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The Crimean-Congo hemorrhagic fever virus glycoproteins, primarily Gn and Gc, are envelope proteins mediating viral interaction with host cells, including cell attachment, entry via receptor-mediated endocytosis, and membrane fusion. Gc is a class II fusion protein whose conformational changes are essential for viral entry. GP38 is a secreted glycoprotein found uniquely in CCHFV, targeted by protective human antibodies, and serves as an immunogen for vaccine development. The glycoproteins form heterodimeric or multimeric structures on the virion surface and interact with host proteins to facilitate infection and immune modulation. These proteins are the primary focus for antiviral drug and vaccine development, with neutralizing antibodies against Gc and GP38 showing protective effects in preclinical models.
Neutralizing antibodies block viral attachment, entry, and fusion (anti-Gc, anti-GP38) Inhibition of glycoprotein conformational changes required for membrane fusion Disruption of glycoprotein function via host factors (e.g., HAX1 sequestering Gn and blocking virion assembly)
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