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2
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Interaction of human immunodeficiency virus type 1 Vif with Gag and Gag-Pol precursors: co-encapsidation and interference with viral protease-mediated Gag processing.1型人类免疫缺陷病毒Vif与Gag和Gag-Pol前体的相互作用：共包装及对病毒蛋白酶介导的Gag加工的干扰
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Inhibition of human and simian immunodeficiency virus protease function by targeting Vpx-protease-mutant fusion protein into viral particles.通过将Vpx-蛋白酶突变体融合蛋白靶向病毒颗粒来抑制人类和猿猴免疫缺陷病毒蛋白酶功能。
J Virol. 1996 Jun;70(6):3378-84. doi: 10.1128/JVI.70.6.3378-3384.1996.

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Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.1型人类免疫缺陷病毒（HIV-1）的Gag-Pro-Pol前体中的加工位点被病毒蛋白酶以不同速率切割。
Retrovirology. 2005 Nov 1;2:66. doi: 10.1186/1742-4690-2-66.
7
Human immunodeficiency virus (HIV) type 1 transframe protein can restore activity to a dimerization-deficient HIV protease variant.1型人类免疫缺陷病毒（HIV）移码蛋白可恢复二聚化缺陷型HIV蛋白酶变体的活性。
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The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.蛋白酶和额外蛋白酶结构域的二聚体界面影响蛋白酶的激活以及GagPol裂解的特异性。
J Virol. 2003 Jan;77(1):366-74. doi: 10.1128/jvi.77.1.366-374.2003.
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Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.间隔肽p1内的脯氨酸残基对1型人类免疫缺陷病毒的感染性、蛋白质加工及基因组RNA二聚体稳定性至关重要。
J Virol. 2002 Nov;76(22):11245-53. doi: 10.1128/jvi.76.22.11245-11253.2002.
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Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.从紧邻N端的p6*蛋白上切割出1型人类免疫缺陷病毒蛋白酶，对于高效的Gag多聚蛋白加工和病毒感染性至关重要。
J Virol. 1998 Apr;72(4):3459-63. doi: 10.1128/JVI.72.4.3459-3463.1998.

本文引用的文献

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Avian sarcoma leukemia virus protease linked to the adjacent Gag polyprotein is enzymatically active.
Virology. 1995 Dec 20;214(2):439-44. doi: 10.1006/viro.1995.0054.
2
Modelling, synthesis and biological activity of a BLV proteinase, made of (only) 116 amino acids.一种仅由116个氨基酸组成的牛白血病病毒蛋白酶的建模、合成及生物活性
FEBS Lett. 1993 Jul 12;326(1-3):237-40. doi: 10.1016/0014-5793(93)81798-5.
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Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection: evidence for a role of protease in the early phase.1型人类免疫缺陷病毒蛋白酶抑制剂在单次感染周期中的抗病毒活性：蛋白酶在早期阶段作用的证据
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4
Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.来自一种在蛋白酶（PR）结构域N端带有阻断突变的前体的新型人类免疫缺陷病毒1型蛋白酶蛋白的蛋白水解活性。
J Virol. 1994 Jan;68(1):240-50. doi: 10.1128/JVI.68.1.240-250.1994.
5
Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing.人类免疫缺陷病毒1型Gag-Pol蛋白酶（PR）上游的结构域影响PR的自身加工。
J Virol. 1995 Jun;69(6):3878-84. doi: 10.1128/JVI.69.6.3878-3884.1995.
6
Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor.在大肠杆菌中表达的人类免疫缺陷病毒蛋白酶表现出gag前体的自身加工和特异性成熟。
Proc Natl Acad Sci U S A. 1987 Dec;84(24):8903-6. doi: 10.1073/pnas.84.24.8903.
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Active human immunodeficiency virus protease is required for viral infectivity.活跃的人类免疫缺陷病毒蛋白酶是病毒感染性所必需的。
Proc Natl Acad Sci U S A. 1988 Jul;85(13):4686-90. doi: 10.1073/pnas.85.13.4686.
8
An 11-kDa form of human immunodeficiency virus protease expressed in Escherichia coli is sufficient for enzymatic activity.在大肠杆菌中表达的一种11千道尔顿形式的人类免疫缺陷病毒蛋白酶就足以具备酶活性。
Proc Natl Acad Sci U S A. 1988 Apr;85(8):2449-53. doi: 10.1073/pnas.85.8.2449.
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Genetic locus, primary structure, and chemical synthesis of human immunodeficiency virus protease.
Gene Anal Tech. 1988 Nov-Dec;5(6):109-15. doi: 10.1016/0735-0651(88)90010-6.
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Viral proteinases.病毒蛋白酶
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p6聚合酶-蛋白酶融合蛋白存在于1型人类免疫缺陷病毒的成熟颗粒中。

A p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.

作者信息

Almog N, Roller R, Arad G, Passi-Even L, Wainberg M A, Kotler M

机构信息

Department of Molecular Genetics, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.

出版信息

J Virol. 1996 Oct;70(10):7228-32. doi: 10.1128/JVI.70.10.7228-7232.1996.

DOI:10.1128/JVI.70.10.7228-7232.1996
PMID:8794372
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC190778/
Abstract

Human immunodeficiency virus type 1 (HIV-1) protease (PR) and p6(Pol) are translated as part of the Gag-Pol polyprotein after a ribosomal frameshift. PR is essential to virus replication and is responsible for cleaving Gag and Gag-Pol precursors, but the role of p6(Pol) in HIV-1 infection is poorly understood. Here, we report that (i) PR is present in mature HIV-1 virions primarily as a p6(Pol)-PR fusion protein; (ii) HIV-1 PR cleaves viral precursor proteins expressed in bacterial cells at the Phe-Leu bond (positions 1639 to 1642) located at the junction of the NC and p6(Pol) proteins, releasing the p6(Pol)-PR fusion protein; and (iii) purified p6(Pol)-PR fusion protein undergoes autocleavage in vitro at at least three sites.

摘要

1型人类免疫缺陷病毒（HIV-1）蛋白酶（PR）和p6（Pol）在核糖体移码后作为Gag-Pol多聚蛋白的一部分被翻译。PR对病毒复制至关重要，负责切割Gag和Gag-Pol前体，但p6（Pol）在HIV-1感染中的作用尚不清楚。在此，我们报告：（i）PR主要以p6（Pol）-PR融合蛋白的形式存在于成熟HIV-1病毒颗粒中；（ii）HIV-1 PR在位于NC和p6（Pol）蛋白交界处的苯丙氨酸-亮氨酸键（第1639至1642位）处切割细菌细胞中表达的病毒前体蛋白，释放p6（Pol）-PR融合蛋白；（iii）纯化的p6（Pol）-PR融合蛋白在体外至少在三个位点进行自切割。