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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00535892" target="_blank" >RIV/61388963:_____/20:00535892 - isvavai.cz</a>

Alternative codes found

RIV/68378050:_____/20:00540950 RIV/00216208:11310/20:10421426

Result on the web

<a href="https://doi.org/10.3390/cells9122547" target="_blank" >https://doi.org/10.3390/cells9122547</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/cells9122547" target="_blank" >10.3390/cells9122547</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10607 - Virology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Cells

ISSN

2073-4409

e-ISSN

—

Volume of the periodical

9

Issue of the periodical within the volume

12

Country of publishing house

CH - SWITZERLAND

Number of pages

21

Pages from-to

2547

UT code for WoS article

000601789500001

EID of the result in the Scopus database

2-s2.0-85097038179