TARGETING OF CHROLAMPHENICOL ACETYLTRANSFERASE TO HUMAN-IMMUNODEFICIENCY-VIRUS PARTICLES VIA VPR AND VPX

TARGETING OF CHROLAMPHENICOL ACETYLTRANSFERASE TO HUMAN-IMMUNODEFICIENCY-VIRUS PARTICLES VIA VPR AND VPX
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DOI:
10.1111/j.1348-0421.1995.tb03293.x
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发表时间:
1995-01-01
影响因子:
2.6
通讯作者:
FUJIWARA, T
FUJIWARA, T
中科院分区:
医学4区
文献类型:
--
作者:
SATO, A;ISAKA, Y;FUJIWARA, T

文献摘要

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Vpr和Vpx是人类免疫缺陷病毒(HIV)选择性整合到成熟病毒颗粒中的辅助蛋白,我们发现融合到HIV-1 Vpr、HIV-2 Vpr或HIV-2 Vpx N端的细菌氯霉素乙酰转移酶(CAT)以类型选择性方式整合到成熟病毒颗粒中,通过使用HIV-I Vpr和HIV-2 Vpx之间的嵌合蛋白,我们发现这些蛋白的N端侧HIV-1 Vpr的C端富含精氨酸的区域也被发现将CAT融合蛋白转运到病毒体中,但没有任何类型选择性,此外,HIV-2 Vpr和HIV-2 Vpx的相应区域没有这种活性,HIV-1 Vpr的这个区域可能与病毒基因组RNA非特异性相互作用,总的来说,Vpr和Vpx可能提供一种将外源蛋白和其他分子引入HIV病毒体的方法治疗目的。
Vpr and Vpx are the auxiliary proteins of human immunodeficiency viruses (HIVs) selectively incorporated into mature viral particles, We showed that the bacterial chloramphenicol acetyltransferase (CAT) fused to the N-terminus of HIV-1 Vpr, HIV-2 Vpr, or HIV-2 Vpx was incorporated into mature virions in a type-selective manner, By using chimeric proteins between HIV-I Vpr and HIV-2 Vpx, we found that the N-terminal side of these proteins was mainly important for type-selective virion incorporation, The C-terminal arginine-rich region of HIV-I Vpr was also found to transport CAT fusion proteins into virions but without any type selectivity, Furthermore, the corresponding regions of HIV-2 Vpr and HIV-2 Vpx had no such activity, This region of HIV-1 Vpr may interact nonspecifically with viral genomic RNA, Collectively, Vpr and Vpx may provide a means to introduce foreign proteins and other molecules into HIV virions for therapeutic purposes.