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The Respiratory syncytial virus (RSV) prefusion F glycoprotein (subgroup B) is a key surface protein that facilitates viral entry by mediating the fusion of the viral envelope with the host cell membrane (McLellan et al., 2013, Science). It is a Class I viral fusion protein that exists in a metastable prefusion (pre-F) state, which is highly immunogenic and contains potent neutralizing epitopes like Site Ø (Ngwuta et al., 2015, Science Translational Medicine). Subgroup B is one of the two major antigenic lineages of RSV, and its F protein shares approximately 90% sequence identity with subgroup A, though specific mutations can impact antibody binding (Graham, 2017, Immunological Reviews). This protein is the primary target for modern prophylactic interventions, including monoclonal antibodies like nirsevimab and bivalent vaccines like Abrysvo, which include a stabilized pre-F component from subgroup B (Hammitt et al., 2022, NEJM). By targeting the pre-F conformation, these therapies prevent the structural rearrangement into the postfusion state, effectively neutralizing the virus before it can infect respiratory epithelial cells. This target is essential for preventing severe RSV-related diseases such as bronchiolitis and pneumonia in vulnerable populations, including infants and the elderly (Falsey et al., 2005, NEJM).
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 (McLellan et al., 2013).
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