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Open AccessArticle

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

1
Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, IOCB Gilead Research Center, 16000 Prague, Czech Republic
2
Department of Genetics and Microbiology, Faculty of Science, Charles University, BIOCEV, 25250 Vestec, Czech Republic
3
Institute of Molecular Genetics of the Czech Academy of Sciences, 14220 Prague, Czech Republic
*
Author to whom correspondence should be addressed.
Cells 2020, 9(12), 2547; https://doi.org/10.3390/cells9122547
Received: 30 September 2020 / Revised: 19 November 2020 / Accepted: 24 November 2020 / Published: 26 November 2020
(This article belongs to the Special Issue Hepatitis B Virus and Host Interactions)
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. View Full-Text
Keywords: hepatitis B virus; HBc; post-translational modifications; ubiquitination; ubiquitin; E3 ubiquitin-protein ligase hepatitis B virus; HBc; post-translational modifications; ubiquitination; ubiquitin; E3 ubiquitin-protein ligase
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    Doi: 10.6019/PXD021712
    Link: http://proteomecentral.proteomexchange.org/cgi/GetDataset?ID=PXD021712
    Description: "The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD021712 and 10.6019/PXD021712". Project accession: PXD021712 Project DOI: 10.6019/PXD021712 Reviewer account details: Username: [email protected] Password: QUzED2S3
MDPI and ACS Style

Langerová, H.; Lubyová, B.; Zábranský, A.; Hubálek, M.; Glendová, K.; Aillot, L.; Hodek, J.; Strunin, D.; Janovec, V.; Hirsch, I.; Weber, J. Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination. Cells 2020, 9, 2547.

AMA Style

Langerová H, Lubyová B, Zábranský A, Hubálek M, Glendová K, Aillot L, Hodek J, Strunin D, Janovec V, Hirsch I, Weber J. Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination. Cells. 2020; 9(12):2547.

Chicago/Turabian Style

Langerová, Hana; Lubyová, Barbora; Zábranský, Aleš; Hubálek, Martin; Glendová, Kristýna; Aillot, Ludovic; Hodek, Jan; Strunin, Dmytro; Janovec, Václav; Hirsch, Ivan; Weber, Jan. 2020. "Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination" Cells 9, no. 12: 2547.

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