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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

. 2020 ; 594 (12) : 1989-2004. [pub] -

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc21020488

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.

Citace poskytuje Crossref.org

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$a Tick-borne encephalitis virus (TBEV), a member of flaviviruses, represents a serious health threat by causing human encephalitis mainly in central and eastern Europe, Russia, and northeastern Asia. As no specific therapy is available, there is an urgent need to understand all steps of the TBEV replication cycle at the molecular level. One of the critical events is the packaging of flaviviral genomic RNA by TBEV C protein to form a nucleocapsid. We purified recombinant TBEV C protein and used a combination of physical-chemical approaches, such as size-exclusion chromatography, circular dichroism, NMR spectroscopies, and transmission electron microscopy, to analyze its structural stability and its ability to dimerize/oligomerize. We compared the ability of TBEV C protein to assemble in vitro into a nucleocapsid-like structure with that of dengue C protein.
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$a Dostálková, Alžběta $u Department of Biotechnology, University of Chemistry and Technology, Prague, Prague, Czech Republic $7 xx0267672
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$a Pekárek, Lukáš $u Department of Biotechnology, University of Chemistry and Technology, Prague, Prague, Czech Republic
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$a Bednárová, Lucie $u Institute of Organic Chemistry and Biochemistry (IOCB) Research Centre & Gilead Sciences, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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$a Křížová, Ivana $u Department of Biotechnology, University of Chemistry and Technology, Prague, Prague, Czech Republic
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$a Černý, Jiří $u Faculty of Tropical AgriSciences, Czech University of Life Sciences, Prague, Prague, Czech Republic
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$a Grubhoffer, Libor $u Institute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice, Czech Republic $u Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic
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$a Ruml, Tomáš $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Prague, Czech Republic
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$a Hrabal, Richard $u NMR Laboratory, University of Chemistry and Technology, Prague, Prague, Czech Republic
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$a Rumlová, Michaela $u Department of Biotechnology, University of Chemistry and Technology, Prague, Prague, Czech Republic
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