Suppr超能文献

弗林蛋白酶和PC1转化酶均可将人类免疫缺陷病毒(HIV)-1包膜糖蛋白gp160切割成gp120(HIV-1 SU)和gp41(HIV-1 TM)。

The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM).

作者信息

Decroly E, Vandenbranden M, Ruysschaert J M, Cogniaux J, Jacob G S, Howard S C, Marshall G, Kompelli A, Basak A, Jean F

机构信息

Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université libre de Bruxelles, Belgium.

出版信息

J Biol Chem. 1994 Apr 22;269(16):12240-7.

PMID:8163529
Abstract

Intracellular proteolytic processing of human immunodeficiency virus envelope glycoprotein precursor (gp160) is an essential step for virus infectivity. Northern blot analysis provided evidence that furin and PC1, but not PC2, are expressed in the CD4+ human lymphoblastoid H9 cell line, suggesting the possible participation of these convertases in human immunodeficiency virus (HIV) gp160 proteolytic processing. Purified PC1 and furin cleaved specifically in vitro gp160 into gp120 (HIV-I SU) and gp41 (HIV-I TM). NH2-terminal sequence analysis of the produced gp41 (HIV-I TM) demonstrated that the cleavage occurred within the sequence Arg-Glu-Lys-Arg decreases Ala-Val-Gly-Ile, which is identical to the bond cleaved in vivo. Transition state analog peptides were designed and tested in vitro for their ability to inhibit the PC1- or furin-mediated gp160 cleavage. The best inhibitor was decanoyl-Arg-Lys-Arg-Arg-psi [CH2NH]-Phe-Leu-Gly-Phe-NH2.

摘要

人类免疫缺陷病毒包膜糖蛋白前体(gp160)的细胞内蛋白水解加工是病毒感染性的关键步骤。Northern印迹分析表明,弗林蛋白酶和PC1在CD4 +人淋巴母细胞H9细胞系中表达,而PC2不表达,这表明这些转化酶可能参与人类免疫缺陷病毒(HIV)gp160的蛋白水解加工。纯化的PC1和弗林蛋白酶在体外可将gp160特异性切割成gp120(HIV-1 SU)和gp41(HIV-1 TM)。对产生的gp41(HIV-1 TM)进行的氨基末端序列分析表明,切割发生在序列Arg-Glu-Lys-Arg↓Ala-Val-Gly-Ile内,这与体内切割的位点相同。设计了过渡态类似物肽并在体外测试其抑制PC1或弗林蛋白酶介导的gp160切割的能力。最佳抑制剂是癸酰基-Arg-Lys-Arg-Arg-ψ[CH2NH]-Phe-Leu-Gly-Phe-NH2。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验