Host-pathogen interactions during hepatitis B virus infection

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00645520" target="_blank" >RIV/61388963:_____/25:00645520 - isvavai.cz</a>

Výsledek na webu

<a href="https://hdl.handle.net/11104/0375312" target="_blank" >https://hdl.handle.net/11104/0375312</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Host-pathogen interactions during hepatitis B virus infection

Popis výsledku v původním jazyce

Hepatitis B virus (HBV) is a human pathogen that causes serious liver diseases including hepatocellular carcinoma. While vaccination effectively prevents new infections, there is a need for improved therapies for chronic HBV. To develop novel effective treatments, it is crucial to understand the interactions between the virus and the host cells. We aimed to identify HBV-induced proteomic changes in human hepatocytes following in vitro infection and to identify host factors that regulate HBV replication. We used label-free differential proteomics and data-independent acquisition mass spectrometry to quantify proteins in naïve and HBV-infected primary human hepatocytes (PHH) and corresponding culture fluids. We used the selective HBV entry inhibitor bulevirtide to distinguish specific viral effects from non-specific inoculum effects. To analyze the role of selected cellular proteins in HBV replication, we evaluated the effect of RNA silencing on HBV infection in human hepatoblastoma HepG2-NTCP cells, primary human hepatocytes and HepG2.2.15 cells—a subclone of HepG2 cells that stably express the hepatitis B virus. We have quantified over 5900 proteins and identified HBV-induced proteomic changes after HBV infection in vitro. We found that the majority of changes can be attributed to non-viral components of the inoculum and identified protein changes induced by the productive HBV infection. We also analyzed how the secretory carrier membrane proteins (SCAMP) regulate HBV infection. The SCAMP protein family consists of proteins involved in the regulation of membrane trafficking processes. Silencing of SCAMP3 significantly reduced HBV RNA production and antigen secretion in HepG2-NTCP and PHH cells but had no effect in HepG2.2.15 cells. These results suggest that SCAMP3 is involved in early infection.nThis work was supported by the project National Institute of Virology and Bacteriology (Programme EXCELES, ID Project No. LX22NPO5103) – Funded by the European Union – NextGenerationEU.

Název v anglickém jazyce

Host-pathogen interactions during hepatitis B virus infection

Popis výsledku anglicky

Hepatitis B virus (HBV) is a human pathogen that causes serious liver diseases including hepatocellular carcinoma. While vaccination effectively prevents new infections, there is a need for improved therapies for chronic HBV. To develop novel effective treatments, it is crucial to understand the interactions between the virus and the host cells. We aimed to identify HBV-induced proteomic changes in human hepatocytes following in vitro infection and to identify host factors that regulate HBV replication. We used label-free differential proteomics and data-independent acquisition mass spectrometry to quantify proteins in naïve and HBV-infected primary human hepatocytes (PHH) and corresponding culture fluids. We used the selective HBV entry inhibitor bulevirtide to distinguish specific viral effects from non-specific inoculum effects. To analyze the role of selected cellular proteins in HBV replication, we evaluated the effect of RNA silencing on HBV infection in human hepatoblastoma HepG2-NTCP cells, primary human hepatocytes and HepG2.2.15 cells—a subclone of HepG2 cells that stably express the hepatitis B virus. We have quantified over 5900 proteins and identified HBV-induced proteomic changes after HBV infection in vitro. We found that the majority of changes can be attributed to non-viral components of the inoculum and identified protein changes induced by the productive HBV infection. We also analyzed how the secretory carrier membrane proteins (SCAMP) regulate HBV infection. The SCAMP protein family consists of proteins involved in the regulation of membrane trafficking processes. Silencing of SCAMP3 significantly reduced HBV RNA production and antigen secretion in HepG2-NTCP and PHH cells but had no effect in HepG2.2.15 cells. These results suggest that SCAMP3 is involved in early infection.nThis work was supported by the project National Institute of Virology and Bacteriology (Programme EXCELES, ID Project No. LX22NPO5103) – Funded by the European Union – NextGenerationEU.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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