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The Respiratory Syncytial Virus (RSV) fusion (F) protein is a critical surface glycoprotein that mediates viral penetration by fusing the viral envelope with the host cell plasma membrane. In the Memphis 37b strain, which is frequently utilized in human clinical challenge models, the F protein serves as the primary target for both naturally occurring neutralizing antibodies and therapeutic interventions. The protein exists in two distinct conformational states: a metastable pre-fusion (preF) form and a stable post-fusion (postF) form. Modern therapeutic strategies, including monoclonal antibodies like nirsevimab and recently approved vaccines, specifically target the highly immunogenic pre-fusion conformation to prevent viral entry. Because the F protein is highly conserved across RSV subgroups, it remains the most viable target for preventing severe lower respiratory tract infections, such as bronchiolitis and pneumonia, in infants and older adults.
Neutralization of viral infectivity by binding to the F protein and preventing the conformational change from the metastable pre-fusion state to the stable post-fusion state, thereby inhibiting the fusion of viral and host cell membranes.
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