Tick-borne encephalitis virus envelope, membrane, and capsid protein (TBEV E, M, and C protein)

The Tick-borne encephalitis virus (TBEV) is a member of the Flavivirus genus. Its structural proteins include: - The envelope protein (E), a surface glycoprotein responsible for viral attachment to host cells and mediating fusion between viral and host membranes. The E protein is the principal target of neutralizing antibodies and critical for vaccine development; its structure includes four domains, with domain III implicated in receptor binding and domain II containing the fusion loop[3][4][7]. - The membrane protein (M), produced by proteolytic cleavage of prM, acts as a scaffold during virion assembly. M interacts with E protein to regulate the fusion-competent state and supports virion maturation[4][7]. - The capsid protein (C) binds and packages the viral RNA, forming the nucleocapsid. It mediates RNA recruitment, enables nucleocapsid–membrane contact during virion assembly, and can affect host cell function by modulating nuclear processes[1][2]. Together, these proteins mediate virion formation, protect the genome, promote infectivity, and determine host and tissue tropism. They are highly conserved among flaviviruses and are primary targets for therapeutic antibodies and vaccine design[3][4][7].

Other names

TBEV E protein (Envelope glycoprotein E)TBEV M protein (Membrane protein)TBEV C protein (Capsid protein)

Neutralizing antibodies bind E protein to block viral entry or membrane fusion[7]. Small molecules may interfere with envelope-mediated fusion or assembly. Inhibitors can block proper folding or cleavage of prM-M or E, preventing maturation and infectivity[4][6].