Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination

0535892 - ÚOCHB 2021 RIV CH eng J - Journal Article
Langerová, Hana - Lubyová, Barbora - Zábranský, Aleš - Hubálek, Martin - Glendová, Kristýna - Aillot, Ludovic - Hodek, Jan - Strunin, Dmytro - Janovec, Václav - Hirsch, Ivan - Weber, Jan
Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination.
Cells. Roč. 9, č. 12 (2020), č. článku 2547. E-ISSN 2073-4409
R&D Projects: GA ČR GA17-15422S; GA MŠMT(CZ) EF16_019/0000729
Institutional support: RVO:61388963
Keywords : hepatitis B virus * HBc * post-translational modifications * ubiquitination * ubiquitin * E3 ubiquitin-protein ligase
OECD category: Virology
Impact factor: 6.600, year: 2020
Method of publishing: Open access
https://doi.org/10.3390/cells9122547

Hepatitis B virus (HBV) core protein (HBc) plays many roles in the HBV life cycle, such as regulation of transcription, RNA encapsidation, reverse transcription, and viral release. To accomplish these functions, HBc interacts with many host proteins and undergoes different post-translational modifications (PTMs). One of the most common PTMs is ubiquitination, which was shown to change the function, stability, and intracellular localization of different viral proteins, but the role of HBc ubiquitination in the HBV life cycle remains unknown. Here, we found that HBc protein is post-translationally modified through K29-linked ubiquitination. We performed a series of co-immunoprecipitation experiments with wild-type HBc, lysine to arginine HBc mutants and wild-type ubiquitin, single lysine to arginine ubiquitin mutants, or single ubiquitin-accepting lysine constructs. We observed that HBc protein could be modified by ubiquitination in transfected as well as infected hepatoma cells. In addition, ubiquitination predominantly occurred on HBc lysine 7 and the preferred ubiquitin chain linkage was through ubiquitin-K29. Mass spectrometry (MS) analyses detected ubiquitin protein ligase E3 component N-recognin 5 (UBR5) as a potential E3 ubiquitin ligase involved in K29-linked ubiquitination. These findings emphasize that ubiquitination of HBc may play an important role in HBV life cycle.
Permanent Link: http://hdl.handle.net/11104/0313857