Tick-borne encephalitis virus envelope glycoprotein (TBEV E) (TBEV E)

The Tick-borne encephalitis virus (TBEV) envelope glycoprotein (E protein) is the primary surface protein of the TBEV virion and the main target for neutralizing antibodies (Heinz & Stiasny, 2012, Advances in Virus Research). It is a class II fusion protein that mediates viral attachment to host cells and subsequent membrane fusion in the endosome (Stiasny et al., 2006, Journal of Virology). The E protein is composed of three domains (DI, DII, and DIII), with DIII being a major site for the binding of potent neutralizing antibodies (Füzik et al., 2018, Nature Communications). Human B-cell receptors (BCRs) specific for these epitopes are activated during infection or vaccination to produce protective antibodies (Characterization of the human B-cell response to TBEV, 2021, Journal of Virology). This protein is the basis for all licensed TBEV vaccines, such as FSME-IMMUN and Encepur, which aim to elicit a robust B-cell response (WHO, 2011, TBE Vaccine Position Paper). Research into these BCRs has led to the identification of highly potent human monoclonal antibodies that are being explored as potential therapeutics for post-exposure prophylaxis (Füzik et al., 2018). Targeting the E protein effectively prevents the virus from entering host cells, thereby neutralizing the infection. The structural conservation of the E protein across different TBEV subtypes makes it an ideal target for broad-spectrum vaccine development.

Other names

TBEV E proteinEnvelope protein ETick-borne encephalitis virus E proteinTBEV glycoprotein E

Neutralization of viral infectivity by blocking attachment to host cells or inhibiting pH-dependent membrane fusion (Heinz & Stiasny, 2012).