Tick-borne encephalitis virus polyprotein (TBEV polyprotein)

Tick-borne encephalitis virus (TBEV) peptide epitopes are specific amino acid sequences within the viral polyprotein, primarily located on the Envelope (E) protein, that are recognized by the host's B-cells and T-cells. The E protein is the major surface component of the virus and is responsible for receptor binding and membrane fusion, making its epitopes the primary targets for neutralizing antibodies (Pulkkinen et al., 2022, Viruses). While the E protein is the dominant antigen, non-structural proteins like NS1 also contain important epitopes that can trigger protective T-cell responses (Blom et al., 2018, Journal of Virology). These epitopes are the functional components of inactivated whole-virus vaccines, such as FSME-IMMUN and Encepur, which elicit long-term immunity against the virus (WHO, 2011). In a clinical context, identifying these epitopes is essential for developing high-sensitivity diagnostic assays and next-generation recombinant vaccines. The target is considered 'incorrect' as a single entity because it refers to a heterogeneous collection of peptide fragments rather than a discrete, individual molecular target.

Other names

Multiple TBEV peptide epitopesTick-borne encephalitis virus antigensTBEV E proteinTBEV structural proteinsTBEV non-structural proteins

Induction of humoral and cellular immune responses, specifically the production of neutralizing antibodies that bind to the viral envelope (E) protein to prevent host cell entry and fusion (Pulkkinen et al., 2022, Viruses).