which the type I integral membrane fusion protein (F‐protein) plays a pivotal role in the pathogenesis of RSV by mediating the fusion between the viral and the host cell membrane (Barretto et al, 2003; Collins 2007; Levine et …

Mar 19, 2024 · RSV has a characteristic fusion protein (F protein) on its surface, facilitating its entry into host cells. RSV is primarily transmitted through respiratory droplets, which are expelled when an infected person coughs or sneezes.

Sep 24, 2019 · Respiratory syncytial virus (RSV) is a major cause of severe respiratory disease in the very young, elderly, and immunocompromised for which there is no vaccine. The surface exposed RSV fusion (F) glycoprotein is required for membrane fusion and infection and is a desirable vaccine candidate.

Human respiratory syncytial virus (RSV) is one of the most important causes of severe respiratory tract infections in early childhood. The only prophylactic protection is the neutralizing antibody, palivizumab, which targets a conformational epitope of the RSV fusion (F) protein.

Vaccines use the RSV fusion (F) protein as an immunogen, but the protein is flexible and locking it in its “prefusion” conformation allows the immune system to build a response that is most beneficial for neutralizing RSV infection.

Jun 7, 2021 · This latter class of nAbs recognizes an epitope located between Site Ø, Site II, and Site V on the F-protein, identifying an important site of pathogen vulnerability. Keywords: RSV; functional antibody repertoire; human monoclonal antibodies; vaccine development.

In this chapter, we review the structure and function of the RSV surface glycoproteins, including recent X-ray crystallographic data of the F glycoprotein in its pre- and postfusion conformations, and discuss how this information informs antigen selection and vaccine development.