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The Respiratory syncytial virus (RSV) fusion (F) glycoprotein in its prefusion conformation is a critical target for preventing RSV infection (McLellan et al., Science, 2013). As a class I viral fusion protein, it undergoes a dramatic structural rearrangement to facilitate the fusion of the viral and host cell membranes (Graham, Science, 2017). The prefusion state (PreF) is highly metastable but displays the most potent neutralizing epitopes, such as Site Ø, which are absent in the postfusion form (O'Dell et al., Journal of Virology, 2021). Modern therapeutic strategies, including the development of stabilized recombinant vaccines like Arexvy and Abrysvo, and monoclonal antibodies like nirsevimab, specifically target these prefusion epitopes to block viral entry effectively (FDA, 2023). This target is central to protecting vulnerable populations, including infants and older adults, from severe lower respiratory tract disease caused by RSV (CDC, 2024).
Neutralization of viral entry by binding to the prefusion conformation of the F protein, thereby preventing the structural transition to the postfusion state required for membrane fusion (FDA, 2023).
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