IDENTIFICATION OF A PRENYLATION SITE IN DELTA-VIRUS LARGE ANTIGEN

被引：250

作者：

GLENN, JS ^{[1
]}

WATSON, JA ^{[1
]}

HAVEL, CM ^{[1
]}

WHITE, JM ^{[1
]}

机构：

[1] UNIV CALIF SAN FRANCISCO, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA

来源：

SCIENCE | 1992年 / 256卷 / 5061期

关键词：

D O I：

10.1126/science.1598578

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 carboxyl 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.

引用

页码：1331 / 1333

页数：3

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