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APOBEC3G 在细胞和无细胞系统中直接结合乙型肝炎病毒核心蛋白。

APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems.

机构信息

Department of Anatomy, School of Medicine, Zhejiang University, Hangzhou 310058, PR China.

出版信息

Virus Res. 2010 Aug;151(2):213-9. doi: 10.1016/j.virusres.2010.05.009. Epub 2010 May 25.

Abstract

APOBEC3G (A3G) is an intrinsic antiretroviral factor which can inhibit Hepatitis B virus (HBV) replication. This antiviral activity mainly depends on A3G incorporation into viral particles. However, the mechanisms of A3G packaging into HBV particles have not been well characterized. In this paper, we demonstrated that A3G interacted with the HBV core protein (HBc) directly in co-transfected HepG2 cells using the fluorescence resonance energy transfer (FRET) approach. In addition, we further found that this interaction did not require other factors in vitro using surface plasmon resonance (SPR) technology on BIAcore 3000. While cellular RNA or viral RNA was added to A3G protein solution before flow through the BIAcore chip, the interaction was not affected. In conclusion, these results suggest the possibility that A3G is incorporated into HBV viral particles via direct binding with HBc protein.

摘要

APOBEC3G (A3G) 是一种内在的抗病毒因子,可抑制乙型肝炎病毒 (HBV) 的复制。这种抗病毒活性主要依赖于 A3G 整合到病毒颗粒中。然而,A3G 包装到 HBV 颗粒中的机制尚未得到很好的描述。在本文中,我们使用荧光共振能量转移 (FRET) 方法证明 A3G 与 HepG2 细胞中转染的乙型肝炎核心蛋白 (HBc) 直接相互作用。此外,我们还进一步发现,使用 BIAcore 3000 上的表面等离子体共振 (SPR) 技术,在体外这种相互作用不需要其他因素。当细胞 RNA 或病毒 RNA 在 A3G 蛋白溶液流过 BIAcore 芯片之前添加时,相互作用不受影响。总之,这些结果表明 A3G 可能通过与 HBc 蛋白直接结合而被整合到 HBV 病毒颗粒中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b70c/7173111/dc0fcec4e88d/gr1.jpg

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