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The **mumps virus fusion glycoprotein F, prefusion-stabilized** (canonical abbreviation: Mumps F [Pre-F]) is an envelope surface glycoprotein of mumps virus, specifically engineered and stabilized in its metastable prefusion conformation for structural and immunogenic optimization as a vaccine antigen. This protein, naturally present as a type I viral fusion protein, mediates the merging of viral and host cell membranes via a large, conformational rearrangement from a prefusion trimer to a postfusion six-helix bundle, thereby enabling viral entry. Stabilizing the protein in the prefusion conformation enhances the exposure of potent neutralizing epitopes and elicits stronger protective antibody responses compared to postfusion forms. The prefusion form is a leading target for next-generation mumps vaccines and potent neutralizing monoclonal antibodies, as well as a molecular probe for immune studies. No direct-acting small molecule drugs target this protein, but various neutralizing antibody epitopes have been structurally defined.
Neutralizing antibodies bind prefusion-specific epitopes, block conformational change needed for membrane fusion Fusion inhibitors stabilize prefusion form or prevent transition to postfusion state
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