Publication Date:
1992-05-29
Description:
During replication, hepatitis delta virus (HDV) switches from production of small to large delta antigen. Both antigen isoforms have an HDV genome binding domain and are packaged into hepatitis B virus (HBV)-derived envelopes but differ at their carboxy termini. The large antigen was shown to contain a terminal CXXX box and undergo prenylation. The large, but not the small, antigen formed secreted particles when expressed singly with HBV surface antigen. Mutation of Cys211 in the CXXX box of the large antigen abolished both prenylation and particle formation, suggesting that this site is important for virion morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glenn, J S -- Watson, J A -- Havel, C M -- White, J M -- New York, N.Y. -- Science. 1992 May 29;256(5061):1331-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143-0450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598578" target="_blank"〉PubMed〈/a〉
Keywords:
3T3 Cells
;
Amino Acid Sequence
;
Animals
;
Antigens, Viral/genetics/isolation & purification/*metabolism
;
Cell Line
;
Cysteine
;
Hepatitis Delta Virus/genetics/metabolism/*physiology
;
Hepatitis delta Antigens
;
Mevalonic Acid/*metabolism
;
Mice
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
Proline/metabolism
;
Protein Biosynthesis
;
RNA, Messenger/metabolism
;
Rabbits
;
Reticulocytes/metabolism
;
Serine
;
Transfection
;
Virus Replication
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
