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Characterization and in vitro assembly of tick-borne encephalitis virus C protein
F. Kaufman, A. Dostálková, L. Pekárek, TD. Thanh, M. Kapisheva, R. Hadravová, L. Bednárová, R. Novotný, I. Křížová, J. Černý, L. Grubhoffer, T. Ruml, R. Hrabal, M. Rumlová
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Wiley Free Content od 1997 do Před 1 rokem
Elsevier Open Archive Journals od 1968-07-01 do Před 1 rokem
Odkazy
PubMed
32510601
DOI
10.1002/1873-3468.13857
Knihovny.cz E-zdroje
- 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
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.
Department of Biotechnology University of Chemistry and Technology Prague Prague Czech Republic
Faculty of Science University of South Bohemia České Budějovice Czech Republic
Faculty of Tropical AgriSciences Czech University of Life Sciences Prague Prague Czech Republic
Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czech Republic
NMR Laboratory University of Chemistry and Technology Prague Prague Czech Republic
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- $a 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.
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