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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
Language English Country Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2005 to 1 year ago
Medline Complete (EBSCOhost)
from 2005-01-01 to 1 year ago
Wiley Free Content
from 2005 to 1 year ago
PubMed
34839586
DOI
10.1111/febs.16304
Knihovny.cz E-resources
- MeSH
- Cysteine metabolism MeSH
- Endoplasmic Reticulum metabolism MeSH
- Hepatitis B e Antigens * metabolism MeSH
- Hepatitis B * metabolism MeSH
- Humans MeSH
- Membrane Glycoproteins MeSH
- Protein Sorting Signals genetics MeSH
- Calcium-Binding Proteins MeSH
- Receptors, Cytoplasmic and Nuclear MeSH
- Receptors, Peptide MeSH
- Hepatitis B virus metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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.
References provided by Crossref.org
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