https://scholars.lib.ntu.edu.tw/handle/123456789/568797
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Mu J.-J. | en_US |
dc.contributor.author | Chen D.-S. | en_US |
dc.contributor.author | PEI-JER CHEN | en_US |
dc.date.accessioned | 2021-07-03T03:35:52Z | - |
dc.date.available | 2021-07-03T03:35:52Z | - |
dc.date.issued | 2001 | - |
dc.identifier.issn | 0022-538X | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84983719356&doi=10.1128%2fJVI.75.19.9087-9095.2001&partnerID=40&md5=b41d10f0040574d7cf7b15f7a00b6f1e | - |
dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/568797 | - |
dc.description.abstract | Hepatitis delta virus (HDV) small delta antigen (S-HDAg) plays a critical role in virus replication. We previously demonstrated that the S-HDAg phosphorylation occurs on both serine and threonine residues. However, their biological significance and the exact phosphorylation sites of S-HDAg are still unknown. In this study, phosphorylated S-HDAg was detected only in the intracellular compartment, not in viral particles. In addition, the number of phosphorylated isoforms of S-HDAg significantly increased with the extent of viral replication in transfection system. Site-directed mutagenesis showed that alanine replacement of serine 177, which is conserved among all the known HDV strains, resulted in reduced phosphorylation of S-HDAg, while the mutation of the other two conserved serine residues (2 and 123) had little effect. The S177A mutant dramatically decreased its capability in assisting HDV RNA replication, with a preferential and profound impairment of the antigenomic RNA replication. Furthermore, the viral RNA editing, a step relying upon antigenomic RNA replication, was also abolished by this mutation. These results suggested that phosphorylation of S-HDAg, with serine 177 as a presumable site, plays a critical role in viral RNA replication, especially in augmenting the replication of antigenomic RNA. | - |
dc.publisher | American Society for Microbiology | - |
dc.relation.ispartof | Journal of Virology | - |
dc.subject.classification | [SDGs]SDG3 | - |
dc.subject.other | virus RNA; amino acid substitution; article; DNA transfection; Hepatitis delta virus; immunoprecipitation; nonhuman; Northern blotting; phosphorylation; polyacrylamide gel electrophoresis; priority journal; reverse transcription polymerase chain reaction; RNA editing; RNA replication; site directed mutagenesis; virus mutation; Western blotting | - |
dc.title | The conserved serine 177 in the delta antigen of hepatitis delta virus is one putative phosphorylation site and is required for efficient viral RNA replication | en_US |
dc.type | journal article | en |
dc.identifier.doi | 10.1128/JVI.75.19.9087-9095.2001 | - |
dc.identifier.pmid | 11533172 | - |
dc.identifier.scopus | 2-s2.0-84983719356 | - |
dc.relation.pages | 9087-9095 | - |
dc.relation.journalvolume | 75 | - |
dc.relation.journalissue | 19 | - |
item.fulltext | no fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.cerifentitytype | Publications | - |
item.openairetype | journal article | - |
item.grantfulltext | none | - |
crisitem.author.dept | Clinical Medicine | - |
crisitem.author.orcid | 0000-0001-8316-3785 | - |
crisitem.author.parentorg | College of Medicine | - |
顯示於: | 臨床醫學研究所 |
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