FEBS Letters | |
Characterization and invitro assembly of tick-borne encephalitis virus C protein | |
article | |
Filip Kaufman1  Alžběta Dostálková1  Lukáš Pekárek1  Tung Dinh Thanh1  Marina Kapisheva1  Romana Hadravová1  Lucie Bednárová2  Radim Novotný1  Ivana Křížová1  Jiří Černý4  Libor Grubhoffer5  Tomáš Ruml7  Richard Hrabal3  Michaela Rumlová1  | |
[1] Department of Biotechnology, University of Chemistry and Technology;Institute of Organic Chemistry and Biochemistry (IOCB) Research Centre & Gilead Sciences, Academy of Sciences of the Czech Republic;NMR Laboratory, University of Chemistry and Technology;Faculty of Tropical AgriSciences, Czech University of Life Sciences;Institute of Parasitology, Biology Centre, Czech Academy of Sciences;Faculty of Science, University of South Bohemia;Department of Biochemistry and Microbiology, University of Chemistry and Technology | |
关键词: assembly; C protein; DENV; flavivirus; protein-nucleic acid interaction; TBEV; | |
DOI : 10.1002/1873-3468.13857 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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