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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
H. Zábranská, A. Zábranský, B. Lubyová, J. Hodek, A. Křenková, M. Hubálek, J. Weber, I. Pichová
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2005 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2005-01-01 do Před 1 rokem
Wiley Free Content
od 2005 do Před 1 rokem
PubMed
34839586
DOI
10.1111/febs.16304
Knihovny.cz E-zdroje
- MeSH
- cystein metabolismus MeSH
- endoplazmatické retikulum metabolismus MeSH
- hepatitida B - antigeny e * metabolismus MeSH
- hepatitida B * metabolismus MeSH
- lidé MeSH
- membránové glykoproteiny MeSH
- proteiny - lokalizační signály genetika MeSH
- proteiny vázající vápník MeSH
- receptory cytoplazmatické a nukleární MeSH
- receptory peptidů MeSH
- virus hepatitidy B metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Hepatitis B virus uses e antigen (HBe), which is dispensable for virus infectivity, to modulate host immune responses and achieve viral persistence in human hepatocytes. The HBe precursor (p25) is directed to the endoplasmic reticulum (ER), where cleavage of the signal peptide (sp) gives rise to the first processing product, p22. P22 can be retro-translocated back to the cytosol or enter the secretory pathway and undergo a second cleavage event, resulting in secreted p17 (HBe). Here, we report that translocation of p25 to the ER is promoted by translocon-associated protein complex. We have found that p25 is not completely translocated into the ER; a fraction of p25 is phosphorylated and remains in the cytoplasm and nucleus. Within the p25 sp sequence, we have identified three cysteine residues that control the efficiency of sp cleavage and contribute to proper subcellular distribution of the precore pool.
Citace poskytuje Crossref.org
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