CEEPC/IPM/CMSC - Abstrakt prezentace

(CEEPC/IPM/CMSC 2022 - SaO-21)
Proteomic Analysis of Hepatitis B Virus

Martin Hubálek 1 *, Aleš Zábranský 1, Alena Křenková 1, Michal Korecký 1, Marta Vlková 1, Jan Weber 1, Iva Pichová 1

  1. Ústav organické chemie a biochemie AV ČR, v.v.i.


According to the World Health Organisation, an estimated 296 million people worldwide are infected with Hepatitis B virus (HBV). HBV is a small enveloped DNA virus from Hepadnaviridae family that persists in the infected hepatocytes by establishing an episomal covalently closed circular double-stranded DNA (cccDNA) genome containing four open reading frames (C, P, S and X). The ORFs largely overlap and encode multiple proteins using different in-frame start codons. The S ORF encodes three forms of surface envelope glycoproteins S-, M-, and L- HBs). The HBV preC-C gene gives rise to two different products translated from distinct mRNAs – core protein (HBc) and precore protein (HBe). Despite their high sequence similarity, these proteins exhibit different functions and subcellular localizations. The P ORF encodes viral polymerase, and the X ORF encodes regulatory HBx protein.
Mass Spectrometry department of IOCB has established a collaboration with the groups of Iva Pichova and Jan Weber from IOCB. This collaboration on proteomics experiments lead to the discovery of several important biological and biochemical findings including identification of interacting partners of HBc, HBx and HBe proteins or posttranslational modifications of HBc protein. The collaboration resulted in several publications. The proteomic analysis of individually expressed viral proteins has also captured out-of-frame products suggesting the possibility of frameshift or alternative internal initiation of translation. The presentation will highlight the proteomic analyses of HBV at IOCB

* Korespondující autor: hubalek@uochb.cas.cz


  1. Zábranská H, et al; Biogenesis of hepatitis B virus e antigen is driven by translocon-associated protein complex and regulated by conserved cysteine residues within its signal peptide sequence. FEBS J. 2022 May; 289(10):2895-2914. doi: 10.1111/febs.163
  2. Langerová H, et al; Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination. Cells. 2020 Nov 26; 9(12):2547. doi: 10.3390/cells9122547. 3. Ramakrishnan D, et al; Hepatitis B Virus X Protein Function Requires Zinc Bi
  3. Ramakrishnan D, et al; Hepatitis B Virus X Protein Function Requires Zinc Binding. J Virol. 2019 Jul 30; 93(16):e00250-19. doi: 10.1128/JVI.00250-19.

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