Document Detail


Large hepatitis delta antigen in packaging and replication inhibition: role of the carboxyl-terminal 19 amino acids and amino-terminal sequences.
MedLine Citation:
PMID:  7636976     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hepatitis delta virus (HDV) encodes two proteins, the small delta antigen (SHDAg) and large delta antigen (LHDAg). The latter is identical to the former except for the presence of additional 19 amino acids at the C terminus. While SHDAg is required for HDV replication, LHDAg inhibits replication and, together with hepatitis B surface antigen (HBsAg), is required for the assembly of HDV. The last 19 C-terminal amino acids of LHDAg are essential for HDV assembly. Most of LHDAg (amino acids 19 to 146 and 163 to 195) had been shown to be dispensable for packaging with HBsAg. To discern whether the last 19 C-terminal amino acids solely constitute the signal for packaging with HBsAg, we constructed two LHDAg deletion mutants and tested their abilities to be packaged with HBsAg in cotransfection experiments. We found that deletion of amino acids 2 to 21 and 142 to 165 did not affect LHDAg packaging. This result suggested that only the last 19 C-terminal amino acids of LHDAg are required for packaging. We further constructed two plasmids which expressed c-H-ras with or without additional 19 C-terminal amino acids identical to those in LHDAg. Only c-H-ras with additional 19 amino acids could be cosecreted with HBsAg in the cotransfection experiment. This result confirmed that the C-terminal 19 amino acids are the packaging signal for HBsAg. We also tested the trans activation activity and trans-dominant inhibitory activity of the deletion mutants of SHDAg and LHDAg, respectively. In contrast to deletion of amino acids 142 to 165, deletion of amino acids 2 to 21 impaired the trans-dominant inhibitory activity of LHDAg. Deletion of amino acids 2 to 21 and 142 to 165 did not affect the trans activation activity of SHDAg. This result suggested that a functional domain which is important for the trans-dominant inhibitory activity of LHDAg exists in the amino terminus of HDAg.
Authors:
C Z Lee; P J Chen; D S Chen
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of virology     Volume:  69     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1995 Sep 
Date Detail:
Created Date:  1995-09-14     Completed Date:  1995-09-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5332-6     Citation Subset:  IM    
Affiliation:
Department of Internal Medicine, University Hospital, National Taiwan University, Taipei.
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MeSH Terms
Descriptor/Qualifier:
Antigens, Viral / biosynthesis,  isolation & purification,  metabolism*
Carcinoma, Hepatocellular
Cell Line
Hepatitis B Surface Antigens / metabolism
Hepatitis Delta Virus / physiology*
Hepatitis delta Antigens
Humans
Immunoblotting
Liver Neoplasms
Mutagenesis
RNA, Viral / metabolism
Recombinant Proteins / biosynthesis,  isolation & purification,  metabolism
Sequence Deletion*
Transcriptional Activation
Transfection
Virus Replication*
Chemical
Reg. No./Substance:
0/Antigens, Viral; 0/Hepatitis B Surface Antigens; 0/Hepatitis delta Antigens; 0/RNA, Viral; 0/Recombinant Proteins; 0/hepatitis delta virus large antigen
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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