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The envelope glycoprotein (E protein) of the tick-borne encephalitis virus (TBEV) is the major surface protein and a critical component of the mature virion. It plays essential roles in viral entry, membrane fusion, receptor binding, and induction of protective immunity. The E glycoprotein consists of 496 amino acid residues organized into four domains: Domain I (central β-barrel), Domain II (elongated/fusion loop/dimerization interface), Domain III (Ig-like fold), and the Stem-anchor region. It is glycosylated at Asn154. The E protein mediates attachment to host cell receptors and triggers low-pH-induced fusion between viral and endosomal membranes. It undergoes conformational changes ("virus breathing") influencing antibody accessibility and is a major target for neutralizing antibodies.
Viral entry inhibition (potential target for antivirals)
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