scholarly journals Hepatitis B virus p25 precore protein accumulates in Xenopus oocytes as an untranslocated phosphoprotein with an uncleaved signal peptide.

1992 ◽  
Vol 66 (1) ◽  
pp. 37-45 ◽  
Author(s):  
S Q Yang ◽  
M Walter ◽  
D N Standring
2021 ◽  
Author(s):  
Helena Zábranská ◽  
Aleš Zábranský ◽  
Barbora Lubyová ◽  
Jan Hodek ◽  
Alena Křenková ◽  
...  

Hepatitis B virus (HBV) 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 (TRAP). We 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 identified three cysteine residues that control the efficiency of sp cleavage and contribute to proper subcellular distribution of the precore pool.


2001 ◽  
Vol 120 (5) ◽  
pp. A64-A64
Author(s):  
R CHEN ◽  
P DESMOND ◽  
W DELANEY ◽  
D COLLEDGE ◽  
R EDWARDS ◽  
...  

2003 ◽  
Vol 38 (1) ◽  
pp. 95-101 ◽  
Author(s):  
Lee C.-M. ◽  
Chen C.-H. ◽  
Lu S.-N. ◽  
Tung H.-D. ◽  
Chou W.-J. ◽  
...  

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