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The Crimean-Congo hemorrhagic fever virus glycoproteins (Gn, Gc, and GP38) are structural proteins located on the surface of the viral envelope, essential for the virus's ability to bind to host cell receptors, mediate membrane fusion, and initiate infection. Gn and Gc form heterodimers that create a lattice on the virion surface, orchestrating receptor-mediated endocytosis and driving membrane fusion via structural rearrangements, especially by Gc (a class II fusion protein). GP38 is a secreted glycoprotein unique to CCHFV, structurally related to Gn, and is the target of protective antibodies that can prevent infection in animal models, making it a promising candidate for vaccine or immunotherapeutic development. These glycoproteins are critical therapeutic targets due to their central role in viral entry and pathogenesis, but host protein-glycoprotein interactions remain incompletely characterized, complicating therapeutic strategies.
Neutralizing antibodies (e.g., targeting GP38 or Gc) inhibit viral attachment, membrane fusion, and entry into host cells Antibody-mediated immune clearance
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