Abstract:
:A unique feature of the large hepadnavirus envelope protein (L) is its mixed transmembrane topology, resulting from partial posttranslational translocation of the pre-S domain. Using protease protection analysis, we demonstrate for duck hepatitis B virus an essential role for the small envelope protein (S) in this process, providing the first experimental evidence for an S translocation channel. Further analysis revealed that the presumed cytoplasmic loop between TM1 and TM2 in the C-terminal S domain is membrane embedded and protrudes to the particle surface. These data suggest that some L molecules form a highly folded, potentially spring-loaded topology with five membrane-spanning regions and a membrane-traversing pre-S chain.
journal_name
J Viroljournal_title
Journal of virologyauthors
Grgacic EV,Kuhn C,Schaller Hdoi
10.1128/jvi.74.5.2455-2458.2000subject
Has Abstractpub_date
2000-03-01 00:00:00pages
2455-8issue
5eissn
0022-538Xissn
1098-5514journal_volume
74pub_type
杂志文章abstract::The DNase/alkaline exonuclease (AE) genes are well conserved in all herpesvirus families, but recent studies have shown that the AE proteins of gammaherpesviruses such as Epstein-Barr virus (EBV) and Kaposi's sarcoma-associated herpesvirus (KSHV) exhibit an additional function which shuts down host protein synthesis. ...
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pub_type: 临床试验,杂志文章
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