ISOPRENYLATION MEDIATES DIRECT PROTEIN-PROTEIN INTERACTIONS BETWEEN HEPATITIS LARGE DELTA-ANTIGEN AND HEPATITIS-B VIRUS SURFACE-ANTIGEN

被引:106
作者
HWANG, SB
LAI, MMC
机构
[1] UNIV SO CALIF,SCH MED,HOWARD HUGHES MED INST,LOS ANGELES,CA 90033
[2] UNIV SO CALIF,SCH MED,DEPT MICROBIOL,LOS ANGELES,CA 90033
关键词
D O I
10.1128/JVI.67.12.7659-7662.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Hepatitis delta antigen (HDAg) consists of two protein species of 195 and 214 amino acids, respectively, which are identical in sequence except that the large HDAg has additional 19 amino acids at its C terminus and is prenylated. Previous studies have shown that the large HDAg and the surface antigen of hepatitis B virus (HBsAg) together can form empty hepatitis delta virus (HDV) particles. To understand the molecular mechanism of HDV virion morphogenesis, we investigated the possible direct protein-protein interaction between HDAg and HBsAg. We constructed recombinant baculoviruses expressing the major form of HBsAg and various mutant HDAgs and used these proteins for far-Western protein binding assays. We demonstrated that HBsAg interacted specifically with the large HDAg but not with the small HDAg. Using mutant HDAgs which have defective or aberrant prenylation, we showed that this interaction required isoprenylates on the cysteine residue of the C terminus of the large HDAg. Isoprenylation alone, without the remainder of the C-terminal amino acids of the large HDAg, was insufficient to mediate interaction with HBsAg. This study demonstrates a novel role of prenylates in HDV virion assembly.
引用
收藏
页码:7659 / 7662
页数:4
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