Tick-borne encephalitis virus (TBEV) is a member of the virus family Flaviviridae, genus Flavivirus. TBEV infection causes the tick-borne encephalitis (TBE), a virus infectious disease affecting humans in Europe and Asia. TBE often manifests as encephalitis, meningitis, or meningoencephalitis. TBE can also cause mild fever in some cases. It has become a notifiable disease in 16 European countries. Mortality rate of TBE is 1% to 2%. The death often happens about one week after the onset of neurologic signs. TBEV now is known to infect multiple hosts including ruminants, carnivores, birds, rodents, horses and humans, and the TBE disease can be zoonotic too. The principal source of infection for humans is dogs and ruminants.
Fig. 1 Transmission of tick-borne encephalitis virus within the life cycle of I. ricinus (K. L. Mansfield et al. Journal of General Virology. 2009)
TBEV is a small, lipid-enveloped virus with a diameter of 40-60 nm, as well as other members of Flavivirus. The TBEV genome is a single-stranded, positive-sense RNA with a length of approximately 11 kb, containing a 5' cap which is important for the stability and translation of mRNA. TBEV genome lacks of polyadenylate tail and contains a single open reading fragment (ORF). This ORF encodes all the TBEV viral proteins including three structural proteins- the large enveloped glycoprotein (protein E), the membrane protein M (which are formed by cleavage from its precursor prM), the capsid protein C- and seven nonstructural protein- NS1 (glycoprotein), NS2A, NS2B (protease component), NS3 (protease, helicase and NTPase activity), NS4A, NS4B and NS5 (RNA-dependent polymerase). 5' and 3' ends or the TBEV genome are just non-coding regions.
Fig. 2 Tick-borne encephalitis virus particles
TBEV protein E have been studied in many researches, it is known to exist as flat dimers and is believed to play an important role in the formulation of TBEV virion. It also has the ability to form enveloped recombinant subviral particles (RSPs) together with prM. As well as other Flaviviruses, TBEV NS3 protein is multifunctional, its C-terminal region have both nucleoside triphosphatase (NTPase) and helicase activities, while the N-terminal region of NS3 protein possesses a protease activity, which is critical for post-translational cleavage of the viral polyprotein precurser. The NS5 protein consists of two domains: the C-terminal domain and the N-terminal domain. The C-terminal domain is identified as a RNA-dependent RNA polymerase (RdRp), and the N-terminal domain is recognized as a methyltransferase core that enables NS5 to exhibit the (nucleoside-2'-O-)-methyltransferase activity required for methylation of the cap structure at the 5' end of the RNA genome.
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