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The Respiratory Syncytial Virus (RSV) F (fusion) and G (attachment) glycoproteins are the primary surface antigens of the virus and are essential for its infectivity (UniProt P03420, P03423). The G protein facilitates the initial attachment of the virus to host respiratory epithelial cells, primarily through interactions with glycosaminoglycans or the CX3CR1 receptor (PubMed: 26121444). Following attachment, the F protein undergoes a dramatic conformational rearrangement from a metastable prefusion state to a stable postfusion state, mediating the fusion of the viral envelope with the host cell membrane (PubMed: 23640626). This process allows the viral genome to enter the cytoplasm and initiate replication. These glycoproteins are the principal targets for the host's neutralizing antibody response and are the focus of modern therapeutic strategies, including monoclonal antibodies like nirsevimab and palivizumab, as well as recently approved prefusion-stabilized F protein vaccines like Arexvy and Abrysvo (FDA, 2023). Targeting these proteins aims to prevent severe lower respiratory tract infections, such as bronchiolitis and pneumonia, particularly in vulnerable populations like infants and the elderly (CDC, 2024).
Neutralization of viral particles and inhibition of viral-host membrane fusion (F-targeted) or attachment (G-targeted) to prevent viral entry and replication.
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