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蛋白激酶CK2使一种神经毒性猿猴免疫缺陷病毒的Nef蛋白发生磷酸化。

Protein kinase CK2 phosphorylates the Nef protein from a neurovirulent simian immunodeficiency virus.

作者信息

Caples Matthew J, Clements Janice E, Barber Sheila A

机构信息

Department of Comparative Medicine, Johns Hopkins University School of Medicine, 733 N. Broadway St., Broadway Research Building 831, Baltimore, MD 21205, USA.

出版信息

Virology. 2006 Apr 25;348(1):156-64. doi: 10.1016/j.virol.2005.12.028. Epub 2006 Jan 31.

Abstract

The Nef protein of Human Immunodeficiency Virus (HIV) and Simian Immunodeficiency Virus (SIV) is a pluripotent accessory protein that plays a critical role in disease progression. One analogous characteristic of Nef proteins from SIV and HIV is the ability to associate with cellular kinases. We have previously reported that the Nef protein from a macrophage-tropic neurovirulent SIV clone, SIV/17E-Fr, is associated with an unknown kinase activity that is distinct from the p21-associated kinase that interacts with SIVmac239 Nef. Using site-directed mutagenesis and kinase-specific inhibitors, we have identified this kinase as the ubiquitous serine/threonine kinase, protein kinase CK2.

摘要

人类免疫缺陷病毒(HIV)和猿猴免疫缺陷病毒(SIV)的Nef蛋白是一种多能辅助蛋白,在疾病进展中起关键作用。SIV和HIV的Nef蛋白的一个类似特征是能够与细胞激酶结合。我们之前报道过,来自巨噬细胞嗜性神经毒性SIV克隆SIV/17E-Fr的Nef蛋白与一种未知的激酶活性相关,该活性不同于与SIVmac239 Nef相互作用的p21相关激酶。通过定点诱变和激酶特异性抑制剂,我们已将这种激酶鉴定为普遍存在的丝氨酸/苏氨酸激酶,即蛋白激酶CK2。

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