Tick-borne encephalitis virus (TBEV), a member of flaviviruses, represents a serious health threat by causing human encephalitis mainly in central and eastern Europe, Russia, and northeastern Asia. As no specific therapy is available, there is an urgent need to understand all steps of the TBEV replication cycle at the molecular level. One of the critical events is the packaging of flaviviral genomic RNA by TBEV C protein to form a nucleocapsid. We purified recombinant TBEV C protein and used a combination of physical-chemical approaches, such as size-exclusion chromatography, circular dichroism, NMR spectroscopies, and transmission electron microscopy, to analyze its structural stability and its ability to dimerize/oligomerize. We compared the ability of TBEV C protein to assemble in vitro into a nucleocapsid-like structure with that of dengue C protein.
- MeSH
- cirkulární dichroismus MeSH
- gelová chromatografie MeSH
- koncentrace vodíkových iontů MeSH
- magnetická rezonanční spektroskopie MeSH
- nukleokapsida chemie metabolismus MeSH
- rekombinantní proteiny chemie genetika izolace a purifikace MeSH
- virové proteiny chemie genetika izolace a purifikace metabolismus MeSH
- virus dengue chemie MeSH
- viry klíšťové encefalitidy chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
This work is dedicated to the study of the variability of the main antigenic envelope protein E among different strains of tick-borne encephalitis virus at the level of physical and chemical properties of the amino acid residues. E protein variants were extracted from then NCBI database. Four amino acid residues properties in the polypeptide sequences were investigated: the average volume of the amino acid residue in the protein tertiary structure, the number of amino acid residue hydrogen bond donors, the charge of amino acid residue lateral radical and the dipole moment of the amino acid residue. These physico-chemical properties are involved in antigen-antibody interactions. As a result, 103 different variants of the antigenic determinants of the tick-borne encephalitis virus E protein were found, significantly different by physical and chemical properties of the amino acid residues in their structure. This means that some strains among the natural variants of tick-borne encephalitis virus can potentially escape the immune response induced by the standard vaccine.
- MeSH
- aminokyseliny chemie MeSH
- antigeny virové chemie imunologie metabolismus MeSH
- chemické jevy MeSH
- proteiny virového obalu chemie imunologie metabolismus MeSH
- protilátky virové metabolismus MeSH
- vazba proteinů MeSH
- viry klíšťové encefalitidy chemie imunologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- MeSH
- antigeny analýza MeSH
- fluorescenční protilátková technika MeSH
- interferony biosyntéza MeSH
- kultivace virů MeSH
- kultivační techniky MeSH
- kuřecí embryo MeSH
- myši MeSH
- replikace viru MeSH
- věkové faktory MeSH
- viry klíšťové encefalitidy chemie metabolismus patogenita MeSH
- zvířata MeSH
- Check Tag
- kuřecí embryo MeSH
- myši MeSH
- zvířata MeSH