真核生物起始因子4GI是HIV-1蛋白酶的不良底物。

Eukaryotic initiation factor 4GI is a poor substrate for HIV-1 proteinase.

作者信息

Schlick Petra, Skern Tim

机构信息

Institute for Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria.

出版信息

FEBS Lett. 2002 Oct 9;529(2-3):337-40. doi: 10.1016/s0014-5793(02)03415-4.

DOI:10.1016/s0014-5793(02)03415-4

PMID:12372624

Abstract

Eukaryotic initiation factor (eIF) 4GI is efficiently cleaved during picornaviral replication. eIF4GI processing has also recently been observed during HIV-1 replication. We have compared the efficiency of eIF4GI proteolysis in rabbit reticulocyte lysates during translation of mRNAs encoding the foot-and-mouth disease virus leader proteinase (L(pro)) or the HIV-1 proteinase (HIV-1(pro)). L(pro) cleaved 50% eIF4GI within 12 min whereas HIV-1(pro) required 4 h; the concentrations were 2 pg/microl (0.1 nM) for L(pro) and 60 pg/microl (2.66 nM) for HIV-1(pro). HIV-1(pro) processing of eIF4GI is therefore not quantitatively analogous to that of L(pro), suggesting that the primary function of eIF4GI cleavage in HIV-1 replication may not be protein synthesis inhibition.

摘要

真核生物起始因子（eIF）4GI在小核糖核酸病毒复制过程中被有效切割。最近在HIV-1复制过程中也观察到了eIF4GI的加工处理。我们比较了在编码口蹄疫病毒前导蛋白酶（L(pro)）或HIV-1蛋白酶（HIV-1(pro)）的mRNA翻译过程中，兔网织红细胞裂解物中eIF4GI蛋白水解的效率。L(pro)在12分钟内切割了50%的eIF4GI，而HIV-1(pro)则需要4小时；L(pro)的浓度为2 pg/μl（0.1 nM），HIV-1(pro)的浓度为60 pg/μl（2.66 nM）。因此，HIV-1(pro)对eIF4GI的加工处理在数量上与L(pro)不同，这表明在HIV-1复制过程中eIF4GI切割的主要功能可能不是抑制蛋白质合成。