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The Tick-borne encephalitis virus (TBEV) envelope protein (E protein) is the primary surface glycoprotein of the TBEV virion and serves as the major target for neutralizing antibodies. It is a class II viral fusion protein organized as antiparallel dimers on the mature virus surface, consisting of three distinct structural domains: Domain I (DI), Domain II (DII), and Domain III (DIII). The E protein is responsible for critical steps in the viral life cycle, including attachment to host cell receptors and low-pH-triggered membrane fusion within endosomes. Vaccine-induced polyclonal antibodies, such as those generated by the FSME-IMMUN and Encepur vaccines, primarily recognize epitopes within Domain II, whereas natural infection often elicits a more potent response against Domain III. Therapeutic strategies targeting this protein include inactivated whole-virus vaccines and passive immunization with TBE-specific immunoglobulins to prevent or neutralize infection.
Neutralization of viral entry and inhibition of membrane fusion by binding to surface epitopes, thereby preventing the virus from infecting host cells and inducing a protective humoral immune response.
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